Cell junction organization (Homo sapiens)

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162, 29, 33627151634164, 2219103142891712, 213223, 25303, 1912, 2116271188165, 2620, 3135328137, 11cytosolcytosolLAMA3 CADM3 PVRL3 CDH4 CLDN12 ITGB1 LIMS1 Nectin-1:Nectin-4trans heterodimerCADM3 PXN CDH7 Par3:Par6:aPKCcomplexCadherin:CatenincomplexITGB4 CDH9 PARVBARHGEF6 CLDN11 CDH12 CRB3:PALS1:PATJcomplexTESK1ITGB4 PARVAINADL PVRL2 LAMC2 SDK2 CLDN3 CLDN14 PARVA CDH9 claudintrans-homodimerPVRL4 PARVA:TESK1CDH8 Rsu-1:Pinch1 complexNectin-2:PVRL3transheterodimerITGA6(24-1130) PARVB CLDN10 PVR CDH10 Nectin-3:Necl-2trans heterodimerCDH8 PVRL1 PVRL1 PVRL3 CDH12 PVRL1 CLDN7 Afadin:F-actinPVRL3 FLNA VE-cadherin CDH2 JUP CDH4 PARVB PVRL3 Necl-1:Nectin-1trans heterodimerILK CDH18 PVRL4 CLDN17 FLNC Necl-1/Necl-2/Necl-3trans homodimerCLDN10 CADM3 CDH18 PVRL1CDH17 ARHGEF6DST COL17A1(1-1497) PVRL2 CADM3 DST CDH1(155-882) CTNND1VASPCDH10 ILKCLDN15 CADM2 ITGB1ITGA6(24-1130) Migfilin:FilaminA:F-actinJUP CADM1CLDN18 Keratin 5/14Integrinalpha6:beta4:Plectin:BP180 complexFilaminPLEC LAMC2 JAM-A:PAR-aPKCcomplexLAMC2 PINCH-ILK-parvincomplexCLDN4 CLDN3 CTNNA1CLDN19 CDH7 CD151CDH2 CTNNA1 PARVA:PaxillinCLDN6 CTNND1 CDH6 LAMA3 CDH9 PVRL4 PVRL3 PVRL1 CDH24 CLDN9 INADLNectin-1:PVRL3 transheterodimerNecl-1:Necl-2 transheterodimerSDK2SDK1(?-2213) LAMB3 LAMA3 MIGFILIN:VASPCLDN2 Integrin alpha6beta4CDH11 CDH17 LAMA3 CDH6 COL17A1(1-1497) MLLT4-2PVRL2 CLDN6 F11R CDH11 COL17A1(1-1497) VE-cadherin PLEC CADM1 SDK1(?-2213)MLLT4-2 ANG Trans-homophilicSDK1 dimerCLDN23 LIMS1 CLDN7 LAMB3 PXNITGA6(24-1130) PARD6A VE-cadherin CLDN5 CDH13 ACTN1CLDN9 CDH2 PLEC Integrinalpha6:beta4:Plectin:BP180:Laminin-322 complexLIMS2 PVRL2 PRKCI CLDN16 ITGA6(24-1130) RSU1PLEC CADM3CDH3 CRB3 Nectin-2 cishomodimerACTN1 CLDN20 ILK:Integrin beta-1PVRL1 beta-catenin PVRL4 PVRL4 Type IIhemidesmosomePRKCI CLDN18 ITGA6(24-1130) CADM2 CLDN8 FLNA PVRF-actinPVRL3 PLECPINCHCRB3PLEC PVRL3 Ca2+PARD6B CLDN1 F11RMIG-2:MIGFILINFBLIM1 ClaudinNectin transhomodimerITGB4 F-actin Integrin alpha6:beta 4:PlectincomplexPARVB PVRL1 CDH4 CLDN19 CDH13 ITGB4 CDH7 CLDN1 PVRL1 CLDN4 CDH17 LAMB3 F-actin LAMB3 DST CLDN22 COL17A1(1-1497) Nectin:afadinPARVA Classic CadherinPRV:PVRL3 transheterodimerCADM1 CD151 Cadherintrans-homodimerNectin cis-homodimerMLLT4-2 PARVA Trans-homophilicSDK2 dimerFERMT2 CDH24 CDH18 CDH10 PLEC PVRL3 CDH1(155-882) CD151 CDH3 CDH6 PARVB:alpha actininNecl-1:Nectin-3trans heterodimerCADM1 ITGB4 LAMC2 LIMS1LAMC2 PVRL2 CLDN2 NectinPVRL3 ITGA6(24-1130) PVRL4 beta-catenin PARD3 PARD6B LAMA3 CLDN20 BP230CLDN8 Necl-1/Necl-2/Necl-3homodimerCDH15 CDH1(155-882) F-actin:ANGPARVB RSU1 CLDN15 CDH11 ANGPARD6G CLDN14 Keratin 5/14 LAMB3 CDH15 FBLIM1CADM1 FBLIM1 PARD3 COL17A1(1-1497) PARD6A FERMT2CLDN17 PVRL3 dimerCLDN5 PVRL2 PVRL3 DST F-actinMPP5CLDN16 F-actin CLDN23 CDH15 CDH12 CADM3 CDH3 PVRL1 CLDN11 CD151:BP230:BP180:Plectin:Integrin alpha 6 beta 4: LamininNectin-4 cishomodimerCDH13 CLDN12 TESK1 LIMS2 PARVA MPP5 ITGB4 ITGB4 LIMS1 VASP CDH24 PARD6G FBLIM1 Laminin-332alpha/beta parvinILK COL17A1(1-1497)Nectin-1 cishomodimerFLNC CDH8 ITGA6(24-1130) BP230:BP180:Plectin:integrin alpha 6 beta 4:Laminin 332PVRL3CLDN22 ParvB/Affixin:Alpha-PixBeta-catenin/gammacatenin24


Cell junction organization in Reactome currently covers aspects of cell-cell junction organization, cell-extracellular matrix interactions, and Type I hemidesmosome assembly. View original pathway at Reactome.


