Dissociation of Emerin from Barrier-to-autointegration Factor Is Regulated through Mitotic Phosphorylation of Emerin in a Xenopus Egg Cell-free System

• Published in: The Journal of biological chemistry Vol. 280; no. 48; pp. 39925 - 39933
• Main Authors: Hirano, Yasuhiro, Segawa, Masashi, Ouchi, Fumiko S., Yamakawa, Yoshio, Furukawa, Kazuhiro, Takeyasu, Kunio, Horigome, Tsuneyoshi
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 02.12.2005; American Society for Biochemistry and Molecular Biology
• Subjects: Animals; Cell Cycle; Cell-Free System; Chromatin - chemistry; Chromatin - metabolism; Chymotrypsin - chemistry; Cytosol - metabolism; DNA-Binding Proteins - metabolism; Glutathione Transferase - metabolism; Humans; Mass Spectrometry; Membrane Proteins - metabolism; Mitosis; Muscular Dystrophy, Emery-Dreifuss - genetics; Muscular Dystrophy, Emery-Dreifuss - metabolism; Mutation; Nuclear Proteins - metabolism; Oocytes - metabolism; Peptides - chemistry; Phosphopeptides - chemistry; Phosphorylation; Point Mutation; Protein Binding; Recombinant Fusion Proteins - chemistry; Serine - chemistry; Spectrometry, Mass, Electrospray Ionization; Thymopoietins - metabolism; Trypsin - chemistry; Xenopus

Emerin is the gene product of STA whose mutations cause Emery-Dreifuss muscular dystrophy. It is an inner nuclear membrane protein and phosphorylated in a cell cycle-dependent manner. However, the means of phosphorylation of emerin are poorly understood. We investigated the regulation mechanism for...