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Biochemistry (Moscow)

, Volume 83, Issue 10, pp 1196–1206 | Cite as

αB-Crystallin Phosphorylation: Advances and Problems

  • L. K. Muranova
  • M. V. Sudnitsyna
  • N. B. GusevEmail author
Review
  • 86 Downloads

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.

Keywords

small heat shock proteins crystallins phosphorylation protein kinases 

Abbreviations

HspB5

αB-crystallin

sHsp (or HspB)

small heat shock protein

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Copyright information

© Pleiades Publishing, Ltd. 2018

Authors and Affiliations

  • L. K. Muranova
    • 1
  • M. V. Sudnitsyna
    • 1
  • N. B. Gusev
    • 1
    Email author
  1. 1.Faculty of BiologyLomonosov Moscow State UniversityMoscowRussia

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