Editor-in-Chief: Brüne, Bernhard
Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred
SCImago Journal Rank (SJR) 2015: 1.607
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Characterization of rat BLOS2/Ceap, a putative yeast She3 homolog, as interaction partner of apoptosis antagonizing transcription factor/Che-1
1Institute of Genetics, University of Bonn, Roemerstr. 164, D-53117 Bonn, Germany
The first two authors contributed equally to this work.
2Institute of Genetics, University of Bonn, Roemerstr. 164, D-53117 Bonn, Germany
3Institute of Genetics, University of Bonn, Roemerstr. 164, D-53117 Bonn, Germany and Present address: Institute of Molecular Medicine and Experimental Immunology, University of Bonn, Sigmund-Freud-Str. 25, D-53105 Bonn, Germany.
4Institute of Genetics, University of Bonn, Roemerstr. 164, D-53117 Bonn, Germany
5Institute of Genetics, University of Bonn, Roemerstr. 164, D-53117 Bonn, Germany
Citation Information: Biological Chemistry. Volume 388, Issue 6, Pages 569–582, ISSN (Online) 14316730, ISSN (Print) 14374315, DOI: 10.1515/BC.2007.073, June 2007
- Published Online:
AATF/Che-1 is a coactivator of several transcription factors, including steroid hormone receptors. In search of novel interaction partners of AATF, we identified BLOS2 (BLOC1S2, also termed Ceap) from a rat cDNA library. BLOS2 is extremely conserved with a high degree of homology to yeast She3p. The clone isolated represents a splice variant encoding a polypeptide of 168 residues. Rat BLOS2 mRNA is highly expressed in brain and testis and at lower levels in other tissues, but not in skeletal or smooth muscle. Expression as a tagged fusion protein revealed predominant cytoplasmic, but also nuclear localization. In the cytoplasm, BLOS2 fusion proteins exhibit diffuse, filamentous, or dotted distribution, with the latter partially co-localizing with recycling endosomes. In addition, BLOS2 localizes to centrosomes or the pericentrosomal region. Moreover, BLOS2 co-localizes with myosin V globular tail domains in vesicle-like structures. However, a direct interaction could not be demonstrated. In transactivation assays, BLOS2 enhanced transcription from androgen receptor and p53-responsive promoters. However, this enhancement correlated with accumulation of both androgen receptor and p53, suggesting that BLOS2 has a stabilizing effect on these transcription factors. We propose that BLOS2 functions as an adapter in processes such as protein and vesicle processing and transport, and perhaps transcription.
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