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Published online July 7, 2008
doi:10.1083/jcb.200712124
The Journal of Cell Biology, Vol. 182, No. 1, 35-39
The Rockefeller University Press, 0021-9525 $30.00
© 2008 Zhang et al.
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 Sumoylation regulates lamin A function and is lost in lamin A mutants associated with familial cardiomyopathies

Yu-Qian Zhang and Kevin D. Sarge

Department of Molecular and Cellular Biochemistry, Chandler Medical Center, University of Kentucky, Lexington, KY 40536

Correspondence to Kevin Sarge: kdsarge{at}uky.edu

Lamin A mutations cause many diseases, including cardiomyopathies and Progeria Syndrome. The covalent attachment of small ubiquitin-like modifier (SUMO) polypeptides regulates the function of many proteins. Until now, no examples of human disease-causing mutations that occur within a sumoylation consensus sequence and alter sumoylation were known. We show that lamin A is sumoylated at lysine 201 and that two lamin A mutants associated with familial dilated cardiomyopathy, E203G and E203K, exhibit decreased sumoylation. E203 occupies the conserved +2 position in the sumoylation consensus {Psi}KXE. Lamin A mutants E203G, E203K, and K201R all exhibit a similar aberrant subcellular localization and are associated with increased cell death. Fibroblasts from an individual with the E203K lamin A mutation also exhibit decreased lamin A sumoylation and increased cell death. These results suggest that SUMO modification is important for normal lamin A function and implicate an involvement for altered sumoylation in the E203G/E203K lamin A cardiomyopathies.

Abbreviation used in this paper: SUMO, small ubiquitin-like modifier.


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Related In this Issue article

SUMO KEEPS LAMIN A IN PLACE
Richard Robinson
J. Cell Biol. 2008 182: 2. [Full Text] [PDF]



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