TAILIEUCHUNG - Báo cáo Y học: The Emery–Dreifuss muscular dystrophy associated-protein emerin is phosphorylated on serine 49 by protein kinase A

Emerin is a ubiquitously expressed inner nuclear membrane protein of unknown function. Mutations in its gene give rise to X-linked Emery–Drei-fuss muscular dystrophy (X-EDMD), a neuromuscular condition with an associated life-threatening cardiomyopathy. We have previously reported that emerin is phosphorylated in a cell cycle-dependent manner in human lymphoblastoid cell lines [Ellis et al. (1998) Aberrant intracellular targeting and cell cycle-dependent phosphorylation of emerin contribute to the EDMD . Cell Sci. 111, 781–792]. . | sFEBS Journal The Emery-Dreifuss muscular dystrophy associated-protein emerin is phosphorylated on serine 49 by protein kinase A Rhys C. Roberts1 i Andrew J. Sutherland-Smith1 i Matthew A. Wheeler2 Ole Norregaard Jensen3 Lindsay J. Emerson2 Ioannis I. Spiliotis2 Christopher G. Tate1 John Kendrick-Jones1 and Juliet A. Ellis2 1 MRC Laboratory of Molecular Biology Cambridge UK 2 The RandallDivision of Celland Molecular Biophysics Kings College London UK 3 Protein Research Group Department of Biochemistry and Molecular Biology University of Southern Denmark Odense Denmark Keywords emerin Emery-Dreifuss muscular dystrophy mass spectrometry phosphorylation protein kinase A Correspondence J. A. Ellis The RandallDivision of Celland Molecular Biophysics Kings College New Hunts House Guy s Campus London SE1 1UL UK Fax 44 20 78486435 Tel 44 20 78486498 E-mail Present address The NationalHospitalfor Neurology and Neurosurgery London UK Institute of Molecular Biosciences Massey University Palmerston North New Zealand These authors contributed equally to this work Received 23 May 2006 revised 27 July 2006 accepted 14 August 2006 doi Emerin is a ubiquitously expressed inner nuclear membrane protein of unknown function. Mutations in its gene give rise to X-linked Emery-Drei-fuss muscular dystrophy X-EDMD a neuromuscular condition with an associated life-threatening cardiomyopathy. We have previously reported that emerin is phosphorylated in a cell cycle-dependent manner in human lymphoblastoid cell lines Ellis et al. 1998 Aberrant intracellular targeting and cell cycle-dependent phosphorylation of emerin contribute to the EDMD phenotype. J. Cell Sci. 111 781-792 . Recently five residues in human emerin were identified as undergoing cell cycle-dependent phosphorylation using a Xenopus egg mitotic cytosol model system Hirano et al. 2005 Dissociation of emerin from BAF is regulated through mitotic phosphorylation of emerin in a

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