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Interaction of human HSP22 (HSPB8) with other small heat shock proteins.

Abstract
Mammalian small heat shock proteins (sHSP) are abundant in muscles and are implicated in both muscle function and myopathies. Recently a new sHSP, HSP22 (HSPB8, H11), was identified in the human heart by its interaction with HSP27 (HSPB1). Using phylogenetic analysis we show that HSP22 is a true member of the sHSP superfamily. sHSPs interact with each other and form homo- and hetero-oligomeric complexes. The function of these complexes is poorly understood. Using gel filtration HPLC, the yeast two-hybrid method, immunoprecipitation, cross-linking, and fluorescence resonance energy transfer microscopy, we report that (i). HSP22 forms high molecular mass complexes in the heart, (ii). HSP22 interacts with itself, cvHSP (HSPB7), MKBP (HSPB2) and HSP27, and (iii). HSP22 has two binding domains (N- and C-terminal) that are specific for different binding partners. HSP22 homo-dimers are formed through N-N and N-C interactions, and HSP22-cvHSP hetero-dimers through C-C interaction. HSP22-MKBP and HSP22-HSP27 hetero-dimers involve the N and C termini of HSP22 and HSP27, respectively, but appear to require full-length protein as a binding partner.
AuthorsXiankui Sun, Jean-Marc Fontaine, Joshua S Rest, Eric A Shelden, Michael J Welsh, Rainer Benndorf
JournalThe Journal of biological chemistry (J Biol Chem) Vol. 279 Issue 4 Pg. 2394-402 (Jan 23 2004) ISSN: 0021-9258 [Print] United States
PMID14594798 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)
Chemical References
  • Heat-Shock Proteins
  • HSPB8 protein, human
  • Protein-Serine-Threonine Kinases
Topics
  • Cloning, Molecular
  • Dimerization
  • Heat-Shock Proteins (genetics, metabolism)
  • Humans
  • Phylogeny
  • Protein Binding
  • Protein Structure, Tertiary
  • Protein-Serine-Threonine Kinases

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