αB-Crystallin Phosphorylation: Advances and Problems
- Authors: Muranova L.K.1, Sudnitsyna M.V.1, Gusev N.B.1
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Affiliations:
- Faculty of Biology
- Issue: Vol 83, No 10 (2018)
- Pages: 1196-1206
- Section: Review
- URL: https://journals.rcsi.science/0006-2979/article/view/151736
- DOI: https://doi.org/10.1134/S000629791810005X
- ID: 151736
Cite item
Abstract
The review is dedicated to phosphorylation of αB-crystallin (HspB5), one of ubiquitously expressed small heat shock proteins. We describe the structure and properties of αB-crystallin and protein kinases involved in its phosphorylation in different cells and tissues, advantages and drawbacks of pseudophosphorylation mutants in elucidation of the mechanism of αB-crystallin functioning, effects of phosphorylation on the quaternary structure and intracellular location of αB-crystallin, interactions of αB-crystallin with different elements of the cytoskeleton, and effect of phosphorylation on the chap-erone-like activity of αB-crystallin. We also discuss the validity of experimental data obtained by overexpression of pseudophosphorylation mutants for understanding the effect of phosphorylation on physiologically important properties of αB-crystallin, as well as the question why multiple attempts to phosphorylate αB-crystallin in vitro have been unsuccessful so far.
About the authors
L. K. Muranova
Faculty of Biology
Email: NBGusev@mail.ru
Russian Federation, Moscow, 119991
M. V. Sudnitsyna
Faculty of Biology
Email: NBGusev@mail.ru
Russian Federation, Moscow, 119991
N. B. Gusev
Faculty of Biology
Author for correspondence.
Email: NBGusev@mail.ru
Russian Federation, Moscow, 119991