Mechanisms of Small Heat Shock Proteins
| Autor: | Rachel E. Klevit, Hannah E.R. Baughman, Maria K. Janowska, Christopher N. Woods |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
030102 biochemistry & molecular biology Protein Conformation fungi Oxidation reduction Protein aggregation Protein Homeostasis Biology Hydrogen-Ion Concentration General Biochemistry Genetics and Molecular Biology Cell biology Heat-Shock Proteins Small 03 medical and health sciences Oxidative Stress 030104 developmental biology Protein structure PERSPECTIVES Metals Heat shock protein Humans Chaperone activity Phosphorylation Small Heat-Shock Proteins Oxidation-Reduction Function (biology) |
| Zdroj: | Cold Spring Harb Perspect Biol |
| ISSN: | 1943-0264 |
| Popis: | Small heat shock proteins (sHSPs) are ATP-independent chaperones that delay formation of harmful protein aggregates. sHSPs' role in protein homeostasis has been appreciated for decades, but their mechanisms of action remain poorly understood. This gap in understanding is largely a consequence of sHSP properties that make them recalcitrant to detailed study. Multiple stress-associated conditions including pH acidosis, oxidation, and unusual availability of metal ions, as well as reversible stress-induced phosphorylation can modulate sHSP chaperone activity. Investigations of sHSPs reveal that sHSPs can engage in transient or long-lived interactions with client proteins depending on solution conditions and sHSP or client identity. Recent advances in the field highlight both the diversity of function within the sHSP family and the exquisite sensitivity of individual sHSPs to cellular and experimental conditions. Here, we will present and highlight current understanding, recent progress, and future challenges. |
| Databáze: | OpenAIRE |
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