Nesprin-1alpha self-associates and binds directly to emerin and lamin A in vitro.
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.
Mesh Terms:
Carrier Proteins, DNA-Binding Proteins, Dimerization, Humans, Lamin Type A, Lamins, Membrane Proteins, Nerve Tissue Proteins, Nuclear Envelope, Nuclear Proteins, Peptide Fragments, Protein Binding, Protein Structure, Tertiary, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Thymopoietins, Transcription Factors, Two-Hybrid System Techniques
Carrier Proteins, DNA-Binding Proteins, Dimerization, Humans, Lamin Type A, Lamins, Membrane Proteins, Nerve Tissue Proteins, Nuclear Envelope, Nuclear Proteins, Peptide Fragments, Protein Binding, Protein Structure, Tertiary, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Thymopoietins, Transcription Factors, Two-Hybrid System Techniques
FEBS Lett.
Date: Aug. 14, 2002
PubMed ID: 12163176
View in: Pubmed Google Scholar
Download Curated Data For This Publication
8731
Switch View:
- Interactions 4