Pathway is converted from Reactome ID: 446728
Reactome version: 74

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Ontology Terms



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  1. Tu Y, Huang Y, Zhang Y, Hua Y, Wu C.; ''A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading.''; PubMed Europe PMC Scholia
  2. Dong X, Xu F, Gong Y, Gao J, Lin P, Chen T, Peng Y, Qiang B, Yuan J, Peng X, Rao Z.; ''Crystal structure of the V domain of human Nectin-like molecule-1/Syncam3/Tsll1/Igsf4b, a neural tissue-specific immunoglobulin-like cell-cell adhesion molecule.''; PubMed Europe PMC Scholia
  3. Takahashi K, Nakanishi H, Miyahara M, Mandai K, Satoh K, Satoh A, Nishioka H, Aoki J, Nomoto A, Mizoguchi A, Takai Y.; ''Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a PDZ domain-containing protein.''; PubMed Europe PMC Scholia
  4. Mishima W, Suzuki A, Yamaji S, Yoshimi R, Ueda A, Kaneko T, Tanaka J, Miwa Y, Ohno S, Ishigatsubo Y.; ''The first CH domain of affixin activates Cdc42 and Rac1 through alphaPIX, a Cdc42/Rac1-specific guanine nucleotide exchanging factor.''; PubMed Europe PMC Scholia
  5. Lemmers C, Médina E, Delgrossi MH, Michel D, Arsanto JP, Le Bivic A.; ''hINADl/PATJ, a homolog of discs lost, interacts with crumbs and localizes to tight junctions in human epithelial cells.''; PubMed Europe PMC Scholia
  6. de Pereda JM, Lillo MP, Sonnenberg A.; ''Structural basis of the interaction between integrin alpha6beta4 and plectin at the hemidesmosomes.''; PubMed Europe PMC Scholia
  7. Dickson KA, Kang DK, Kwon YS, Kim JC, Leland PA, Kim BM, Chang SI, Raines RT.; ''Ribonuclease inhibitor regulates neovascularization by human angiogenin.''; PubMed Europe PMC Scholia
  8. Mueller S, Wimmer E.; ''Recruitment of nectin-3 to cell-cell junctions through trans-heterophilic interaction with CD155, a vitronectin and poliovirus receptor that localizes to alpha(v)beta3 integrin-containing membrane microdomains.''; PubMed Europe PMC Scholia
  9. Hopkinson SB, Jones JC.; ''The N terminus of the transmembrane protein BP180 interacts with the N-terminal domain of BP230, thereby mediating keratin cytoskeleton anchorage to the cell surface at the site of the hemidesmosome.''; PubMed Europe PMC Scholia
  10. Kakunaga S, Ikeda W, Itoh S, Deguchi-Tawarada M, Ohtsuka T, Mizoguchi A, Takai Y.; ''Nectin-like molecule-1/TSLL1/SynCAM3: a neural tissue-specific immunoglobulin-like cell-cell adhesion molecule localizing at non-junctional contact sites of presynaptic nerve terminals, axons and glia cell processes.''; PubMed Europe PMC Scholia
  11. Padhi AK, Banerjee K, Gomes J, Banerjee M.; ''Computational and functional characterization of Angiogenin mutations, and correlation with amyotrophic lateral sclerosis.''; PubMed Europe PMC Scholia
  12. Yamagata M, Weiner JA, Sanes JR.; ''Sidekicks: synaptic adhesion molecules that promote lamina-specific connectivity in the retina.''; PubMed Europe PMC Scholia
  13. Yamaji S, Suzuki A, Kanamori H, Mishima W, Yoshimi R, Takasaki H, Takabayashi M, Fujimaki K, Fujisawa S, Ohno S, Ishigatsubo Y.; ''Affixin interacts with alpha-actinin and mediates integrin signaling for reorganization of F-actin induced by initial cell-substrate interaction.''; PubMed Europe PMC Scholia
  14. Fontao L, Favre B, Riou S, Geerts D, Jaunin F, Saurat JH, Green KJ, Sonnenberg A, Borradori L.; ''Interaction of the bullous pemphigoid antigen 1 (BP230) and desmoplakin with intermediate filaments is mediated by distinct sequences within their COOH terminus.''; PubMed Europe PMC Scholia
  15. Hülsken J, Birchmeier W, Behrens J.; ''E-cadherin and APC compete for the interaction with beta-catenin and the cytoskeleton.''; PubMed Europe PMC Scholia
  16. Reymond N, Fabre S, Lecocq E, Adelaïde J, Dubreuil P, Lopez M.; ''Nectin4/PRR4, a new afadin-associated member of the nectin family that trans-interacts with nectin1/PRR1 through V domain interaction.''; PubMed Europe PMC Scholia
  17. Hannigan GE, Leung-Hagesteijn C, Fitz-Gibbon L, Coppolino MG, Radeva G, Filmus J, Bell JC, Dedhar S.; ''Regulation of cell adhesion and anchorage-dependent growth by a new beta 1-integrin-linked protein kinase.''; PubMed Europe PMC Scholia
  18. Dougherty GW, Jose C, Gimona M, Cutler ML.; ''The Rsu-1-PINCH1-ILK complex is regulated by Ras activation in tumor cells.''; PubMed Europe PMC Scholia
  19. Lopez M, Aoubala M, Jordier F, Isnardon D, Gomez S, Dubreuil P.; ''The human poliovirus receptor related 2 protein is a new hematopoietic/endothelial homophilic adhesion molecule.''; PubMed Europe PMC Scholia
  20. Ebnet K, Aurrand-Lions M, Kuhn A, Kiefer F, Butz S, Zander K, Meyer zu Brickwedde MK, Suzuki A, Imhof BA, Vestweber D.; ''The junctional adhesion molecule (JAM) family members JAM-2 and JAM-3 associate with the cell polarity protein PAR-3: a possible role for JAMs in endothelial cell polarity.''; PubMed Europe PMC Scholia
  21. Kaufman L, Yang G, Hayashi K, Ashby JR, Huang L, Ross MJ, Klotman ME, Klotman PE.; ''The homophilic adhesion molecule sidekick-1 contributes to augmented podocyte aggregation in HIV-associated nephropathy.''; PubMed Europe PMC Scholia
  22. Rosenberger G, Jantke I, Gal A, Kutsche K.; ''Interaction of alphaPIX (ARHGEF6) with beta-parvin (PARVB) suggests an involvement of alphaPIX in integrin-mediated signaling.''; PubMed Europe PMC Scholia
  23. Wang X, Fukuda K, Byeon IJ, Velyvis A, Wu C, Gronenborn A, Qin J.; ''The structure of alpha-parvin CH2-paxillin LD1 complex reveals a novel modular recognition for focal adhesion assembly.''; PubMed Europe PMC Scholia
  24. Dantzig AH, Hoskins JA, Tabas LB, Bright S, Shepard RL, Jenkins IL, Duckworth DC, Sportsman JR, Mackensen D, Rosteck PR.; ''Association of intestinal peptide transport with a protein related to the cadherin superfamily.''; PubMed Europe PMC Scholia
  25. Lorenz S, Vakonakis I, Lowe ED, Campbell ID, Noble ME, Hoellerer MK.; ''Structural analysis of the interactions between paxillin LD motifs and alpha-parvin.''; PubMed Europe PMC Scholia
  26. Michel D, Arsanto JP, Massey-Harroche D, Béclin C, Wijnholds J, Le Bivic A.; ''PATJ connects and stabilizes apical and lateral components of tight junctions in human intestinal cells.''; PubMed Europe PMC Scholia
  27. Tu Y, Wu S, Shi X, Chen K, Wu C.; ''Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation.''; PubMed Europe PMC Scholia
  28. Ali J, Liao F, Martens E, Muller WA.; ''Vascular endothelial cadherin (VE-cadherin): cloning and role in endothelial cell-cell adhesion.''; PubMed Europe PMC Scholia
  29. Masuda M, Yageta M, Fukuhara H, Kuramochi M, Maruyama T, Nomoto A, Murakami Y.; ''The tumor suppressor protein TSLC1 is involved in cell-cell adhesion.''; PubMed Europe PMC Scholia
  30. LaLonde DP, Brown MC, Bouverat BP, Turner CE.; ''Actopaxin interacts with TESK1 to regulate cell spreading on fibronectin.''; PubMed Europe PMC Scholia
  31. Ebnet K, Suzuki A, Horikoshi Y, Hirose T, Meyer Zu Brickwedde MK, Ohno S, Vestweber D.; ''The cell polarity protein ASIP/PAR-3 directly associates with junctional adhesion molecule (JAM).''; PubMed Europe PMC Scholia
  32. Koster J, Geerts D, Favre B, Borradori L, Sonnenberg A.; ''Analysis of the interactions between BP180, BP230, plectin and the integrin alpha6beta4 important for hemidesmosome assembly.''; PubMed Europe PMC Scholia
  33. Pellissier F, Gerber A, Bauer C, Ballivet M, Ossipow V.; ''The adhesion molecule Necl-3/SynCAM-2 localizes to myelinated axons, binds to oligodendrocytes and promotes cell adhesion.''; PubMed Europe PMC Scholia
  34. Sterk LM, Geuijen CA, Oomen LC, Calafat J, Janssen H, Sonnenberg A.; ''The tetraspan molecule CD151, a novel constituent of hemidesmosomes, associates with the integrin alpha6beta4 and may regulate the spatial organization of hemidesmosomes.''; PubMed Europe PMC Scholia
  35. Zhang Y, Tu Y, Gkretsi V, Wu C.; ''Migfilin interacts with vasodilator-stimulated phosphoprotein (VASP) and regulates VASP localization to cell-matrix adhesions and migration.''; PubMed Europe PMC Scholia


