Heat shock protein family B member 3 (HSPB3)

Heat shock protein family B member 3 (HSPB3) is a small heat shock protein primarily expressed in skeletal and cardiac muscle but also found in smooth muscle and the nervous system[3]. It acts as a molecular chaperone with moderate activity and is particularly important for muscle cell differentiation by regulating nuclear events and maintaining dynamic states of the lamin B receptor (LBR) and associated chromatin structure[1]. HSPB3 functions by binding to specific substrates and prevents their aggregation under cellular stress, thus supporting proteostasis and cytoskeletal integrity[2][3]. It forms oligomeric complexes (such as trimers and tetramers, and hetero-oligomers with HSPB2) and is developmentally regulated, especially upregulated during myoblast differentiation and in response to proteotoxic stress rather than heat shock[1][2][3]. Pathogenic mutations in HSPB3 are associated with neuromuscular diseases manifesting as impaired muscle differentiation, myopathies, and axonal motor neuropathies due to dominant-negative effects and misregulation of nuclear protein quality control[1][3]. *Note: No drugs directly targeting HSPB3, mechanisms of action for inhibitors/modulators, or established biomarker/safety use were found in the supplied literature as of this search. The protein is a specialized chaperone rather than a classic receptor, enzyme, or transporter drug target.*

Other names

Heat shock protein beta-3HSP27HSPL27HspB3HSP 17Heat shock 17 kDa proteinProtein 3DHMN2CHMN2CHMND4heat shock protein beta-3heat shock 27kDa protein 3