Small heat shock proteins and α-crystallins: dynamic proteins with flexible functions

Trends Biochem Sci. 2012 Mar;37(3):106-17. doi: 10.1016/j.tibs.2011.11.005. Epub 2011 Dec 14.

Abstract

The small heat shock proteins (sHSPs) and the related α-crystallins (αCs) are virtually ubiquitous proteins that are strongly induced by a variety of stresses, but that also function constitutively in multiple cell types in many organisms. Extensive research has demonstrated that a majority of sHSPs and αCs can act as ATP-independent molecular chaperones by binding denaturing proteins and thereby protecting cells from damage due to irreversible protein aggregation. As a result of their diverse evolutionary history, their connection to inherited human diseases, and their novel protein dynamics, sHSPs and αCs are of significant interest to many areas of biology and biochemistry. However, it is increasingly clear that no single model is sufficient to describe the structure, function or mechanism of action of sHSPs and αCs. In this review, we discuss recent data that provide insight into the variety of structures of these proteins, their dynamic behavior, how they recognize substrates, and their many possible cellular roles.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Evolution, Molecular
  • Genetic Diseases, Inborn / metabolism
  • Heat-Shock Proteins, Small / chemistry*
  • Heat-Shock Proteins, Small / metabolism*
  • Heat-Shock Proteins, Small / physiology
  • Humans
  • Molecular Chaperones / chemistry
  • Molecular Chaperones / metabolism*
  • Molecular Sequence Data
  • Protein Conformation
  • Stress, Physiological
  • Substrate Specificity
  • alpha-Crystallins / chemistry*
  • alpha-Crystallins / metabolism*
  • alpha-Crystallins / physiology

Substances

  • Heat-Shock Proteins, Small
  • Molecular Chaperones
  • alpha-Crystallins