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Originally published In Press as doi:10.1074/jbc.C400371200 on August 31, 2004

J. Biol. Chem., Vol. 279, Issue 42, 43374-43377, October 15, 2004
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Small Heat Shock Protein {alpha}B-Crystallin Is Part of Cell Cycle-dependent Golgi Reorganization*

Rajendra K. Gangalum{ddagger}, Matthew J. Schibler§, and Suraj P. Bhat{ddagger}§¶||

From the {ddagger}Jules Stein Eye Institute, §Brain Research Institute, Geffen School of Medicine and Molecular Biology Institute, University of California, Los Angeles, California 90095-7000

{alpha}B-Crystallin is a developmentally regulated small heat shock protein known for its binding to a variety of denatured polypeptides and suppression of protein aggregation in vitro. Elevated levels of {alpha}B-crystallin are known to be associated with a number of neurodegenerative pathologies such as Alzheimer disease and multiple sclerosis. Mutations in {alpha}B-crystallin gene have been linked to desminrelated cardiomyopathy and cataractogenesis. The physiological function of this protein, however, is unknown. Using discontinuous sucrose density gradient fractionation of post-nuclear supernatants, prepared from rat tissues and human glioblastoma cell line U373MG, we have identified discrete membrane-bound fractions of {alpha}B-crystallin, which co-sediment with the Golgi matrix protein, GM130. Confocal microscopy reveals co-localization of {alpha}B-crystallin with BODIPY TR ceramide and the Golgi matrix protein, GM130, in the perinuclear Golgi in human glioblastoma U373MG cells. Examination of synchronized cultures indicated that {alpha}B-crystallin follows disassembly of the Golgi at prometaphase and its reassembly at the completion of cytokinesis, suggesting that this small heat shock protein, with its chaperone-like activity, may have an important role in the Golgi reorganization during cell division.


Received for publication, August 5, 2004 , and in revised form, August 20, 2004.

* This work was supported by NEI/National Institutes of Health grants (to S. P. B.). 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.

|| A Research to Prevent Blindness Inc., Wasserman Merit Scholar. To whom correspondence should be addressed: Vision Molecular Biology Laboratory, Jules Stein Eye Inst., BH 623, Geffen School of Medicine at UCLA, Los Angeles, CA 90095-7000. Tel.: 310-825-9543; Fax: 310-794-2144; E-mail: bhat{at}jsei.ucla.edu.


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