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113167view11:23, 2 November 2020ReactomeTeamReactome version 74
112395view15:33, 9 October 2020ReactomeTeamReactome version 73
101299view11:18, 1 November 2018ReactomeTeamreactome version 66
100836view20:49, 31 October 2018ReactomeTeamreactome version 65
100377view19:24, 31 October 2018ReactomeTeamreactome version 64
99924view16:08, 31 October 2018ReactomeTeamreactome version 63
99479view14:40, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
99133view12:40, 31 October 2018ReactomeTeamreactome version 62
94016view13:51, 16 August 2017ReactomeTeamreactome version 61
93635view11:29, 9 August 2017ReactomeTeamreactome version 61
86749view09:25, 11 July 2016ReactomeTeamreactome version 56
83402view11:08, 18 November 2015ReactomeTeamVersion54
81600view13:08, 21 August 2015ReactomeTeamVersion53
77057view08:35, 17 July 2014ReactomeTeamFixed remaining interactions
76762view12:12, 16 July 2014ReactomeTeamFixed remaining interactions
75796view11:33, 10 June 2014ReactomeTeamReactome 48 Update
75147view14:09, 8 May 2014AnweshaFixing comment source for displaying WikiPathways description
74794view08:53, 30 April 2014ReactomeTeamReactome46
44989view14:35, 6 October 2011MartijnVanIerselOntology Term : 'cell adhesion signaling pathway' added !
42016view21:50, 4 March 2011MaintBotAutomatic update
39819view05:51, 21 January 2011MaintBotNew pathway

