Post-translational modifications are used by cells to link additional information to proteins. Most modifications are subtle and concern small moieties such as a phosphate group or a lipid. In contrast, protein ubiquitylation entails the covalent attachment of a full-length protein such as ubiquitin. The protein ubiquitylation machinery is remarkably complex, comprising more than 15 Ubls (ubiquitin-like proteins) and several hundreds of ubiquitin-conjugating enzymes. Ubiquitin is best known for its role as a tag that induces protein destruction either by the proteasome or through targeting to lysosomes. However, addition of one or more Ubls also affects vesicular traffic, protein–protein interactions and signal transduction. It is by now well established that ubiquitylation is a component of most, if not all, cellular signalling pathways. Owing to its abundance in controlling cellular functions, ubiquitylation is also of key relevance to human pathologies, including cancer and inflammation. In the present review, we focus on its role in the control of cell adhesion, polarity and directional migration. It will become clear that protein modification by Ubls occurs at every level from the receptors at the plasma membrane down to cytoskeletal components such as actin, with differential consequences for the pathway's final output. Since ubiquitylation is fast as well as reversible, it represents a bona fide signalling event, which is used to fine-tune a cell's responses to receptor agonists.
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February 2012
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Review Article|
January 27 2012
Ubiquitin links to cytoskeletal dynamics, cell adhesion and migration
Antje Schaefer;
Antje Schaefer
1
*Department of Molecular Cell Biology, Sanquin Research and Landsteiner Laboratory, Academic Medical Center, University of Amsterdam, Plesmanlaan 125, 1066 CX Amsterdam, The Netherlands
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Micha Nethe;
Micha Nethe
1
†Center for Cell Signaling, University of Virginia, Charlottesville, VA 22908, U.S.A.
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Peter L. Hordijk
Peter L. Hordijk
2
*Department of Molecular Cell Biology, Sanquin Research and Landsteiner Laboratory, Academic Medical Center, University of Amsterdam, Plesmanlaan 125, 1066 CX Amsterdam, The Netherlands
2To whom correspondence should be addressed (email p.hordijk@sanquin.nl).
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Publisher: Portland Press Ltd
Received:
October 11 2011
Revision Received:
October 31 2011
Accepted:
November 04 2011
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2012 Biochemical Society
2012
Biochem J (2012) 442 (1): 13–25.
Article history
Received:
October 11 2011
Revision Received:
October 31 2011
Accepted:
November 04 2011
Citation
Antje Schaefer, Micha Nethe, Peter L. Hordijk; Ubiquitin links to cytoskeletal dynamics, cell adhesion and migration. Biochem J 15 February 2012; 442 (1): 13–25. doi: https://doi.org/10.1042/BJ20111815
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