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A 'molecular guillotine' reveals the interphase function of Kinesin-5.

Authors
  • Lv, Zhiyi1
  • Rosenbaum, Jan2
  • Aspelmeier, Timo2
  • Großhans, Jörg3
  • 1 Institute for Developmental Biochemistry, Medical School, University of Göttingen, Justus-von-Liebig Weg 11, 37077 Göttingen, Germany. , (Germany)
  • 2 Institute for Mathematical Stochastics and Felix Bernstein Institute for Mathematical Statistics in the Biosciences, University of Göttingen, Goldschmidtstraße 7, 37077 Göttingen, Germany. , (Germany)
  • 3 Institute for Developmental Biochemistry, Medical School, University of Göttingen, Justus-von-Liebig Weg 11, 37077 Göttingen, Germany [email protected] , (Germany)
Type
Published Article
Journal
Journal of Cell Science
Publisher
The Company of Biologists
Publication Date
Feb 08, 2018
Volume
131
Issue
3
Identifiers
DOI: 10.1242/jcs.210583
PMID: 29361546
Source
Medline
Keywords
License
Unknown

Abstract

Motor proteins are important for transport and force generation in a variety of cellular processes and in morphogenesis. Here, we describe a general strategy for conditional motor mutants by inserting a protease cleavage site into the 'neck' between the head domain and the stalk of the motor protein, making the protein susceptible to proteolytic cleavage at the neck by the corresponding protease. To demonstrate the feasibility of this approach, we inserted the cleavage site of the tobacco etch virus (TEV) protease into the neck of the tetrameric motor Kinesin-5. Application of TEV protease led to a specific depletion and functional loss of Kinesin-5 in Drosophila embryos. With our approach, we revealed that Kinesin-5 stabilizes the microtubule network during interphase in syncytial embryos. The 'molecular guillotine' can potentially be applied to many motor proteins because Kinesins and myosins have conserved structures with accessible neck regions.This article has an associated First Person interview with the first author of the paper.

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