| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
|
|
|
|||||||
|
|||||||||
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Papers In Press, published online ahead of print August 31, 2004
JulesStein Eye Institute, UCLA School Of Medicine, Los Angeles, Ca 90095-7000
Corresponding Author: bhat{at}jsei.ucla.edu
J. Biol. Chem, 10.1074/jbc.C400371200
Submitted on August 5, 2004
Revised on August 20, 2004
Accepted on August 31, 2004
Small heat shock protein
B-crystallin is part of cell cycle dependent golgi reorganization
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 B-crystallin are known to be associated with a number of neurodegenerative pathologies such as Alzheimer’s disease and multiple sclerosis. Mutations in B-crystallin gene have been linked to DRM (desmin-related 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-associated fractions of B-crystallin, which co-sediment with the Golgi matrix protein, GM130. Confocal microscopy reveals colocalization of 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 aB-crystallin follows the disassembly of the Golgi at prometaphase and its reassembly at the completion of cell division and 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.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  P. Santhoshkumar and K. K. Sharma Conserved F84 and P86 residues in {alpha}B-crystallin are essential to effectively prevent the aggregation of substrate proteins. Protein Sci., November 1, 2006; 15(11): 2488 - 2498. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 C.-h. Xia, H. Liu, B. Chang, C. Cheng, D. Cheung, M. Wang, Q. Huang, J. Horwitz, and X. Gong Arginine 54 and Tyrosine 118 Residues of {alpha}A-Crystallin Are Crucial for Lens Formation and Transparency. Invest. Ophthalmol. Vis. Sci., July 1, 2006; 47(7): 3004 - 3010. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. den Engelsman, D. Gerrits, W. W. de Jong, J. Robbins, K. Kato, and W. C. Boelens Nuclear Import of {alpha}B-crystallin Is Phosphorylation-dependent and Hampered by Hyperphosphorylation of the Myopathy-related Mutant R120G J. Biol. Chem., November 4, 2005; 280(44): 37139 - 37148. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
F. Y. Lee, H. R. Kast-Woelbern, J. Chang, G. Luo, S. A. Jones, M. C. Fishbein, and P. A. Edwards {alpha}-Crystallin Is a Target Gene of the Farnesoid X-activated Receptor in Human Livers J. Biol. Chem., September 9, 2005; 280(36): 31792 - 31800. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 K.-S. Chae, K.-S. Oh, and S. E. Dryer Growth Factors Mobilize Multiple Pools of KCa Channels in Developing Parasympathetic Neurons: Role of ADP-Ribosylation Factors and Related Proteins J Neurophysiol, August 1, 2005; 94(2): 1597 - 1605. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
