Advertisement
MCP
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Originally published In Press as doi:10.1074/mcp.M700173-MCP200 on October 15, 2007.
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental Data
Right arrow All Versions of this Article:
M700173-MCP200v1
7/1/132    most recent
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
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 arrowRequest Permissions
Right arrow Glossary
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Matic, I.
Right arrow Articles by Vertegaal, A. C. O.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Matic, I.
Right arrow Articles by Vertegaal, A. C. O.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Molecular & Cellular Proteomics 7:132-144, 2008.
© 2008 by The American Society for Biochemistry and Molecular Biology, Inc.


Research

In Vivo Identification of Human Small Ubiquitin-like Modifier Polymerization Sites by High Accuracy Mass Spectrometry and an in Vitro to in Vivo Strategy*,S

Ivan Matic{ddagger},§, Martijn van Hagen§, Joost Schimmel, Boris Macek{ddagger}, Stephen C. Ogg||, Michael H. Tatham**, Ronald T. Hay**, Angus I. Lamond**,{ddagger}{ddagger}, Matthias Mann{ddagger},§§ and Alfred C. O. Vertegaal,¶¶

From the {ddagger} Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany, Department of Molecular Cell Biology, Leiden University Medical Center, 2300 RC Leiden, the Netherlands, || Centre for Molecular Medicine, 61 Biopolis Drive (Proteos), Singapore 138673, Singapore, and ** Wellcome Trust Biocentre, University of Dundee, Dundee DD1 5EH, United Kingdom

The length and precise linkage of polyubiquitin chains is important for their biological activity. Although other ubiquitin-like proteins have the potential to form polymeric chains their identification in vivo is challenging and their functional role is unclear. Vertebrates express three small ubiquitin-like modifiers, SUMO-1, SUMO-2, and SUMO-3. Mature SUMO-2 and SUMO-3 are nearly identical and contain an internal consensus site for sumoylation that is missing in SUMO-1. Combining state-of-the-art mass spectrometry with an "in vitro to in vivo" strategy for post-translational modifications, we provide direct evidence that SUMO-1, SUMO-2, and SUMO-3 form mixed chains in cells via the internal consensus sites for sumoylation in SUMO-2 and SUMO-3. In vitro, the chain length of SUMO polymers could be influenced by changing the relative amounts of SUMO-1 and SUMO-2. The developed methodology is generic and can be adapted for the identification of other sumoylation sites in complex samples.


§§ To whom correspondence may be addressed. Tel.: 49-89-8578-2557; Fax: 49-89-8578-2219; E-mail: mmann{at}biochem.mpg.de

¶¶ To whom correspondence may be addressed. Tel.: 31-71-526-9621; Fax: 31-7-526-8270; E-mail: vertegaal{at}lumc.nl


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
J. Cell Sci.Home page
M. Lang, T. Jegou, I. Chung, K. Richter, S. Munch, A. Udvarhelyi, C. Cremer, P. Hemmerich, J. Engelhardt, S. W. Hell, et al.
Three-dimensional organization of promyelocytic leukemia nuclear bodies
J. Cell Sci., February 1, 2010; 123(3): 392 - 400.
[Abstract] [Full Text] [PDF]


Home page
DevelopmentHome page
K.-o. Srilunchang, N. G. Krohn, and T. Dresselhaus
DiSUMO-like DSUL is required for nuclei positioning, cell specification and viability during female gametophyte maturation in maize
Development, January 15, 2010; 137(2): 333 - 345.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
Y. Wang and M. Dasso
SUMOylation and deSUMOylation at a glance
J. Cell Sci., December 1, 2009; 122(23): 4249 - 4252.
[Full Text] [PDF]


Home page
Mol. Cell. ProteomicsHome page
H.-H. Hsiao, E. Meulmeester, B. T. C. Frank, F. Melchior, and H. Urlaub
"ChopNSpice," a Mass Spectrometric Approach That Allows Identification of Endogenous Small Ubiquitin-like Modifier-conjugated Peptides
Mol. Cell. Proteomics, December 1, 2009; 8(12): 2664 - 2675.
[Abstract] [Full Text] [PDF]


Home page
FASEB J.Home page
C. Figueroa-Romero, J. A. Iniguez-Lluhi, J. Stadler, C.-R. Chang, D. Arnoult, P. J. Keller, Y. Hong, C. Blackstone, and E. L. Feldman
SUMOylation of the mitochondrial fission protein Drp1 occurs at multiple nonconsensus sites within the B domain and is linked to its activity cycle
FASEB J, November 1, 2009; 23(11): 3917 - 3927.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. ProteomicsHome page
V. Matafora, A. D'Amato, S. Mori, F. Blasi, and A. Bachi
Proteomics Analysis of Nucleolar SUMO-1 Target Proteins upon Proteasome Inhibition
Mol. Cell. Proteomics, October 1, 2009; 8(10): 2243 - 2255.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
R. Zunino, E. Braschi, L. Xu, and H. M. McBride
Translocation of SenP5 from the Nucleoli to the Mitochondria Modulates DRP1-dependent Fission during Mitosis
J. Biol. Chem., June 26, 2009; 284(26): 17783 - 17795.
[Abstract] [Full Text] [PDF]


Home page
Sci SignalHome page
F. Golebiowski, I. Matic, M. H. Tatham, C. Cole, Y. Yin, A. Nakamura, J. Cox, G. J. Barton, M. Mann, and R. T. Hay
System-Wide Changes to SUMO Modifications in Response to Heat Shock
Sci. Signal., May 26, 2009; 2(72): ra24 - ra24.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. ProteomicsHome page
J. Schimmel, K. M. Larsen, I. Matic, M. van Hagen, J. Cox, M. Mann, J. S. Andersen, and A. C. O. Vertegaal
The Ubiquitin-Proteasome System Is a Key Component of the SUMO-2/3 Cycle
Mol. Cell. Proteomics, November 1, 2008; 7(11): 2107 - 2122.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. ProteomicsHome page
L. F. Waanders, R. Almeida, S. Prosser, J. Cox, D. Eikel, M. H. Allen, G. A. Schultz, and M. Mann
A Novel Chromatographic Method Allows On-line Reanalysis of the Proteome
Mol. Cell. Proteomics, August 1, 2008; 7(8): 1452 - 1459.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Journal of Biological Chemistry 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2008 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement