Open AccessKinesin-14 motors participate in a force balance at microtubule plus-ends to regulate dynamic instability
Author(s) -
Allison Ogren,
Sneha Parmar,
Soumya Mukherjee,
Samuel J. Gonzalez,
Melissa Plooster,
Mark McClellan,
Anirudh Gautam Mannava,
Elliott Davidson,
Trisha N. Davis,
Melissa K. Gardner
Publication year - 2022
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.2108046119
Subject(s) - microtubule , kinesin , motor protein , molecular motor , microtubule associated protein , microbiology and biotechnology , biology
Significance Kinesin-14 motors represent an essential class of molecular motors that bind to microtubules and then walk toward the microtubule minus-end. However, whether these motors can interact with growing plus-ends of microtubules to impact the lengthening of microtubules remains unknown. We found that Kinesin-14 motors could bind to a protein that resides at growing microtubule plus-ends and then pull this protein away from the growing end. This interaction acted to disrupt microtubule growth and decrease microtubule lengths in cells, likely by exerting minus-end–directed forces at the microtubule tip to alter the configuration of the growing microtubule plus-end. This work demonstrates general principles for the diverse roles that force-generating molecular motors can play in regulating cellular processes.