One size does not fit all: the oligomeric states of αB crystallin

FEBS Lett. 2013 Apr 17;587(8):1073-80. doi: 10.1016/j.febslet.2013.01.021. Epub 2013 Jan 20.


Small Heat Shock Proteins (sHSPs) are a diverse family of molecular chaperones that delay protein aggregation through interactions with non-native and aggregate-prone protein states. This function has been shown to be important to cellular viability and sHSP function/dysfunction is implicated in many diseases, including Alzheimer's and Alexander disease. Though their gene products are small, many sHSPs assemble into a distribution of large oligomeric states that undergo dynamic subunit exchange. These inherent properties present significant experimental challenges for characterizing sHSP oligomers. Of the human sHSPs, αB crystallin is a paradigm example of sHSP oligomeric properties. Advances in our understanding of sHSP structure, oligomeric distribution, and dynamics have prompted the proposal of several models for the oligomeric states of αB. The aim of this review is to highlight characteristics of αB crystallin (αB) that are key to understanding its structure and function. The current state of knowledge, existing models, and outstanding questions that remain to be addressed are presented.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Amino Acid Sequence
  • Heat-Shock Proteins, Small / chemistry
  • Heat-Shock Proteins, Small / genetics
  • Heat-Shock Proteins, Small / metabolism
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Binding
  • Protein Multimerization*
  • Protein Structure, Quaternary*
  • Protein Structure, Secondary*
  • alpha-Crystallin B Chain / chemistry*
  • alpha-Crystallin B Chain / genetics
  • alpha-Crystallin B Chain / metabolism


  • Heat-Shock Proteins, Small
  • alpha-Crystallin B Chain