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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: 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

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1437-4315
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Volume 387, Issue 4

Issues

BID, an interaction partner of protein kinase CK2α

Birgitte B. Olsen
  • Institute for Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, DK-5230 Odense M, Denmark
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Jørgen Petersen / Olaf-Georg Issinger
  • Institute for Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, DK-5230 Odense M, Denmark
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2006-04-11 | DOI: https://doi.org/10.1515/BC.2006.059

Abstract

Recombinant murine BID protein was used as an in vitro substrate for the CK2 holoenzyme and the catalytic CK2α subunit. The results obtained show that BID can only serve as a substrate for the catalytic CK2α subunit. Phosphorylation of BID using the CK2 holoenzyme was only possible in the presence of polylysine, supporting the notion that BID behaves similarly to calmodulin. Co-immunoprecipitation of BID and CK2 subunits revealed that BID is preferentially associated with the CK2α subunit. Enzyme kinetic analyses yielded a K m value for BID that is a level of magnitude lower than that measured for casein and the synthetic peptide, suggesting more specific and tight binding of BID to CK2α. In contrast are the V max values observed, with a significantly higher phosphorylation rate measured for casein and the synthetic peptide than for BID. When BID was phosphorylated by polylysine-stimulated CK2 holoenzyme prior to caspase-8 cleavage, the formation of tC-BID was reduced in comparison to treatment with caspase-8 in the absence of protein kinase. Mass spectrometric analysis of BID phosphorylated by CK2α before and after cleavage with caspase-8 showed phosphorylation of residues Thr58 and Ser76.

Keywords: mass spectrometry; phosphorylation; polyamines; protein interaction

About the article

Corresponding author


Received: September 24, 2005

Accepted: January 27, 2006

Published Online: 2006-04-11

Published in Print: 2006-04-01


Citation Information: Biological Chemistry, Volume 387, Issue 4, Pages 441–449, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2006.059.

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