Journal
FEBS LETTERS
Volume 525, Issue 1-3, Pages 135-140Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(02)03105-8
Keywords
spectrin repeat; crosslinker; inner nuclear membrane; lamin A/C; emerin; nuclear enveloped; Emery-Dreifuss muscular dystrophy
Funding
- NHLBI NIH HHS [HL63783, HL-07237] Funding Source: Medline
- NICHD NIH HHS [HD-07009] Funding Source: Medline
- NIGMS NIH HHS [GM48646] Funding Source: Medline
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Nesprin-1alpha 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-1alpha-interacting proteins showed that nesprin-1alpha interacted with itself. Blot overlay experiments revealed that nesprin-1alpha's third SR binds the fifth SR. The carboxy-terminal half of nesprin-1alpha directly bound lamin A, a nuclear intermediate filament protein. Biochemical analysis demonstrated that nesprin-1alpha 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-1alpha, 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-1alpha antiparallel dimers interact with both emerin and lamin A to provide scaffolding at the inner nuclear membrane. (C) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
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