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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).
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References:-
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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