Skip to main content

Research Repository

Advanced Search

Identification of key residues that regulate the interaction of kinesins with microtubule ends

Belsham, Hannah R.; Friel, Claire T.

Identification of key residues that regulate the interaction of kinesins with microtubule ends Thumbnail


Authors

Hannah R. Belsham



Abstract

Kinesins are molecular motors that use energy derived from ATP turnover to walk along microtubules, or when at the microtubule end, regulate growth or shrinkage. All kinesins that regulate microtubule dynamics have long residence times at microtubule ends, whereas those that only walk have short end‐residence times. Here, we identify key amino acids involved in end binding by showing that when critical residues from Kinesin‐13, which depolymerises microtubules, are introduced into Kinesin‐1, a walking kinesin with no effect on microtubule dynamics, the end‐residence time is increased up to several‐fold. This indicates that the interface between the kinesin motor domain and the microtubule is malleable and can be tuned to favour either lattice or end binding.

Citation

Belsham, H. R., & Friel, C. T. (2019). Identification of key residues that regulate the interaction of kinesins with microtubule ends. Cytoskeleton, 76(7-8), 440-446. https://doi.org/10.1002/cm.21568

Journal Article Type Article
Acceptance Date Sep 17, 2019
Online Publication Date Oct 1, 2019
Publication Date Oct 1, 2019
Deposit Date Oct 4, 2019
Publicly Available Date Nov 4, 2019
Journal Cytoskeleton
Print ISSN 1949-3584
Electronic ISSN 1949-3592
Publisher Wiley
Peer Reviewed Peer Reviewed
Volume 76
Issue 7-8
Pages 440-446
DOI https://doi.org/10.1002/cm.21568
Keywords MCAK; Kinesin-1; Kinesin-13; protein engineering; 4 helix
Public URL https://nottingham-repository.worktribe.com/output/2748635
Publisher URL https://onlinelibrary.wiley.com/doi/10.1002/cm.21568
Contract Date Oct 4, 2019

Files





You might also like



Downloadable Citations