A method for multiprotein assembly in cells reveals independent action of kinesins in complex

Stephen R. Norris, Virupakshi Soppina, Aslan S. Dizaji, Kristin I. Schimert, David Sept, Dawen Cai, Sivaraj Sivaramakrishnan, Kristen J. Verhey

Research output: Contribution to journalArticlepeer-review

32 Scopus citations

Abstract

Teams of processive molecular motors are critical for intracellular transport and organization, yet coordination between motors remains poorly understood. Here, we develop a system using protein components to generate assemblies of defined spacing and composition inside cells. This system is applicable to studying macromolecular complexes in the context of cell signaling, motility, and intracellular trafficking. We use the system to study the emergent behavior of kinesin motors in teams. We find that two kinesin motors in complex act independently (do not help or hinder each other) and can alternate their activities. For complexes containing a slow kinesin-1 and fast kinesin-3 motor, the slow motor dominates motility in vitro but the fast motor can dominate on certain subpopulations of microtubules in cells. Both motors showed dynamic interactions with the complex, suggesting that motor-cargo linkages are sensitive to forces applied by the motors. We conclude that kinesin motors in complex act independently in a manner regulated by the microtubule track.

Original languageEnglish (US)
Pages (from-to)393-406
Number of pages14
JournalJournal of Cell Biology
Volume207
Issue number3
DOIs
StatePublished - 2014

Bibliographical note

Publisher Copyright:
© 2014 Norris et al.

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