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http://purl.uniprot.org/citations/10984438http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10984438http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10984438http://www.w3.org/2000/01/rdf-schema#comment"The nucleoskeletal protein lamina-associated polypeptide 2(&agr;) (LAP2*) contains a large, unique C terminus and differs significantly from its alternatively spliced, mostly membrane-integrated isoforms, such as LAP2beta. Unlike lamin B-binding LAP2beta, LAP2alpha was found by confocal immunofluorescence microscopy to colocalize preferentially with A-type lamins in the newly formed nuclei assembled after mitosis. While only a subfraction of lamins A and C (lamin A/C) was associated with the predominantly nuclear LAP2alpha in telophase, the majority of lamin A/C colocalized with LAP2alpha in G(1)-phase nuclei. Furthermore, selective disruption of A-type lamin structures by overexpression of lamin mutants in HeLa cells caused a redistribution of LAP2alpha. Coimmunoprecipitation experiments revealed that a fraction of lamin A/C formed a stable, SDS-resistant complex with LAP2alpha in interphase cells and in postmetaphase cell extracts. Blot overlay binding studies revealed a direct binding of LAP2alpha to exclusively A-type lamins and located the interaction domains to the C-terminal 78 amino acids of LAP2alpha and to residues 319-566 in lamin A/C, which include the C terminus of the rod and the entire tail common to lamin A/C. These findings suggest that LAP2alpha and A-type lamins cooperate in the organization of internal nuclear structures."xsd:string
http://purl.uniprot.org/citations/10984438http://purl.org/dc/terms/identifier"doi:10.1242/jcs.113.19.3473"xsd:string
http://purl.uniprot.org/citations/10984438http://purl.org/dc/terms/identifier"doi:10.1242/jcs.113.19.3473"xsd:string
http://purl.uniprot.org/citations/10984438http://purl.uniprot.org/core/author"Foisner R."xsd:string
http://purl.uniprot.org/citations/10984438http://purl.uniprot.org/core/author"Foisner R."xsd:string
http://purl.uniprot.org/citations/10984438http://purl.uniprot.org/core/author"Korbei B."xsd:string
http://purl.uniprot.org/citations/10984438http://purl.uniprot.org/core/author"Korbei B."xsd:string
http://purl.uniprot.org/citations/10984438http://purl.uniprot.org/core/author"Hutchison C.J."xsd:string
http://purl.uniprot.org/citations/10984438http://purl.uniprot.org/core/author"Hutchison C.J."xsd:string
http://purl.uniprot.org/citations/10984438http://purl.uniprot.org/core/author"Vaughan O.A."xsd:string
http://purl.uniprot.org/citations/10984438http://purl.uniprot.org/core/author"Vaughan O.A."xsd:string
http://purl.uniprot.org/citations/10984438http://purl.uniprot.org/core/author"Dechat T."xsd:string
http://purl.uniprot.org/citations/10984438http://purl.uniprot.org/core/author"Dechat T."xsd:string
http://purl.uniprot.org/citations/10984438http://purl.uniprot.org/core/author"Vlcek S."xsd:string
http://purl.uniprot.org/citations/10984438http://purl.uniprot.org/core/author"Vlcek S."xsd:string
http://purl.uniprot.org/citations/10984438http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10984438http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10984438http://purl.uniprot.org/core/name"J. Cell Sci."xsd:string
http://purl.uniprot.org/citations/10984438http://purl.uniprot.org/core/name"J. Cell Sci."xsd:string
http://purl.uniprot.org/citations/10984438http://purl.uniprot.org/core/pages"3473-3484"xsd:string
http://purl.uniprot.org/citations/10984438http://purl.uniprot.org/core/pages"3473-3484"xsd:string
http://purl.uniprot.org/citations/10984438http://purl.uniprot.org/core/title"Lamina-associated polypeptide 2alpha binds intranuclear A-type lamins."xsd:string
http://purl.uniprot.org/citations/10984438http://purl.uniprot.org/core/title"Lamina-associated polypeptide 2alpha binds intranuclear A-type lamins."xsd:string