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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

12 Issues per year


IMPACT FACTOR 2016: 3.273

CiteScore 2016: 3.01

SCImago Journal Rank (SJR) 2016: 1.679
Source Normalized Impact per Paper (SNIP) 2016: 0.800

Online
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1437-4315
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Volume 388, Issue 6 (Jun 2007)

Issues

Characterization of rat BLOS2/Ceap, a putative yeast She3 homolog, as interaction partner of apoptosis antagonizing transcription factor/Che-1

Andrea Felten
  • 1Institute of Genetics, University of Bonn, Roemerstr. 164, D-53117 Bonn, Germany
    The first two authors contributed equally to this work.
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Peter Leister / Sven Burgdorf
  • 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.
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Lutz Uhlmann / Karl Heinz Scheidtmann
Published Online: 2007-06-01 | DOI: https://doi.org/10.1515/BC.2007.073

Abstract

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.

Keywords: AATF/Che-1; androgen receptor; BLOC1S2/Ceap/RSEP; myosin V; p53; She3p

About the article

Corresponding author


Received: 2006-10-24

Accepted: 2007-03-19

Published Online: 2007-06-01


Citation Information: Biological Chemistry, ISSN (Online) 14316730, ISSN (Print) 14374315, DOI: https://doi.org/10.1515/BC.2007.073.

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