REVIEW: α-Crystallins Are Small Heat Shock Proteins: Functional and Structural Properties

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T. S. Tikhomirova^1,2, O. M. Selivanova¹, and O. V. Galzitskaya^1*

¹Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia; E-mail: ogalzit@vega.protres.ru

²Institute for Biological Instrumentation, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia

^* To whom correspondence should be addressed.

Received July 27, 2016; Revision received October 25, 2016

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During its life cycle, a cell can be subjected to various external negative effects. Many proteins provide cell protection, including small heat shock proteins (sHsp) that have chaperone-like activity. These proteins have several important functions involving prevention of apoptosis and retention of cytoskeletal integrity; also, sHsp take part in the recovery of enzyme activity. The action mechanism of sHsp is based on the binding of hydrophobic regions exposed to the surface of a molten globule. α-Crystallins presented in chordate cells as two αA- and αB-isoforms are the most studied small heat shock proteins. In this review, we describe the main functions of α-crystallins, features of their secondary and tertiary structures, and examples of their partners in protein–protein interactions.

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KEY WORDS: aggregation, α-crystallin, apoptosis, cataract, oligomer, chaperone

DOI: 10.1134/S0006297917020031

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