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.
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CITATION STYLE
Mitchem, M. M., Shrader, C., Abedi, E., & Truman, A. W. (2024, February 1). Novel insights into the post-translational modifications of Ydj1/DNAJA1 co-chaperones. Cell Stress and Chaperones. Elsevier B.V. https://doi.org/10.1016/j.cstres.2023.11.001
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