The structural kinetics of switch-1 and the neck linker explain the functions of kinesin-1 and Eg5

Joseph M. Muretta, Yonggun Jun, Steven P. Gross, Jennifer Major, David D. Thomas, Steven S. Rosenfeld

Research output: Contribution to journalArticle

23 Scopus citations

Abstract

Kinesins perform mechanical work to power a variety of cellular functions, from mitosis to organelle transport. Distinct functions shape distinct enzymologies, and this is illustrated by comparing kinesin-1, a highly processive transport motor that can work alone, to Eg5, a minimally processive mitotic motor that works in large ensembles. Although crystallographic models for both motors reveal similar structures for the domains involved in mechanochemical transductionâ€"including switch-1 and the neck linkerâ€"how movement of these two domains is coordinated through the ATPase cycle remains unknown. We have addressed this issue by using a novel combination of transient kinetics and time-resolved fluorescence, which we refer to as “structural kinetics,â€to map the timing of structural changes in the switch-1 loop and neck linker. We find that differences between the structural kinetics of Eg5 and kinesin-1 yield insights into how these two motors adapt their enzymologies for their distinct functions.

Original languageEnglish (US)
Pages (from-to)E6606-E6613
JournalProceedings of the National Academy of Sciences of the United States of America
Volume112
Issue number48
DOIs
StatePublished - Dec 1 2015

Keywords

  • Fluorescence resonance energy transfer
  • Kinesin
  • Molecular motor
  • Time-resolved fluorescence
  • Transient kinetics

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