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Structural analysis of emerin, an inner nuclear membrane protein mutated in X‐linked Emery–Dreifuss muscular dystrophy
Author(s) -
Wolff Nicolas,
Gilquin Bernard,
Courchay Karine,
Callebaut Isabelle,
Worman Howard J.,
Zinn-Justin Sophie
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02649-7
Subject(s) - emerin , lamin , muscular dystrophy , inner membrane , nuclear lamina , biology , genetics , microbiology and biotechnology , nuclear protein , gene , transcription factor , membrane
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.