Mini-Review
The role of 26S proteasome-dependent proteolysis in the formation and restructuring of microtubule networks
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Volume 7, Issue 10 October 2012
Pages 1289 - 1295
http://dx.doi.org/10.4161/psb.21543
Keywords: microtubule dynamics, microtubule-associated proteins, post-translational modifications, tubulin folding, ubiquitin
Authors: Jasmina Kurepa, Songhu Wang and Jan A. Smalle
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- Jasmina Kurepa
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Plant Physiology, Biochemistry and Molecular Biology Program; Department of Plant and Soil Sciences; University of Kentucky; Lexington, KY USA
- Songhu Wang
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Plant Physiology, Biochemistry and Molecular Biology Program; Department of Plant and Soil Sciences; University of Kentucky; Lexington, KY USA
Current affiliation: Department of Plant Sciences; University of California–Davis; Davis, CA USA
- Jan A. Smalle
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Corresponding author: jsmalle@uky.edu
Plant Physiology, Biochemistry and Molecular Biology Program; Department of Plant and Soil Sciences; University of Kentucky; Lexington, KY USA
Abstract:
In this review, we summarize the evidence pointing at the important role of 26S proteasome-dependent proteolysis in the regulation of microtubule synthesis and microtubule dynamics. Because most of the advances in this relatively unexplored research field originate from yeast and animal studies, we have considered those studies that describe the role of proteolysis in processes that are evolutionarily conserved and known to exist in plants. In addition, we place particular emphasis on the proteasome-dependent degradation of plant-specific microtubule-associated protein SPIRAL1 and its function in MT rearrangements associated with salt stress.
Received: July 17, 2012; Accepted: July 19, 2012; Published Online: August 20, 2012
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