Abstract:
The R120G mutation in the small heat shock protein (sHSP) αB-crystallin has been identified in a family suffering from desmin-related myopathy. In this study, we characterized the features of transiently expressed R120GαB-crystallin in mammalian cells. In addition, we examined interactions of this mutant αB-crystallin with Hsp27, another representative sHSP. In HeLa cells, transiently expressed R120GαB-crystallin was mainly fractionated in the insoluble fraction, although wild-type αB-crystallin was predominantly found in the soluble fraction. In immunofluorescence studies, we found 15–25% of R120GαB-crystallin-expressing cells to contain multiple cytosolic inclusion bodies, in which Hsp27 was also localized. When R120GαB-crystallin and Hsp27 were transiently co-expressed in HeLa cells, the amount of R120GαB-crystallin in the soluble fraction was greater than with expression of R120GαB-crystallin alone. Moreover, co-expression resulted in reduced formation of inclusion bodies, suggesting that Hsp27 acts as a molecular chaperone for R120GαB-crystallin.
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Received 16 January 2003; received after revision 19 February 2003; accepted 24 March 2003
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Ito, H., Kamei, K., Iwamoto, I. et al. Hsp27 suppresses the formation of inclusion bodies induced by expression of R120GαB-crystallin, a cause of desmin-related myopathy. CMLS, Cell. Mol. Life Sci. 60, 1217–1223 (2003). https://doi.org/10.1007/s00018-003-3024-9
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DOI: https://doi.org/10.1007/s00018-003-3024-9