Cytoplasmic dynein crosslinks and slides anti-parallel microtubules using its two motor domains

Marvin E. Tanenbaum, Ronald D. Vale, Richard Mckenney

Research output: Contribution to journalArticle

43 Scopus citations

Abstract

Cytoplasmic dynein is the predominant minus-end-directed microtubule (MT) motor in most eukaryotic cells. In addition to transporting vesicular cargos, dynein helps to organize MTs within MT networks such as mitotic spindles. How dynein performs such non-canonical functions is unknown. Here we demonstrate that dynein crosslinks and slides anti-parallel MTs in vitro. Surprisingly, a minimal dimeric motor lacking a tail domain and associated subunits can cause MT sliding. Single molecule imaging reveals that motors pause and frequently reverse direction when encountering an anti-parallel MT overlap, suggesting that the two motor domains can bind both MTs simultaneously. In the mitotic spindle, inward microtubule sliding by dynein counteracts outward sliding generated by kinesin-5, and we show that a tailless, dimeric motor is sufficient to drive this activity in mammalian cells. Our results identify an unexpected mechanism for dynein-driven microtubule sliding, which differs from filament sliding mechanisms described for other motor proteins.

Original languageEnglish (US)
Article numbere00943
JournaleLife
Volume2013
Issue number2
DOIs
StatePublished - Sep 3 2013
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)
  • Medicine(all)
  • Neuroscience(all)

Fingerprint Dive into the research topics of 'Cytoplasmic dynein crosslinks and slides anti-parallel microtubules using its two motor domains'. Together they form a unique fingerprint.

  • Cite this