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A more recent version of this article appeared on March 1, 2006
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Submitted on April 27, 2005
Accepted on December 6, 2005
Department of Cell Biology, Johns Hopkins University School of Medicine, Baltimore MD 21205
Monitoring Editor: Greg Matera
Barrier-to-Autointegration factor (BAF) is a conserved 10 kDa chromatin protein essential in proliferating cells. BAF dimers bind dsDNA, histone H3, histone H1.1, lamin A and transcription regulators, plus emerin and other LEM-domain nuclear proteins. Two-dimensional gel analysis showed that endogenous human and Xenopus BAF are posttranslationally modified by phosphorylation and potentially other modifications, and are hyperphosphorylated during mitosis. The invariant Ser-4 residue on BAF is a major site of phosphorylation during both interphase and mitosis. In HeLa cells that overexpressed the phospho-mimetic BAF missense mutant S4E, but not S4A, emerin mislocalized from the nuclear envelope, suggesting Ser-4-nonphosphorylated BAF normally promotes emerin localization at the nuclear envelope. Supporting this model wildtype BAF, but not mutant S4E, enhanced emerin binding to lamin A in vitro. Thus Ser-4-unphosphorylated BAF has a positive role in localizing emerin; this role may be disease-relevant since loss or mislocalization of emerin causes Emery-Dreifuss muscular dystrophy. Our findings further suggest Ser-4 phosphorylation inhibits BAF binding to emerin and lamin A, and thereby weakens emerin-lamin interactions during both mitosis and interphase.
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