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Gewählte Publikation:

Snyers, L; Vlcek, S; Dechat, T; Skegro, D; Korbei, B; Gajewski, A; Mayans, O; Schöfer, C; Foisner, R.
(2007): Lamina-associated polypeptide 2-alpha forms homo-trimers via its C terminus, and oligomerization is unaffected by a disease-causing mutation.
J Biol Chem. 2007; 282(9):6308-6315 FullText FullText_BOKU

The nucleoplasmic protein, Lamina-associated polypeptide (LAP) 2 alpha, 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, LAP2 alpha has a large unique C-terminal region that contains binding sites for chromatin, A-type lamins, and retinoblastorna protein. By immunoprecipitation analyses of LAP2a complexes from cells expressing differently tagged LAP2 alpha proteins and fragments, we demonstrate that LAP21y forms higher order structures containing multiple LAP2 alpha molecules in vivo and that complex formation is mediated by the C terminus. Solid phase binding assays using recombinant and in vitro translated LAP2 alpha fragments showed direct interactions of LAP2 alpha C termini. Cross-linking of LAP2 alpha complexes and multiangle light-scattering of purified LAP2 alpha revealed the existence of stable homo-trimers in vivo and in vitro. Finally, we show that, in contrast to the LAP2 alpha-lamin A interaction, its self-association is not affected by a disease-linked single point mutation in the LAP2 alpha C terminus.
Autor*innen der BOKU Wien:
Korbei Barbara
Find related publications in this database (using NML MeSH Indexing)
Binding Sites -
DNA-Binding Proteins - genetics
Dimerization -
HeLa Cells -
Humans -
Immunoprecipitation -
Lamin Type A - metabolism
Membrane Proteins - genetics
Mutation -
Protein Binding -
Protein Interaction Mapping -

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