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This protein was first identified as being an actin-binding protein as it was purified from an activity originally attributed to vinculin with which it co-purified (Miron et al, 1991).  The discovery of actin polymerization inhibition in vinculin preparation at the time lead some to discount vinculin as an actin-binding protein, however, the situation has now been clarified by the study of recombinant fragments of vinculin that firmly established that vinculin is in fact an ABP. 

The actin binding region of HSP27 has been determined as being W43-R57 and I92-N106 (Wieske et al, 2001). The association with F-actin in vitro may be phosphorylation dependent (Geum et al, 2002).



Der Perng, M., Cairns, L., van den Ijssel, P., Prescott, A., Hutcheson, A. M. & Quinlan, R. A. (1999) Intermediate filament interactions can be altered by HSP27 and aB-crystalin., J.Cell Sci. 112, 2099-2112.

Geum, D., Son, G. H. & Kim, K. (2002) Phosphorylation-dependent cellular localization and thermoprotective role of heat shock protein 25 in hippocampal progenitor cells. J.Biol.Chem. 277, 19913-19921

Mehlen, P., Kretz-Remy, C., Briolay, J., Fostan, P., Mirault, M. & Arrigo, A. (1995) Intracellular reactive oxygen species as apparent modulators of heat-shock protein 27 (HSP27) structural organization and phosphorylation in basal and tumour necrosis factor a-treated T47D human carcinoma cells., Biochem. J. 312, 367-375.

Wieske, M., Benndorf, R., Behlke, J., Dolling, R., Grelle, G., Bielka, H. & Lutsch, G. (2001) Defined sequence segments of the small heat shock proteins HSP25 and ab-crystalin inhibit actin polymerization, Eur.J.Biochem. 268, 2083-2090.

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