Nesprin-1α self-associates and binds directly to emerin and lamin A in vitro

John M.K. Mislow, James M. Holaska, Marian S. Kim, Kenneth K. Lee, Miriam Segura-Totten, Katherine L. Wilson, Elizabeth M. McNally

Research output: Contribution to journalArticlepeer-review

207 Scopus citations

Abstract

Nesprin-1α is a spectrin repeat (SR)-containing, transmembrane protein of the inner nuclear membrane, and is highly expressed in muscle cells. A yeast two-hybrid screen for nesprin-1α-interacting proteins showed that nesprin-1α interacted with itself. Blot overlay experiments revealed that nesprin-1α's third SR binds the fifth SR. The carboxy-terminal half of nesprin-1α directly bound lamin A, a nuclear intermediate filament protein. Biochemical analysis demonstrated that nesprin-1α dimers bind directly to the nucleoplasmic domain of emerin, an inner nuclear membrane protein, with an affinity of 4 nM. Binding was optimal for full nucleoplasmic dimers of nesprin-1α, since nesprin fragments SR1-5 and SR5-7 bound emerin as monomers with affinities of 53 nM and 250 mM, respectively. We propose that membrane-anchored nesprin-1α antiparallel dimers interact with both emerin and lamin A to provide scaffolding at the inner nuclear membrane.

Original languageEnglish (US)
Pages (from-to)135-140
Number of pages6
JournalFEBS Letters
Volume525
Issue number1-3
DOIs
StatePublished - Aug 14 2002
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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