Literature DB >> 12615927

Interaction of the anaphase-promoting complex/cyclosome and proteasome protein complexes with multiubiquitin chain-binding proteins.

Michael Seeger1, Rasmus Hartmann-Petersen, Caroline R M Wilkinson, Mairi Wallace, Itaru Samejima, Martin S Taylor, Colin Gordon.   

Abstract

Fission yeast Rhp23 and Pus1 represent two families of multiubiquitin chain-binding proteins that associate with the proteasome. We show that both proteins bind to different regions of the proteasome subunit Mts4. The binding site for Pus1 was mapped to a cluster of repetitive sequences also found in the proteasome subunit SpRpn2 and the anaphase-promoting complex/cyclosome (APC/C) subunit Cut4. The putative role of Pus1 as a factor involved in allocation of ubiquitinylated substrates for the proteasome is discussed.

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Year:  2003        PMID: 12615927     DOI: 10.1074/jbc.M208281200

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  26 in total

1.  Multiple interactions of rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysis.

Authors:  Ikjin Kim; Kaixia Mi; Hai Rao
Journal:  Mol Biol Cell       Date:  2004-04-30       Impact factor: 4.138

Review 2.  Getting into position: the catalytic mechanisms of protein ubiquitylation.

Authors:  Lori A Passmore; David Barford
Journal:  Biochem J       Date:  2004-05-01       Impact factor: 3.857

3.  Localization of the proteasomal ubiquitin receptors Rpn10 and Rpn13 by electron cryomicroscopy.

Authors:  Eri Sakata; Stefan Bohn; Oana Mihalache; Petra Kiss; Florian Beck; Istvan Nagy; Stephan Nickell; Keiji Tanaka; Yasushi Saeki; Friedrich Förster; Wolfgang Baumeister
Journal:  Proc Natl Acad Sci U S A       Date:  2012-01-03       Impact factor: 11.205

4.  Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach.

Authors:  Keren Lasker; Friedrich Förster; Stefan Bohn; Thomas Walzthoeni; Elizabeth Villa; Pia Unverdorben; Florian Beck; Ruedi Aebersold; Andrej Sali; Wolfgang Baumeister
Journal:  Proc Natl Acad Sci U S A       Date:  2012-01-23       Impact factor: 11.205

5.  Rpn1 and Rpn2 coordinate ubiquitin processing factors at proteasome.

Authors:  Rina Rosenzweig; Vered Bronner; Daoning Zhang; David Fushman; Michael H Glickman
Journal:  J Biol Chem       Date:  2012-02-08       Impact factor: 5.157

6.  Toward an integrated structural model of the 26S proteasome.

Authors:  Friedrich Förster; Keren Lasker; Stephan Nickell; Andrej Sali; Wolfgang Baumeister
Journal:  Mol Cell Proteomics       Date:  2010-05-13       Impact factor: 5.911

Review 7.  Regulation of proteasome activity in health and disease.

Authors:  Marion Schmidt; Daniel Finley
Journal:  Biochim Biophys Acta       Date:  2013-08-27

8.  Association of Rpn10 with high molecular weight complex is enhanced during retinoic acid-induced differentiation of neuroblastoma cells.

Authors:  Yoko Tayama; Hiroyuki Kawahara; Ryosuke Minami; Masumi Shimada; Hideyoshi Yokosawa
Journal:  Mol Cell Biochem       Date:  2007-08-01       Impact factor: 3.396

9.  Extraproteasomal Rpn10 restricts access of the polyubiquitin-binding protein Dsk2 to proteasome.

Authors:  Yulia Matiuhin; Donald S Kirkpatrick; Inbal Ziv; Woong Kim; Arun Dakshinamurthy; Oded Kleifeld; Steven P Gygi; Noa Reis; Michael H Glickman
Journal:  Mol Cell       Date:  2008-11-07       Impact factor: 17.970

10.  UBL/BAG-domain co-chaperones cause cellular stress upon overexpression through constitutive activation of Hsf1.

Authors:  Esben G Poulsen; Caroline Kampmeyer; Franziska Kriegenburg; Jens V Johansen; Kay Hofmann; Christian Holmberg; Rasmus Hartmann-Petersen
Journal:  Cell Stress Chaperones       Date:  2016-12-14       Impact factor: 3.667

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