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Emerin interacts in vitro with the splicing-associated factor, YT521-B.

http://www.ncbi.nlm.nih.gov/pubmed/12755701

Emerin is a nuclear membrane protein that interacts with lamin A/C at the nuclear envelope. Mutations in either emerin or lamin A/C cause Emery-Dreifuss muscular dystrophy (EDMD). The functions of emerin are poorly understood, but EDMD affects mainly skeletal and cardiac muscle. We used a high-stringency yeast two-hybrid method to screen a human heart cDNA library, with full-length emerin as bait. Four out of five candidate interactors identified were nuclear proteins: lamin A, splicing factor YT521-B, proteasome subunit PA28 gamma and transcription factor vav-1. Specific binding between emerin and the functional C-terminal domain of YT521-B was confirmed by pull-down assays and biomolecular interaction analysis (BIAcore). Inhibition by emerin of YT521-B-dependent splice site selection in vivo suggests that the interaction is physiologically significant. A 'bipartite' binding site for YT521-B in emerin was identified using alanine substitution or disease-associated mutations in emerin. The transcription factor GCL (germ cell-less) has previously been shown to bind to the same site. The results are consistent with an emerging view that lamins and lamina-associated proteins, like emerin, have a regulatory role, as well as a structural role in the nucleus. YT521-B joins a growing list of candidates for a role in a gene expression model of the pathogenesis of EDMD.

Pubmed ID: 12755701 RIS Download

Mesh terms: Binding Sites | Cell Nucleus | Cysteine Endopeptidases | DNA, Complementary | Drosophila Proteins | Gene Library | Genes, Reporter | Humans | In Vitro Techniques | Lamin Type A | Membrane Proteins | Multienzyme Complexes | Muscular Dystrophy, Emery-Dreifuss | Myocardium | Nerve Tissue Proteins | Nuclear Proteins | Open Reading Frames | Precipitin Tests | Proteasome Endopeptidase Complex | Protein Binding | Protein Structure, Tertiary | RNA | RNA Splicing | RNA, Messenger | RNA-Binding Proteins | Thymopoietins | Time Factors | Two-Hybrid System Techniques

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Associated grants

  • Agency: NHLBI NIH HHS, Id: T32 HL07227

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