Nesprin-1alpha self-associates and binds directly to emerin and lamin A in vitro.
FEBS Lett
; 525(1-3): 135-40, 2002 Aug 14.
Article
en En
| MEDLINE
| ID: mdl-12163176
ABSTRACT
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.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Timopoyetinas
/
Proteínas Nucleares
/
Proteínas Portadoras
/
Proteínas de Saccharomyces cerevisiae
/
Proteínas de la Membrana
/
Proteínas del Tejido Nervioso
Tipo de estudio:
Risk_factors_studies
Límite:
Humans
Idioma:
En
Revista:
FEBS Lett
Año:
2002
Tipo del documento:
Article
País de afiliación:
Estados Unidos