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HSPB2/MKBP, a novel and unique member of the small heat‐shock protein family
Author(s) -
Hu Zhiping,
Yang Binbin,
Lu Wei,
Zhou Weijun,
Zeng Liuwang,
Li Ting,
Wang Xiang
Publication year - 2008
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.21682
Subject(s) - myotonic dystrophy , heat shock protein , biology , genetics , protein aggregation , chaperone (clinical) , pathogenesis , conserved sequence , gene , protein family , hsp27 , microbiology and biotechnology , peptide sequence , hsp70 , medicine , immunology , pathology
Abstract Although proteins belonging to the sHSP superfamily are diverse in sequence and size, most share characteristic features, including 1) a small molecular mass of 12–43 kDa, 2) a conserved α‐crystallin domain of 80–100 residues, 3) formation of large oligomers, 4) a dynamic quaternary structure, and 5) induction by stress conditions and chaperone activity in suppressing protein aggregation. HSPB2/MKBP (myotonic dystrophy kinase‐bind‐protein) retains the structural motif of the α‐crystallin family of HSPs but shows a unique nature compared with canonical family members, characterized by gene allocation, specific binding partners in skeletal muscle, and unique stress responsiveness. MKBP may be involved in the pathogenesis of myotonic dystrophy and contribute to the neuropathology in both Alzheimer's disease and hereditary cerebral hemorrhage with amyloidosis, Dutch type. © 2008 Wiley‐Liss, Inc.