External references


View all...
NameTypeDatabase referenceComment
ACTN1 ProteinP12814 (Uniprot-TrEMBL)
ACTN1ProteinP12814 (Uniprot-TrEMBL)
ANG ProteinP03950 (Uniprot-TrEMBL)
ANGProteinP03950 (Uniprot-TrEMBL)
ARHGEF6 ProteinQ15052 (Uniprot-TrEMBL)
ARHGEF6ProteinQ15052 (Uniprot-TrEMBL)
Afadin:F-actinComplexR-HSA-433726 (Reactome)
BP230:BP180:Plectin:integrin alpha 6 beta 4:Laminin 332ComplexR-HSA-446010 (Reactome)
BP230ComplexR-HSA-447012 (Reactome)
Beta-catenin/gamma cateninComplexR-HSA-418993 (Reactome)
CADM1 ProteinQ9BY67 (Uniprot-TrEMBL)
CADM1ProteinQ9BY67 (Uniprot-TrEMBL)
CADM2 ProteinQ8N3J6 (Uniprot-TrEMBL)
CADM3 ProteinQ8N126 (Uniprot-TrEMBL)
CADM3ProteinQ8N126 (Uniprot-TrEMBL)
CD151 ProteinP48509 (Uniprot-TrEMBL)
CD151:BP230:BP180:Plectin:Integrin alpha 6 beta 4: LamininComplexR-HSA-446066 (Reactome)
CD151ProteinP48509 (Uniprot-TrEMBL)
CDH1(155-882) ProteinP12830 (Uniprot-TrEMBL)
CDH10 ProteinQ9Y6N8 (Uniprot-TrEMBL)
CDH11 ProteinP55287 (Uniprot-TrEMBL)
CDH12 ProteinP55289 (Uniprot-TrEMBL)
CDH13 ProteinP55290 (Uniprot-TrEMBL)
CDH15 ProteinP55291 (Uniprot-TrEMBL)
CDH17 ProteinQ12864 (Uniprot-TrEMBL)
CDH18 ProteinQ13634 (Uniprot-TrEMBL)
CDH2 ProteinP19022 (Uniprot-TrEMBL)
CDH24 ProteinQ86UP0 (Uniprot-TrEMBL)
CDH3 ProteinP22223 (Uniprot-TrEMBL)
CDH4 ProteinP55283 (Uniprot-TrEMBL)
CDH6 ProteinP55285 (Uniprot-TrEMBL)
CDH7 ProteinQ9ULB5 (Uniprot-TrEMBL)
CDH8 ProteinP55286 (Uniprot-TrEMBL)
CDH9 ProteinQ9ULB4 (Uniprot-TrEMBL)
CLDN1 ProteinO95832 (Uniprot-TrEMBL)
CLDN10 ProteinP78369 (Uniprot-TrEMBL)
CLDN11 ProteinO75508 (Uniprot-TrEMBL)
CLDN12 ProteinP56749 (Uniprot-TrEMBL)
CLDN14 ProteinO95500 (Uniprot-TrEMBL)
CLDN15 ProteinP56746 (Uniprot-TrEMBL)
CLDN16 ProteinQ9Y5I7 (Uniprot-TrEMBL)
CLDN17 ProteinP56750 (Uniprot-TrEMBL)
CLDN18 ProteinP56856 (Uniprot-TrEMBL)
CLDN19 ProteinQ8N6F1 (Uniprot-TrEMBL)
CLDN2 ProteinP57739 (Uniprot-TrEMBL)
CLDN20 ProteinP56880 (Uniprot-TrEMBL)
CLDN22 ProteinQ8N7P3 (Uniprot-TrEMBL)
CLDN23 ProteinQ96B33 (Uniprot-TrEMBL)
CLDN3 ProteinO15551 (Uniprot-TrEMBL)
CLDN4 ProteinO14493 (Uniprot-TrEMBL)
CLDN5 ProteinO00501 (Uniprot-TrEMBL)
CLDN6 ProteinP56747 (Uniprot-TrEMBL)
CLDN7 ProteinO95471 (Uniprot-TrEMBL)
CLDN8 ProteinP56748 (Uniprot-TrEMBL)
CLDN9 ProteinO95484 (Uniprot-TrEMBL)
COL17A1(1-1497) ProteinQ9UMD9 (Uniprot-TrEMBL)
COL17A1(1-1497)ProteinQ9UMD9 (Uniprot-TrEMBL)
CRB3 ProteinQ9BUF7 (Uniprot-TrEMBL)
CRB3:PALS1:PATJ complexComplexR-HSA-420663 (Reactome)
CRB3ProteinQ9BUF7 (Uniprot-TrEMBL)
CTNNA1 ProteinP35221 (Uniprot-TrEMBL)
CTNNA1ProteinP35221 (Uniprot-TrEMBL)
CTNND1 ProteinO60716 (Uniprot-TrEMBL)
CTNND1ProteinO60716 (Uniprot-TrEMBL)
Ca2+MetaboliteCHEBI:29108 (ChEBI)
Cadherin trans-homodimerComplexR-HSA-418999 (Reactome)
Cadherin:Catenin complexComplexR-HSA-418976 (Reactome)
Classic CadherinComplexR-HSA-418977 (Reactome)
ClaudinComplexR-HSA-419998 (Reactome)
DST ProteinQ03001 (Uniprot-TrEMBL)
F-actin R-HSA-196015 (Reactome)
F-actin R-HSA-201877 (Reactome)
F-actin:ANGComplexR-HSA-5692424 (Reactome)
F-actinR-HSA-196015 (Reactome)
F-actinR-HSA-201877 (Reactome)
F11R ProteinQ9Y624 (Uniprot-TrEMBL)
F11RProteinQ9Y624 (Uniprot-TrEMBL)
FBLIM1 ProteinQ8WUP2 (Uniprot-TrEMBL)
FBLIM1ProteinQ8WUP2 (Uniprot-TrEMBL)
FERMT2 ProteinQ96AC1 (Uniprot-TrEMBL)
FERMT2ProteinQ96AC1 (Uniprot-TrEMBL)
FLNA ProteinP21333 (Uniprot-TrEMBL)
FLNC ProteinQ14315 (Uniprot-TrEMBL)
FilaminComplexR-HSA-446328 (Reactome)
ILK ProteinQ13418 (Uniprot-TrEMBL)
ILK:Integrin beta-1ComplexR-HSA-446408 (Reactome)
ILKProteinQ13418 (Uniprot-TrEMBL)
INADL ProteinQ8NI35 (Uniprot-TrEMBL)
INADLProteinQ8NI35 (Uniprot-TrEMBL)
ITGA6(24-1130) ProteinP23229 (Uniprot-TrEMBL)
ITGB1 ProteinP05556 (Uniprot-TrEMBL)
ITGB1ProteinP05556 (Uniprot-TrEMBL)
ITGB4 ProteinP16144 (Uniprot-TrEMBL)

alpha 6:beta

4:Plectin:BP180:Laminin-322 complex
ComplexR-HSA-445997 (Reactome)
Integrin alpha6:beta4:Plectin:BP180 complexComplexR-HSA-445993 (Reactome)
Integrin alpha

6:beta 4:Plectin

ComplexR-HSA-445996 (Reactome)
Integrin alpha6beta4ComplexR-HSA-215997 (Reactome)
JAM-A:PAR-aPKC complexComplexR-HSA-420006 (Reactome)
JUP ProteinP14923 (Uniprot-TrEMBL)
Keratin 5/14 R-HSA-446069 (Reactome)
Keratin 5/14R-HSA-446069 (Reactome)
LAMA3 ProteinQ16787 (Uniprot-TrEMBL)
LAMB3 ProteinQ13751 (Uniprot-TrEMBL)
LAMC2 ProteinQ13753 (Uniprot-TrEMBL)
LIMS1 ProteinP48059 (Uniprot-TrEMBL)
LIMS1ProteinP48059 (Uniprot-TrEMBL)
LIMS2 ProteinQ7Z4I7 (Uniprot-TrEMBL)
Laminin-332ComplexR-HSA-216001 (Reactome)
MIG-2:MIGFILINComplexR-HSA-430295 (Reactome)
MIGFILIN:VASPComplexR-HSA-446308 (Reactome)
MLLT4-2 ProteinP55196-2 (Uniprot-TrEMBL)
MLLT4-2ProteinP55196-2 (Uniprot-TrEMBL)
MPP5 ProteinQ8N3R9 (Uniprot-TrEMBL)
MPP5ProteinQ8N3R9 (Uniprot-TrEMBL)
Migfilin:Filamin A:F-actinComplexR-HSA-430323 (Reactome) Interaction of Filamin with Migfiln mediates the association with the Migfilin with actin filaments (Tu et al., 2002).
Necl-1/Necl-2/Necl-3 homodimerComplexR-HSA-420583 (Reactome)
Necl-1/Necl-2/Necl-3 trans homodimerComplexR-HSA-420594 (Reactome)
Necl-1:Necl-2 trans heterodimerComplexR-HSA-420587 (Reactome)
Necl-1:Nectin-1 trans heterodimerComplexR-HSA-420585 (Reactome)
Necl-1:Nectin-3 trans heterodimerComplexR-HSA-420577 (Reactome)
Nectin cis-homodimerComplexR-HSA-433730 (Reactome)
Nectin trans homodimerComplexR-HSA-418972 (Reactome)
Nectin-1 cis homodimerComplexR-HSA-420607 (Reactome)
Nectin-1:Nectin-4 trans heterodimerComplexR-HSA-420609 (Reactome)
Nectin-1:PVRL3 trans heterodimerComplexR-HSA-420601 (Reactome)
Nectin-2 cis homodimerComplexR-HSA-420575 (Reactome)
Nectin-2:PVRL3 transheterodimerComplexR-HSA-420605 (Reactome)
Nectin-3:Necl-2 trans heterodimerComplexR-HSA-420578 (Reactome)
Nectin-4 cis homodimerComplexR-HSA-420606 (Reactome)
Nectin:afadinComplexR-HSA-419013 (Reactome)
NectinComplexR-HSA-419017 (Reactome)
PARD3 ProteinQ8TEW0 (Uniprot-TrEMBL)
PARD6A ProteinQ9NPB6 (Uniprot-TrEMBL)
PARD6B ProteinQ9BYG5 (Uniprot-TrEMBL)
PARD6G ProteinQ9BYG4 (Uniprot-TrEMBL)
PARVA ProteinQ9NVD7 (Uniprot-TrEMBL)
PARVA:PaxillinComplexR-HSA-446326 (Reactome)
PARVA:TESK1ComplexR-HSA-446404 (Reactome)
PARVAProteinQ9NVD7 (Uniprot-TrEMBL)
PARVB ProteinQ9HBI1 (Uniprot-TrEMBL)
PARVB:alpha actininComplexR-HSA-446335 (Reactome)
PARVBProteinQ9HBI1 (Uniprot-TrEMBL)
PINCH-ILK-parvin complexComplexR-HSA-432932 (Reactome)
PINCHComplexR-HSA-446104 (Reactome)
PLEC ProteinQ15149 (Uniprot-TrEMBL)
PLECProteinQ15149 (Uniprot-TrEMBL)
PRKCI ProteinP41743 (Uniprot-TrEMBL)
PRV:PVRL3 trans heterodimerComplexR-HSA-420579 (Reactome)
PVR ProteinP15151 (Uniprot-TrEMBL)
PVRL1 ProteinQ15223 (Uniprot-TrEMBL)
PVRL1ProteinQ15223 (Uniprot-TrEMBL)
PVRL2 ProteinQ92692 (Uniprot-TrEMBL)
PVRL3 ProteinQ9NQS3 (Uniprot-TrEMBL)
PVRL3 dimerComplexR-HSA-420590 (Reactome)
PVRL3ProteinQ9NQS3 (Uniprot-TrEMBL)
PVRL4 ProteinQ96NY8 (Uniprot-TrEMBL)
PVRProteinP15151 (Uniprot-TrEMBL)
PXN ProteinP49023 (Uniprot-TrEMBL)
PXNProteinP49023 (Uniprot-TrEMBL)
Par3:Par6:aPKC complexComplexR-HSA-419976 (Reactome)
ParvB/Affixin:Alpha-PixComplexR-HSA-446035 (Reactome)
RSU1 ProteinQ15404 (Uniprot-TrEMBL)
RSU1ProteinQ15404 (Uniprot-TrEMBL)
Rsu-1:Pinch1 complexComplexR-HSA-446302 (Reactome)
SDK1(?-2213) ProteinQ7Z5N4 (Uniprot-TrEMBL)
SDK1(?-2213)ProteinQ7Z5N4 (Uniprot-TrEMBL)
SDK2 ProteinQ58EX2 (Uniprot-TrEMBL)
SDK2ProteinQ58EX2 (Uniprot-TrEMBL)
TESK1 ProteinQ15569 (Uniprot-TrEMBL)
TESK1ProteinQ15569 (Uniprot-TrEMBL)
Trans-homophilic SDK1 dimerComplexR-HSA-373699 (Reactome)
Trans-homophilic SDK2 dimerComplexR-HSA-373698 (Reactome)
Type II hemidesmosomeComplexR-HSA-446086 (Reactome)
VASP ProteinP50552 (Uniprot-TrEMBL)
VASPProteinP50552 (Uniprot-TrEMBL)
VE-cadherin ProteinP33151 (Uniprot-TrEMBL)
alpha/beta parvinComplexR-HSA-446032 (Reactome)
beta-catenin R-HSA-191731 (Reactome)
claudin trans-homodimerComplexR-HSA-421252 (Reactome)

Annotated Interactions

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SourceTargetTypeDatabase referenceComment
ACTN1R-HSA-430308 (Reactome)
ANGR-HSA-5692437 (Reactome)
ARHGEF6R-HSA-432946 (Reactome)
Afadin:F-actinArrowR-HSA-433725 (Reactome)
BP230:BP180:Plectin:integrin alpha 6 beta 4:Laminin 332ArrowR-HSA-432956 (Reactome)
BP230:BP180:Plectin:integrin alpha 6 beta 4:Laminin 332R-HSA-446083 (Reactome)
BP230R-HSA-432956 (Reactome)
Beta-catenin/gamma cateninR-HSA-419002 (Reactome)
CADM1R-HSA-420586 (Reactome)
CADM1R-HSA-420595 (Reactome)
CADM3R-HSA-420582 (Reactome)
CADM3R-HSA-420584 (Reactome)
CADM3R-HSA-420586 (Reactome)
CD151:BP230:BP180:Plectin:Integrin alpha 6 beta 4: LamininArrowR-HSA-446083 (Reactome)
CD151:BP230:BP180:Plectin:Integrin alpha 6 beta 4: LamininR-HSA-446077 (Reactome)
CD151R-HSA-446083 (Reactome)
COL17A1(1-1497)R-HSA-432952 (Reactome)
CRB3:PALS1:PATJ complexArrowR-HSA-420661 (Reactome)
CRB3R-HSA-420661 (Reactome)
CTNNA1R-HSA-419002 (Reactome)
CTNND1R-HSA-419002 (Reactome)
Ca2+R-HSA-419001 (Reactome)
Cadherin trans-homodimerArrowR-HSA-419001 (Reactome)
Cadherin:Catenin complexArrowR-HSA-419002 (Reactome)
Classic CadherinR-HSA-419001 (Reactome)
Classic CadherinR-HSA-419002 (Reactome)
ClaudinR-HSA-420019 (Reactome)
F-actin:ANGArrowR-HSA-5692437 (Reactome)
F-actinR-HSA-430347 (Reactome)
F-actinR-HSA-433725 (Reactome)
F-actinR-HSA-5692437 (Reactome)
F11RR-HSA-419981 (Reactome)
FBLIM1R-HSA-430341 (Reactome)
FBLIM1R-HSA-430347 (Reactome)
FBLIM1R-HSA-446364 (Reactome)
FERMT2R-HSA-430341 (Reactome)
FilaminR-HSA-430347 (Reactome)
ILK:Integrin beta-1ArrowR-HSA-432897 (Reactome)
ILKR-HSA-432897 (Reactome)
ILKR-HSA-446391 (Reactome)
INADLR-HSA-420661 (Reactome)
ITGB1R-HSA-432897 (Reactome)

alpha 6:beta

4:Plectin:BP180:Laminin-322 complex
ArrowR-HSA-446089 (Reactome)

alpha 6:beta

4:Plectin:BP180:Laminin-322 complex
R-HSA-432956 (Reactome)
Integrin alpha6:beta4:Plectin:BP180 complexArrowR-HSA-432952 (Reactome)
Integrin alpha6:beta4:Plectin:BP180 complexR-HSA-446089 (Reactome)
Integrin alpha

