Molecular Biology of the Cell click for ASCB 2009 Annual Meeting page

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
QUICK SEARCH:   [advanced]


     

Originally published as MBC in Press, 10.1091/mbc.E08-05-0511 on October 22, 2008

Vol. 20, Issue 1, 410-418, January 1, 2009

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental Materials
Right arrow All Versions of this Article:
E08-05-0511v1
20/1/410    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Klein, U. R.
Right arrow Articles by Muller, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Klein, U. R.
Right arrow Articles by Muller, S.

RanBP2 and SENP3 Function in a Mitotic SUMO2/3 Conjugation-Deconjugation Cycle on Borealin

Ulf R. Klein*, Markus Haindl{dagger}, Erich A. Nigg*, and Stefan Muller{dagger}

*Departments of Cell Biology and {dagger}Molecular Cell Biology, Max Planck Institute of Biochemistry, D-82152 Martinsried, Germany

Submitted May 22, 2008; Revised October 8, 2008; Accepted October 14, 2008
Monitoring Editor: Yixian Zheng

The ubiquitin-like SUMO system controls cellular key functions, and several lines of evidence point to a critical role of SUMO for mitotic progression. However, in mammalian cells mitotic substrates of sumoylation and the regulatory components involved are not well defined. Here, we identify Borealin, a component of the chromosomal passenger complex (CPC), as a mitotic target of SUMO. The CPC, which additionally comprises INCENP, Survivin, and Aurora B, regulates key mitotic events, including chromosome congression, the spindle assembly checkpoint, and cytokinesis. We show that Borealin is preferentially modified by SUMO2/3 and demonstrate that the modification is dynamically regulated during mitotic progression, peaking in early mitosis. Intriguingly, the SUMO ligase RanBP2 interacts with the CPC, stimulates SUMO modification of Borealin in vitro, and is required for its modification in vivo. Moreover, the SUMO isopeptidase SENP3 is a specific interaction partner of Borealin and catalyzes the removal of SUMO2/3 from Borealin. These data thus delineate a mitotic SUMO2/3 conjugation–deconjugation cycle of Borealin and further assign a regulatory function of RanBP2 and SENP3 in the mitotic SUMO pathway.

This was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E08-05-0511) on October 22, 2008.

Address correspondence to: Stefan Muller (stmuelle{at}biochem.mpg.de).




This article has been cited by other articles:


Home page
 Mol. Cell. ProteomicsHome page
H. A. Blomster, V. Hietakangas, J. Wu, P. Kouvonen, S. Hautaniemi, and L. Sistonen
Novel Proteomics Strategy Brings Insight into the Prevalence of SUMO-2 Target Sites
Mol. Cell. Proteomics, June 1, 2009; 8(6): 1382 - 1390.
[Abstract] [Full Text] [PDF]


Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Copyright © 2009 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.