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

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


  • Wilkinson FL
  • Holaska JM
  • Zhang Z
  • Sharma A
  • Manilal S
  • Holt I
  • Stamm S
  • Wilson KL
  • Morris GE


European journal of biochemistry / FEBS

Publication Data

June 20, 2003

Associated Grants

  • Agency: NHLBI NIH HHS, Id: T32 HL07227

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