6:beta 4:Plectin

ArrowR-HSA-432909 (Reactome)
Integrin alpha

6:beta 4:Plectin

R-HSA-432952 (Reactome)
Integrin alpha6beta4R-HSA-432909 (Reactome)
JAM-A:PAR-aPKC complexArrowR-HSA-419981 (Reactome)
Keratin 5/14R-HSA-446077 (Reactome)
LIMS1R-HSA-430311 (Reactome)
Laminin-332R-HSA-446089 (Reactome)
MIG-2:MIGFILINArrowR-HSA-430341 (Reactome)
MIGFILIN:VASPArrowR-HSA-446364 (Reactome)
MLLT4-2R-HSA-419003 (Reactome)
MLLT4-2R-HSA-433725 (Reactome)
MPP5R-HSA-420661 (Reactome)
Migfilin:Filamin A:F-actinArrowR-HSA-430347 (Reactome)
Necl-1/Necl-2/Necl-3 homodimerR-HSA-420592 (Reactome)
Necl-1/Necl-2/Necl-3 trans homodimerArrowR-HSA-420592 (Reactome)
Necl-1:Necl-2 trans heterodimerArrowR-HSA-420586 (Reactome)
Necl-1:Nectin-1 trans heterodimerArrowR-HSA-420582 (Reactome)
Necl-1:Nectin-3 trans heterodimerArrowR-HSA-420584 (Reactome)
Nectin cis-homodimerArrowR-HSA-433711 (Reactome)
Nectin cis-homodimerR-HSA-419011 (Reactome)
Nectin trans homodimerArrowR-HSA-419011 (Reactome)
Nectin-1 cis homodimerR-HSA-420580 (Reactome)
Nectin-1 cis homodimerR-HSA-420598 (Reactome)
Nectin-1:Nectin-4 trans heterodimerArrowR-HSA-420598 (Reactome)
Nectin-1:PVRL3 trans heterodimerArrowR-HSA-420580 (Reactome)
Nectin-2 cis homodimerR-HSA-420591 (Reactome)
Nectin-2:PVRL3 transheterodimerArrowR-HSA-420591 (Reactome)
Nectin-3:Necl-2 trans heterodimerArrowR-HSA-420595 (Reactome)
Nectin-4 cis homodimerR-HSA-420598 (Reactome)
Nectin:afadinArrowR-HSA-419003 (Reactome)
NectinR-HSA-419003 (Reactome)
NectinR-HSA-433711 (Reactome)
PARVA:PaxillinArrowR-HSA-446322 (Reactome)
PARVA:TESK1ArrowR-HSA-446372 (Reactome)
PARVAR-HSA-446322 (Reactome)
PARVAR-HSA-446372 (Reactome)
PARVB:alpha actininArrowR-HSA-430308 (Reactome)
PARVBR-HSA-430308 (Reactome)
PARVBR-HSA-432946 (Reactome)
PINCH-ILK-parvin complexArrowR-HSA-446391 (Reactome)
PINCHR-HSA-446391 (Reactome)
PLECR-HSA-432909 (Reactome)
PRV:PVRL3 trans heterodimerArrowR-HSA-420593 (Reactome)
PVRL1R-HSA-420582 (Reactome)
PVRL3 dimerR-HSA-420580 (Reactome)
PVRL3 dimerR-HSA-420591 (Reactome)
PVRL3R-HSA-420584 (Reactome)
PVRL3R-HSA-420593 (Reactome)
PVRL3R-HSA-420595 (Reactome)
PVRR-HSA-420593 (Reactome)
PXNR-HSA-446322 (Reactome)
Par3:Par6:aPKC complexR-HSA-419981 (Reactome)
ParvB/Affixin:Alpha-PixArrowR-HSA-432946 (Reactome)
R-HSA-373741 (Reactome) SDK1 and SDK2 are homophilic adhesion molecules. Cells expressing them exhibit a strong preference to interact exclusively with cells expressing the same sidekick form. The N-terminal four Ig domains are arranged in a horseshoe conformation and mediate homophilic adhesion, with Ig1-2 conferring the majority of binding affinity and differential specificity.
R-HSA-373745 (Reactome) SDK1 and SDK2 are homophilic adhesion molecules. Cells expressing them exhibit a strong preference to interact exclusively with cells expressing the same sidekick form. The N-terminal four Ig domains are arranged in a horseshoe conformation and mediate homophilic adhesion, with Ig1-2 conferring the majority of binding affinity and differential specificity.
R-HSA-419001 (Reactome) Cadherins are the major cell adhesion molecules at adherens junctions (AJs). Classical cadherins are Ca2+-dependent, homophilic adhesion molecules that link adjacent cells (Gumbiner, 2005; Halbleib and Nelson, 2006; Pokutta and Weis, 2007). The extracellular domain of classical cadherins consists of five cadherin-type repeats (called "extracellular cadherin" (EC) -domains). In the presence of Ca2+, the monomers form parallel cis-dimers resulting in a rod-like structure (Gumbiner, 2005). The cis-dimers undergo trans homophilic interactions to mediate homotypic cell-cell interactions. The cytoplasmic tails of classical cadherins interact with different proteins (primarily catenins) to regulate cell surface expression levels, linkage to the actin cytoskeleton, and cell signaling. Non-classical cadherins (Atypical cadherins, Proto-cadherins, cadherin-related proteins) have a variable number of cadherin-type repeats, do not associate with catenins, and are not associated with AJs (Halbleib and Nelson, 2006).
R-HSA-419002 (Reactome) The cytoplasmic tails of classical cadherins form a multiprotein complex with alpha-catenin, beta/gamma-catenins and p120 catenin (p120ctn) (Gumbiner, 2005). Beta-catenin and p120ctn directly interact with the cadherin molecule through highly conserved regions in the membrane-distal and membrane-proximal domains, respectively, of the cadherin. The interactions with beta-catenin and p120ctn regulate cadherin localization at cell-cell contacts as well as its adhesive activity (Halbleib and Nelson, 2006). The association of beta-catenin and alpha-catenin probably serves to link the cadherin-catenin complex to the F-actin cytoskeleton through the protein ELPIN (Abe and Takeichi, 2008). Independently of its association with the cadherin-catenin complex, alpha-catenin also regulates the bundling and growth of actin filaments at sites of cell-cell contact formation (Drees et al., 2005; Weis and Nelson, 2006).
R-HSA-419003 (Reactome) Nectins are immunoglobulin-like cell adhesion molecules comprising a family of four members, nectin 1 - 4 (Takai and Nakanishi, 2003). In contrast to classical cadherins which interact only homophilically, nectins undergo trans-homophilic and trans-heterophilic interactions with nectins and nectin-like molecules (Takai et al., 2008b). Nectins cooperate with cadherins in regulating the formation of adherens junctions (AJs) and the strength of cell-cell adhesion. Nectins are linked to the underlying actin cytoskeleton through their interaction with the actin-binding protein Afadin (Takai et al., 2008a). Nectin-based cell–cell adhesions contribute to formation of many types of cell-cell junctions including AJs, tight junctions, and synaptic junctions.
