Format

Send to

Choose Destination
See comment in PubMed Commons below
FEBS Lett. 2013 Apr 17;587(8):1073-80. doi: 10.1016/j.febslet.2013.01.021. Epub 2013 Jan 20.

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

Author information

1
Department of Biochemistry, Box 357350, University of Washington, Seattle, WA 98195-7350, USA.

Abstract

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.

PMID:
23340341
PMCID:
PMC3865782
DOI:
10.1016/j.febslet.2013.01.021
[Indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Wiley Icon for PubMed Central
    Loading ...
    Support Center