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

Cell. 1985 Aug;42(1):39-50. doi: 10.1016/s0092-8674(85)80099-4.

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 depended primarily on its unusual property of forming a high affinity complex with microtubules in the presence of a nonhydrolyzable ATP analog, adenylyl imidodiphosphate. The protein, once released from microtubules 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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphate / pharmacology
  • Adenylyl Imidodiphosphate
  • Animals
  • Axons / analysis
  • Brain Chemistry
  • Cattle
  • Centrifugation, Density Gradient
  • Chromatography, Gel
  • Decapodiformes
  • Kinesin
  • Microspheres
  • Microtubules / physiology*
  • Molecular Weight
  • Movement
  • Nerve Tissue Proteins / isolation & purification*
  • Nerve Tissue Proteins / pharmacology
  • Optic Lobe, Nonmammalian / analysis
  • Organoids / physiology

Substances

  • Nerve Tissue Proteins
  • Adenylyl Imidodiphosphate
  • Adenosine Triphosphate
  • Kinesin