R-HSA-419011 (Reactome) Nectins are Ca(2+)-independent cell adhesion molecules which interact homophilically and heterophilically in trans to form cell-cell adhesions (reviewed in (Sakisaka et al., 2007; Takai et al., 2008). Each nectin first forms homo-cis-dimers and then homo- or hetero-trans-dimers through the extracellular region, causing cell–cell adhesion. The Nectin protein family is made up of four members, nectin-1, -2, -3, and -4, all of which have an extracellular region with three Ig-like loops, a single transmembrane region, and a cytoplasmic tail region.
R-HSA-419981 (Reactome) PAR-3 exists in a ternary complex with aPKC and PAR-6 to form the PAR-aPKC complex (Macara, 2004; Suzuki and Ohno, 2006). This complex is critically involved in the development of Tight Junctions (TJs) from primordial spot-like Adherens Junctions (AJs) (Suzuki et al., 2002). PAR-3 directly interacts with Junctional Adhesion Molecules (JAM)-A, -B, and -C (Ebnet et al., 2001; Ebnet et al., 2004).The interaction with JAM-A might anchor the PAR-aPKC complex to TJs but might also be necessary to recruit the PAR-aPKC complex to primordial spot-like AJs where it becomes activated in response to cell-cell adhesion (reviewed in (Ebnet et al., 2008). The PAR-aPKC complex might also be physically linked to the second polarity protein complex at TJs, the CRB3-Pals1-PATJ complex through a direct interaction between PAR-6 and Pals1 (Hurd et al., 2003).
R-HSA-420019 (Reactome) Claudins are the major cell adhesion molecules in tight junctions and are involved in regulating the paracellular flux of water-soluble molecules between adjacent cells (reviewed in (Furuse and Tsukita, 2006). Claudins create paired strands through homophilic and heterophilic cis and trans interactions. A strand of one cell associates laterally with a strand in the apposing membrane of an adjacent cell creating a paired TJ strand (Tsukita et al., 2001). The TJ strands contain aqueous pores with size and charge selectivity that are permeable to water-soluble molecules. Differences in the barrier properties in epithelia of different tissues have been explained by the expression of a unique set of claudins in a given tissue (Van Itallie and Anderson, 2006). 24 claudins were identified in humans, which allows a large number of possible combinations and specific barrier properties.
R-HSA-420580 (Reactome) Nectin-1 and Nectin 3 interact forming a trans heterodimer.
R-HSA-420582 (Reactome) Necl-1 displays Ca2+-independent heterophilic cell-cell adhesion activity with Nectin-1 (Kakunaga et al., 2005).
R-HSA-420584 (Reactome) Necl-1 displays Ca2+-independent heterophilic cell-cell adhesion activity with Nectin-3 (Kakunaga et al., 2005).
R-HSA-420586 (Reactome) Necl-1 displays Ca2+-independent heterophilic cell-cell adhesion activity with Necl-2 (Kakunaga et al., 2005).
R-HSA-420591 (Reactome) Nectin-2 and Nectin-3 interact forming a trans heterodimer.
R-HSA-420592 (Reactome) The nectin-like (Necl) family comprises five members, called Necl-1 to -5. Necl have an overall organization like that of nectins with three Ig-like domains, a transmembrane region and a cytoplasmic domain. Necls have a greater variety of functions than nectins and are ubiquitously expressed. In contrast to nectins, Necls do not interact with afadin. Transhomodimerization has been described for Necl-1, -2 and -3 but not for Necl-4 and -5. (Sakisaka et al., 2007; Sakisaka and Takai, 2004; Takai et al., 2008).
R-HSA-420593 (Reactome) Necl-5/PVR and Nectin-3/PVRL3 interact forming a trans heterodimer.
R-HSA-420595 (Reactome) Necl-2 and Nectin 3 form a trans heterodimer.
R-HSA-420598 (Reactome) Nectin-1 and Nectin-4 interact forming a trans heterodimer.
R-HSA-420661 (Reactome) The CRB3–Pals1–PATJ complex is the second major cell polarity protein complex at Tight Junctions (TJs) (Shin et al., 2006). The integral membrane protein CRB3 localizes to the apical domain of epithelial cells and is concentrated at TJs. CRB3 directly associates with Pals1 which interacts with PATJ, a proteins consisting of 10 PDZ domains. The interaction with CRB3 might recruit the Pals1-PATJ complex to TJs (Lemmers et al., 2002; Roh et al., 2003). Although its precise functions of the individual components have not been established, the complex is required for TJ formation, in part through the stabilization of apical and lateral components of tight junctions (Michel et al., 2005; Shin et al., 2005).
R-HSA-430308 (Reactome) PARVB interacts with the actin cross-linking protein Alpha-actinin (Yamaji et al. 2004). The ILK-PARVB complex may serve as an integrin-anchoring site for alpha-actinin and thereby mediate integrin signaling to alpha-actinin, which has been shown to play an important role in actin polymerization at focal adhesions (Yamaji et al., 2004).
R-HSA-430311 (Reactome) The Ras suppressor, Rsu-1, interacts with the LIM 5 domain of PINCH1 (but not PINCH2) and may inhibit cell migration by stabilizing the Pinch-ILK-parvin adhesion complex (Dougherty et al., 2008; Kadrmas et al., 2004).
R-HSA-430341 (Reactome) Migfilin functions in cell shape modulation regulating filamin-mediated cross-linking and stabilization of actin filaments. Migfilin is recruited to cell–Extra Cellular Matrix adhesion sites in a variety of fibroblasts, epithelial, and endothelial cells by interaction with Mig-2 (Tu et al., 2003).
R-HSA-430347 (Reactome) Migfilin associates with actin filaments as a result of its interaction with filamin (Tu et al., 2003). Migfilin associates with actin filaments and loss of migfilin decreases the level of F-actin suggesting that, in addition to providing an anchoring site for actin filaments at cell-ECM adhesions, migfilin also functions in the regulation of filamin-mediated cross-linking and stabilization of actin filaments (Tu et al., 2003).
R-HSA-432897 (Reactome) ILK interacts with the cytoplasmic domain of beta1-integrin (Hannigan et al., 1996).
R-HSA-432909 (Reactome) The actin-binding domain of plectin interacts with the first pair of FNIII repeats and the N-terminal 35 amino acids of the connecting segment of integrin b4 ( Geerts et al., 1999; Niessen et al., 1997; Koster et al., 2004). This interaction is thought to be the initial step in hemidesmosome (HD) assembly and is critical for the mechanical stability of the HD. This interaction is destabilized when HD disassembly is required, for example, to allow cell migration during wound healing. The Integrin a6b4 also associates extracellularly with laminin-332 (See Koster et al., 2003).
R-HSA-432946 (Reactome) The Rho GTPases, Cdc42 and Rac1, play critical roles in cell migration by integrating cell-substrate adhesion and actin polymerization. PARVB/affixin appears to participate in the activation of Rac and Cdc42 by associating with alpha PIX through its CH1 domain (Mishima et al., 2004; Rosenberger et al., 2005). This activity of PARVB/affixin could promote the polymerization of actin through the activation of downstream effectors of Rac1/Cdc42, including WASP-Arp2/3 and Mena/VASP. Alpha-PIX, ILK and PARVB can be found at the leading edge of spreading cells (Rosenberger et al., 2005 ), and it is likely that activation of Rac1 and Cdc42 at the lamellipodia in some cells is stimulated by interactions of aPIX with PARVB and regulated by interaction of ILK and PARVB (see Sepulveda and Wu, 2005 ).
R-HSA-432952 (Reactome) BP180 interacts with Plectin following the association of Plectin with Integrin b4 (b4) (Koster et al., 2003). It is not clear whether the binding of BP180 to Plectin and b4 occurs sequentially or at the same time as the interaction between BP180 and Laminin?332.
R-HSA-432956 (Reactome) Following the association of BP180 with the forming hemidesmosome, BP230 is recruited through associations with BP180 and a region on beta 4 integrin that includes the C-terminal 21 amino acids of the connecting segment and the second pair of FNIII repeats (Hopkinson et al.,2000).
R-HSA-433711 (Reactome) The Nectin family of Ca2+-independent cell adhesion molecules (CAMs) is comprised of four members, nectin-1, nectin-2, nectin-3, and nectin-4 (reviewed in Sakisaka et al., 2007). Each nectin first forms homophilic cis-dimers and then forms homophilic or heterophilic trans-dimers involved in cell–cell adhesion. Heterophilic trans-interactions are stronger than homophilic trans-interactions.
R-HSA-433725 (Reactome) Afadin serves as a linker of the actin cytoskeleton to the plasma membrane at cell-to-cell Adherens Junctions (Mandai et al., 1997).
R-HSA-446077 (Reactome) BP230 interacts with cytokeratins K5/K14 (Fontao et al., 2003).
R-HSA-446083 (Reactome) CD151 interacts with the extracellular domain of the integrin alpha 6 subunit. CD151 is thought to play a role in the formation and stability of hemidesmosomes by providing a framework for the spatial organization of the hemidesmosomal components (Sterk et al., 2000).
R-HSA-446089 (Reactome) BP180 interacts with Plectin following the association of Plectin with Integrin b4 (b4) (Koster et al., 2003). It is not clear whether the binding of BP180 to Plectin and b4 occurs sequentially or at the same time as the interaction between BP180 and Laminin?332.
R-HSA-446322 (Reactome) The focal adhesion protein alpha-parvin, interacts with paxillin, through the C-terminal CH-containing fragment of the alpha-parvin and paxillin LD motif (Wang et al., 2008; Lorenz et al., 2008). This interaction likely contributes to the localization of the PINCH-ILK-parvin complexes to focal adhesions.
R-HSA-446364 (Reactome) Migfilin interacts with VASP and regulates VASP localization to cell-matrix adhesions (Zhang et al., 2006). Interaction between migfilin and VASP is critical for migfilin-mediated regulation of cell migration (Zhang et al., 2006).
R-HSA-446372 (Reactome) The association of PARVA with TESK1 appears to suppress cell spreading (Lalonde et al. 2005). TESK1 can phosphorylate cofilin and promote F-actin polymerization and cell spreading (Tsumura et al., 2005 ; Toshima et al., 2001; Leeksma et al., 2002). PARVA associates with testicular protein kinase 1 (TESK1) and inhibits its activity (Lalonde et al. 2005).
R-HSA-446391 (Reactome) The PINCH-ILK-parvin complex (Tu et al., 2001; Zhang et al., 2002; Li et al., 1999) localizes to focal adhesions and plays a critical role in the regulation of cell adhesion, cell shape modulation, motility and ECM deposition (Velyvis et al., 2001; Braun et al, 2003). ILK binds PINCH through its N-terminal domain and binds PARVA or PARVB through its C-terminal domain, resulting in formation of the ternary PINCH-ILK-parvin complex (Tu et al., 2001). These complexes form before they are localized to integrin-rich adhesion sites (Zhang et al., 2002). Formation of the ILK-PINCH-parvin complexes stabilizes these proteins by protecting them from degradation by the proteasome (Fukuda et al., 2003).
R-HSA-5692437 (Reactome) Angiogenin (ANG) binds to F-actin on the surface of endothelial cells. Once bound, ANG is endocytosed and translocated to the nucleus where it stimulates ribosomal RNA syntheses which induce vascularisation of normal and malignant tissues (Dickson et al. 2009). Defects in ANG can cause amyotrophic lateral sclerosis 9 (ALS9; MIM:611895), a fatal progressive neurodegenerative disorder characterised by the preferential loss of motor neurons in the brain stem, motor cortex and spinal cord, resulting in paralysis and respiratory failure between 3 to 5 years of onset of symptoms (Padhi et al. 2014).
RSU1R-HSA-430311 (Reactome)
Rsu-1:Pinch1 complexArrowR-HSA-430311 (Reactome)
SDK1(?-2213)R-HSA-373745 (Reactome)
SDK2R-HSA-373741 (Reactome)
TESK1R-HSA-446372 (Reactome)
Trans-homophilic SDK1 dimerArrowR-HSA-373745 (Reactome)
Trans-homophilic SDK2 dimerArrowR-HSA-373741 (Reactome)
Type II hemidesmosomeArrowR-HSA-446077 (Reactome)
VASPR-HSA-446364 (Reactome)
alpha/beta parvinR-HSA-446391 (Reactome)
claudin trans-homodimerArrowR-HSA-420019 (Reactome)
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