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Journal of Undergraduate Research

Keywords

HSPB2, small Heat Shock Proteins, sHSP, structural element

College

Life Sciences

Department

Microbiology and Molecular Biology

Abstract

HSPB2 is one of ten known small Heat Shock Proteins (sHSP) that share a conserved structural element called the alpha-crystallin domain. Extreme heat or cold, oxidative & reductive stress, and heavy metal exposure can induce the expression of these sHSP. HSPB2 is located on Chromosome 11, only 958 base pairs upstream of CYRAB. The protein homology and proximity of these two genes suggests they share structural and regulatory elements and serve as a model of inverted gene duplication. Both CRYAB and HSPB2 act as molecular chaperones to form complexes around denatured proteins and help them to refold into their normal shape while preventing protein aggregation. HSPB2 co-localizes with the mitochondria in a variety of cell lines and is known to associate with the outer membrane. Overexpression of this sHSP contributes to the survival of cells when heat stress is introduced. sHSP have been suggested to be redundant in their protein clientele. Our investigation of the binding partners of both CRYAB and HSPB2 reveals the chaperone mechanism of each sHSP and that the protein clientele are non-redundant in binding. We created the first protein interactome for any sHSP that provides insight to how HSPB2 contributes to cardiac muscle maintenance and metabolism.

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