Cellular proteostasis (WP4918)

Homo sapiens

In order to maintain protein homeostasis and cell function, cells are constantly synthesizing as well as degrading proteins. This is especially important when proteins are misfolded, due to extra- or intracellular stress or a genetic mutation, as this is the basis for many diseases. This pathway shows the major events which are involved in proteostasis.

Authors

Anna Baya Meuleman , Marvin Martens , Eric Weitz , and Egon Willighagen

Activity

last edited

Discuss this pathway

Check for ongoing discussions or start your own.

Cited In

Are you planning to include this pathway in your next publication? See How to Cite and add a link here to your paper once it's online.

Organisms

Homo sapiens

Communities

Annotations

Pathway Ontology

translation pathway protein folding pathway

Participants

Label Type Compact URI Comment
PFDN3 GeneProduct ensembl:ENSG00000155959
PFDN1 GeneProduct ensembl:ENSG00000113068
Hsp110 GeneProduct ensembl:ENST00000629751
Hsp40 GeneProduct ensembl:ENSG00000213946
Hsp90 GeneProduct ensembl:ENSG00000224411
CHIP GeneProduct ensembl:ENST00000565813.1
Hsp70 GeneProduct ensembl:ENSG00000225217
PFDN4 GeneProduct ensembl:ENSG00000101132
PFDN5 GeneProduct ensembl:ENSG00000123349
PFDN6 GeneProduct ensembl:ENSG00000204220
PFDN2 GeneProduct ensembl:ENSG00000143256
Hsp40 GeneProduct ensembl:ENSG00000213946
Hsp70 GeneProduct ensembl:ENSG00000225217
Hsp40 GeneProduct ensembl:ENSG00000213946
Hsp70 GeneProduct ensembl:ENSG00000225217
Hsp110 GeneProduct ensembl:ENST00000629751
Hsp40 GeneProduct ensembl:ENSG00000213946
Hsp70 GeneProduct ensembl:ENSG00000225217
Hsp90 GeneProduct ensembl:ENSG00000224411
Hsp70 GeneProduct ensembl:ENSG00000225217
Hsp70 GeneProduct ensembl:ENSG00000225217
Hsp90 GeneProduct ensembl:ENSG00000224411
CHIP GeneProduct ensembl:ENST00000565813.1

References

  1. Pathways of cellular proteostasis in aging and disease. Klaips CL, Jayaraj GG, Hartl FU. J Cell Biol. 2018 Jan 2;217(1):51–63. PubMed Europe PMC Scholia
  2. Prefoldin, a jellyfish-like molecular chaperone: functional cooperation with a group II chaperonin and beyond. Sahlan M, Zako T, Yohda M. Biophys Rev. 2018 Apr;10(2):339–45. PubMed Europe PMC Scholia