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Altered chemomechanical coupling causes impaired motility of the kinesin-4 motors KIF27 and KIF7.

Authors
  • Yue, Yang1
  • Blasius, T Lynne1
  • Zhang, Stephanie2
  • Jariwala, Shashank3
  • Walker, Benjamin2
  • Grant, Barry J3
  • Cochran, Jared C2
  • Verhey, Kristen J4
  • 1 Department of Cell and Developmental Biology, University of Michigan Medical School, Ann Arbor, MI.
  • 2 Department of Molecular and Cellular Biochemistry, Indiana University, Bloomington, IN. , (India)
  • 3 Department of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, MI.
  • 4 Department of Cell and Developmental Biology, University of Michigan Medical School, Ann Arbor, MI [email protected]
Type
Published Article
Journal
The Journal of Cell Biology
Publisher
The Rockefeller University Press
Publication Date
Apr 02, 2018
Volume
217
Issue
4
Pages
1319–1334
Identifiers
DOI: 10.1083/jcb.201708179
PMID: 29351996
Source
Medline
License
Unknown

Abstract

Kinesin-4 motors play important roles in cell division, microtubule organization, and signaling. Understanding how motors perform their functions requires an understanding of their mechanochemical and motility properties. We demonstrate that KIF27 can influence microtubule dynamics, suggesting a conserved function in microtubule organization across the kinesin-4 family. However, kinesin-4 motors display dramatically different motility characteristics: KIF4 and KIF21 motors are fast and processive, KIF7 and its Drosophila melanogaster homologue Costal2 (Cos2) are immotile, and KIF27 is slow and processive. Neither KIF7 nor KIF27 can cooperate for fast processive transport when working in teams. The mechanistic basis of immotile KIF7 behavior arises from an inability to release adenosine diphosphate in response to microtubule binding, whereas slow processive KIF27 behavior arises from a slow adenosine triphosphatase rate and a high affinity for both adenosine triphosphate and microtubules. We suggest that evolutionarily selected sequence differences enable immotile KIF7 and Cos2 motors to function not as transporters but as microtubule-based tethers of signaling complexes.

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