Interaction of human HSP22 (HSPB8) with other small heat shock proteins
- PMID: 14594798
- DOI: 10.1074/jbc.M311324200
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.
Similar articles
-
Interactions of HSP22 (HSPB8) with HSP20, alphaB-crystallin, and HSPB3.Biochem Biophys Res Commun. 2005 Nov 25;337(3):1006-11. doi: 10.1016/j.bbrc.2005.09.148. Epub 2005 Oct 3. Biochem Biophys Res Commun. 2005. PMID: 16225851
-
Abnormal small heat shock protein interactions involving neuropathy-associated HSP22 (HSPB8) mutants.FASEB J. 2006 Oct;20(12):2168-70. doi: 10.1096/fj.06-5911fje. Epub 2006 Aug 25. FASEB J. 2006. PMID: 16935933
-
Induction of Hsp22 (HspB8) by estrogen and the metalloestrogen cadmium in estrogen receptor-positive breast cancer cells.Cell Stress Chaperones. 2007 Winter;12(4):307-19. doi: 10.1379/csc-276.1. Cell Stress Chaperones. 2007. PMID: 18229450 Free PMC article.
-
Small heat shock proteins HSP27 (HspB1), αB-crystallin (HspB5) and HSP22 (HspB8) as regulators of cell death.Int J Biochem Cell Biol. 2012 Oct;44(10):1622-31. doi: 10.1016/j.biocel.2012.04.002. Epub 2012 Apr 13. Int J Biochem Cell Biol. 2012. PMID: 22521623 Review.
-
Structure, properties, and functions of the human small heat-shock protein HSP22 (HspB8, H11, E2IG1): a critical review.J Neurosci Res. 2008 Feb 1;86(2):264-9. doi: 10.1002/jnr.21441. J Neurosci Res. 2008. PMID: 17722063 Review.
Cited by
-
The Role of Small Heat Shock Proteins in Protein Misfolding Associated Motoneuron Diseases.Int J Mol Sci. 2022 Oct 4;23(19):11759. doi: 10.3390/ijms231911759. Int J Mol Sci. 2022. PMID: 36233058 Free PMC article. Review.
-
Small heat shock proteins are necessary for heart migration and laterality determination in zebrafish.Dev Biol. 2013 Dec 15;384(2):166-80. doi: 10.1016/j.ydbio.2013.10.009. Epub 2013 Oct 17. Dev Biol. 2013. PMID: 24140541 Free PMC article.
-
Neuromuscular Diseases Due to Chaperone Mutations: A Review and Some New Results.Int J Mol Sci. 2020 Feb 19;21(4):1409. doi: 10.3390/ijms21041409. Int J Mol Sci. 2020. PMID: 32093037 Free PMC article. Review.
-
Mammalian Hsp22 is a heat-inducible small heat-shock protein with chaperone-like activity.Biochem J. 2004 Jul 15;381(Pt 2):379-87. doi: 10.1042/BJ20031958. Biochem J. 2004. PMID: 15030316 Free PMC article.
-
Comparison of the small heat shock proteins alphaB-crystallin, MKBP, HSP25, HSP20, and cvHSP in heart and skeletal muscle.Histochem Cell Biol. 2004 Nov;122(5):415-25. doi: 10.1007/s00418-004-0711-z. Epub 2004 Oct 12. Histochem Cell Biol. 2004. PMID: 15480735
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Molecular Biology Databases
Research Materials
Miscellaneous