Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility

Ronald D. Vale, Thomas S. Reese, Michael Sheetz

Research output: Contribution to journalArticle

1276 Scopus citations

Abstract

Axoplasm from the squid giant axon contains a soluble protein translocator that induces movement of microtubules on glass, latex beads on microtubules, and axoplasmic organelles on microtubules. We now report the partial purification of a protein from squid giant axons and optic lobes that induces these microtubule-based movements and show that there is a homologous protein in bovine brain. The purification of the translocator protein depends primarily on its unusual property of forming a high affinity complex with microtubuies in the presence of a nonhydrolyzable ATP analog, adenylyl imidodiphosphate. The protein, once released from microtubuies with ATP, migrates on gel filtration columns with an apparent molecular weight of 600 kilodaltons and contains 110-120 and 60-70 kilodalton polypeptides. This protein is distinct in molecular weight and enzymatic behavior from myosin or dynein, which suggests that it belongs to a novel class of force-generating molecules, for which we propose the name kinesin.

Original languageEnglish (US)
Pages (from-to)39-50
Number of pages12
JournalCell
Volume42
Issue number1
DOIs
StatePublished - Jan 1 1985
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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