| Autor: |
Arrigo AP; Apoptosis, Cancer and Development Laboratory, Lyon Cancer Research Center, INSERM U1052-CNRS UMR5286, Centre Léon Bérard, 28 rue Laennec, Lyon, 69008, France. parrigo@me.com. |
| Jazyk: |
angličtina |
| Zdroj: |
Cell stress & chaperones [Cell Stress Chaperones] 2017 Jul; Vol. 22 (4), pp. 517-529. Date of Electronic Publication: 2017 Jan 31. |
| DOI: |
10.1007/s12192-017-0765-1 |
| Abstrakt: |
Constitutively expressed small heat shock protein HspB1 regulates many fundamental cellular processes and plays major roles in many human pathological diseases. In that regard, this chaperone has a huge number of apparently unrelated functions that appear linked to its ability to recognize many client polypeptides that are subsequently modified in their activity and/or half-life. A major parameter to understand how HspB1 is dedicated to interact with particular clients in defined cellular conditions relates to its complex oligomerization and phosphorylation properties. Indeed, HspB1 structural organization displays dynamic and complex rearrangements in response to changes in the cellular environment or when the cell physiology is modified. These structural modifications probably reflect the formation of structural platforms aimed at recognizing specific client polypeptides. Here, I have reviewed data from the literature and re-analyzed my own studies to describe and discuss these fascinating changes in HspB1 structural organization. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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