Lamina-associated polypeptide 2alpha forms complexes with heat shock proteins Hsp70 and Hsc70 in vivo |
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Authors: | Snyers Luc Schöfer Christian |
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Affiliation: | Center for Anatomy and Cell Biology, Medical University of Vienna, Schwarzspanierstrasse 17, A-1090 Vienna, Austria |
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Abstract: | Lamina-associated polypeptide 2α (LAP2α), one of the alternatively spliced isoforms of the LAP2 gene, is a nucleoplasmic protein which forms oligomers and presumably associates to chromosomes via the LEM- and LEM-like regions. To characterize components of the LAP2α-containing complexes, we have expressed the α-specific C-terminal domain of LAP2α in HeLa cells and, after immunopurification, found that the heat shock proteins Hsp70 and Hsc70 reproducibly co-purified with this domain. Association between endogenous LAP2α and Hsp70 in non-transfected cells was confirmed by co-immunoprecipitation. The association was not mediated by the retinoblastoma protein. |
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Keywords: | LEM, LAP2, Emerin, MAN1 BAF, Barrier-to-Autointegration Factor LAP, lamina-associated polypeptide PC, Protein C-epitope |
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