| Article ID | Journal | Published Year | Pages | File Type | 
|---|---|---|---|---|
| 1936205 | Biochemical and Biophysical Research Communications | 2008 | 5 Pages | 
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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											Authors
												Luc Snyers, Christian Schöfer, 
											