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J. Biol. Chem., Vol. 279, Issue 4, 2394-2402, January 23, 2004

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Interaction of Human HSP22 (HSPB8) with Other Small Heat Shock Proteins^*

Xiankui Sun, Jean-Marc Fontaine, Joshua S. Rest, Eric A. Shelden, Michael J. Welsh, and Rainer Benndorf

From the Departments of Cell and Developmental Biology, University of Michigan Medical School and Ecology and Evolutionary Biology and Museum of Zoology, University of Michigan, Ann Arbor, Michigan 48109

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.

Received for publication, October 15, 2003

^* This work was supported by National Institutes of Health Grants P01ES11188 (to M. J. W. (Principal Investigator) and R. B.) and 5R01ES011196-02 (to E. A. S.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: University of Michigan Medical School, Dept. of Cell and Developmental Biology, 1335 Catherine St., Ann Arbor, MI 48109-0616. Tel.: 734-615-5670; Fax: 734-763-1166; E-mail: rbenndo{at}umich.edu.

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