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Structural analysis of emerin, an inner nuclear membrane protein mutated in X-linked Emery-Dreifuss muscular dystrophy

Abstract : Like Duchenne and Becker muscular dystrophies, Emery-Dreifuss muscular dystrophy (EDMD) is characterized by myopathic and cardiomyopathic abnormalities. EDMD has the particularity of being linked to mutations in nuclear proteins. The X-linked form of EDMD is caused by mutations in the emerin gene, whereas autosomal dominant EDMD is caused by mutations in the lamin A/C gene. Emerin colocalizes with lamin A/C in interphase cells, and binds in vitro to lamin A/C. Recent work suggests that lamin A/C might serve as a receptor for emerin. We have undertaken a structural analysis of emerin, and in particular of its N-terminal domain, which is comprised in the emerin segment critical for binding to lamin A/C. We show that region 2-54 of emerin adopts the LEM fold. This fold was originally described in the two N-terminal domains of another inner nuclear membrane protein called lamina-associated protein 2 (LAP2). The existence of a conserved solvent-exposed surface on the LEM domains of LAP2 and emerin is discussed, as well as the nature of a possible common target.
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https://hal-pasteur.archives-ouvertes.fr/pasteur-02884040
Contributor : Nicolas Wolff <>
Submitted on : Monday, June 29, 2020 - 4:04:06 PM
Last modification on : Thursday, July 9, 2020 - 3:41:42 AM

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Nicolas Wolff, Bernard Gilquin, Karine Courchay, Isabelle Callebaut, Howard Worman, et al.. Structural analysis of emerin, an inner nuclear membrane protein mutated in X-linked Emery-Dreifuss muscular dystrophy. FEBS Letters, Wiley, 2001, 501 (2-3), pp.171-176. ⟨10.1016/s0014-5793(01)02649-7⟩. ⟨pasteur-02884040⟩

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