Heat shock protein beta-1

Definition:

Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state. Plays a role in stress resistance and actin organization. Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins.

References:

[1]. Sergiy Kostenko, et al. PKA-induced F-actin rearrangement requires phosphorylation of Hsp27 by the MAPKAP kinase MK5. Cell Signal. 2009 May;21(5):712-8. [Content Brief]

[2]. Anne Holmgren, et al. Charcot-Marie-Tooth causing HSPB1 mutations increase Cdk5-mediated phosphorylation of neurofilaments. Acta Neuropathol. 2013 Jul;126(1):93-108. [Content Brief]

[3]. Leonardo Almeida-Souza, et al. Increased monomerization of mutant HSPB1 leads to protein hyperactivity in Charcot-Marie-Tooth neuropathy. J Biol Chem. 2010 Apr 23;285(17):12778-86. [Content Brief]

[4]. T Rogalla, et al. Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation. J Biol Chem. 1999 Jul 2;274(27):18947-56. [Content Brief]

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