Article
Lamina-associated polypeptide 2-alpha forms homo-trimers via its C terminus, and oligomerization is unaffected by a disease-causing mutation.
The Journal of biological chemistry - 2 Mar 2007
Snyers Luc, Vlcek Sylvia, Dechat Thomas, Skegro Darko, Korbei Barbara, Gajewski Andreas, Mayans Olga, Schöfer Christian, Foisner Roland
Abstract excerpt
The nucleoplasmic protein, Lamina-associated polypeptide (LAP) 2alpha, is one of six alternatively spliced products of the LAP2gene, which share a common N-terminal region. In contrast to the other isoforms, which also share most of their C termini, LAP2alpha has a large unique C-terminal region that contains binding sites for chromatin, A-type lamins, and retinoblastoma protein. By immunoprecipitation analyses...
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