Post-translational modifications of Hsp70 family proteins: Expanding the chaperone code.

The Journal of Biological Chemistry
NitikaMatthias C Truttmann

Abstract

Cells must be able to cope with the challenge of folding newly synthesized proteins and refolding those that have become misfolded in the context of a crowded cytosol. One such coping mechanism that has appeared during evolution is the expression of well-conserved molecular chaperones, such as those that are part of the heat shock protein 70 (Hsp70) family of proteins that bind and fold a large proportion of the proteome. Although Hsp70 family chaperones have been extensively examined for the last 50 years, most studies have focused on regulation of Hsp70 activities by altered transcription, co-chaperone "helper" proteins, and ATP binding and hydrolysis. The rise of modern proteomics has uncovered a vast array of post-translational modifications (PTMs) on Hsp70 family proteins that include phosphorylation, acetylation, ubiquitination, AMPylation, and ADP-ribosylation. Similarly to the pattern of histone modifications, the histone code, this complex pattern of chaperone PTMs is now known as the "chaperone code." In this review, we discuss the history of the Hsp70 chaperone code, its currently understood regulation and functions, and thoughts on what the future of research into the chaperone code may entail.

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Citations

Dec 11, 2020·Experimental Cell Research·Madison T Wright, Lars Plate
Jan 14, 2021·Pigment Cell & Melanoma Research·I Caroline Le Poole
Feb 10, 2021·Cell Stress & Chaperones·Patricija van Oosten-HawleAndrew W Truman
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Apr 11, 2021·The Journal of Biological Chemistry·Andrew W Truman
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Aug 18, 2021·The Journal of Biological Chemistry·Hongtao LiQinglian Liu
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Feb 8, 2022·Cell Stress & Chaperones·Laura E KnightonAndrew W Truman

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