Journal
CYTOSKELETON
Volume 72, Issue 7, Pages 305-339Publisher
WILEY
DOI: 10.1002/cm.21226
Keywords
microfilaments; septins; MT; IF; SUMO; microtubule-associated proteins; MAPs
Categories
Funding
- National Science Foundation [MCB-1052174]
- Oklahoma Health Research Program of the Oklahoma Center for the Advancement of Science and Technology (OCAST) [HR09-150S]
- O.S.U.
- Oklahoma Agricultural Experiment Station [OKL02715, OKL02961]
- Sloan Foundation
- Niblack Research Scholarship at O.S.U.
- Wentz Research Scholarship at O.S.U.
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Sumoylation is a powerful regulatory system that controls many of the critical processes in the cell, including DNA repair, transcriptional regulation, nuclear transport, and DNA replication. Recently, new functions for SUMO have begun to emerge. SUMO is covalently attached to components of each of the four major cytoskeletal networks, including microtubule-associated proteins, septins, and intermediate filaments, in addition to nuclear actin and actin-regulatory proteins. However, knowledge of the mechanisms by which this signal transduction system controls the cytoskeleton is still in its infancy. One story that is beginning to unfold is that SUMO may regulate the microtubule motor protein dynein by modification of its adaptor Lis1. In other instances, cytoskeletal elements can both bind to SUMO non-covalently and also be conjugated by it. The molecular mechanisms for many of these new functions are not yet clear, but are under active investigation. One emerging model links the function of MAP sumoylation to protein degradation through SUMO-targeted ubiquitin ligases, also known as STUbL enzymes. Other possible functions for cytoskeletal sumoylation are also discussed. (c) 2015 The Authors. Cytoskeleton Published by Wiley Periodicals, Inc.
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