Novel insights into the post-translational modifications of Ydj1/DNAJA1 co-chaperones

Cell Stress Chaperones. 2024 Feb;29(1):1-9. doi: 10.1016/j.cstres.2023.11.001. Epub 2023 Nov 17.

Abstract

The activity of the Hsp70 molecular chaperone is regulated by a suite of helper co-chaperones that include J-proteins. Studies on J-proteins have historically focused on their expression, localization, and activation of Hsp70. There is growing evidence that the post-translational modifications (PTMs) of chaperones (the chaperone code) fine-tune chaperone function. This mini-review summarizes the current understanding of the role and regulation of PTMs on the major J-proteins Ydj1 and DNAJA1. Understanding these PTMs may provide novel therapeutic avenues for targeting chaperone activity in cancer and neurodegenerative diseases.

Keywords: Chaperone code; Co-chaperones; DNAJA1; PTMs; Ydj1.

Publication types

  • Review

MeSH terms

  • HSP40 Heat-Shock Proteins* / metabolism
  • HSP70 Heat-Shock Proteins / metabolism
  • Molecular Chaperones* / metabolism
  • Protein Folding
  • Protein Processing, Post-Translational

Substances

  • Molecular Chaperones
  • HSP40 Heat-Shock Proteins
  • HSP70 Heat-Shock Proteins