Microtubule interaction site of the kinesin motor

Cell. 1997 Jul 25;90(2):207-16. doi: 10.1016/s0092-8674(00)80329-3.

Abstract

Kinesin and myosin are motor proteins that share a common structural core and bind to microtubules and actin filaments, respectively. While the actomyosin interface has been well studied, the location of the microtubule-binding site on kinesin has not been identified. Using alanine-scanning mutagenesis, we have found that microtubule-interacting kinesin residues are located in three loops that cluster in a patch on the motor surface. The critical residues are primarily positively charged, which is consistent with a primarily electrostatic interaction with the negatively charged tubulin molecule. The core of the microtubule-binding interface resides in a highly conserved loop and helix (L12/alpha5) that corresponds topologically to the major actin-binding domain of myosin. Thus, kinesin and myosin have developed distinct polymer-binding domains in a similar region with respect to their common catalytic cores.

Publication types

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

MeSH terms

  • Adenosine Triphosphatases / metabolism
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism
  • Escherichia coli / genetics
  • Kinesin / chemistry
  • Kinesin / genetics*
  • Kinesin / metabolism*
  • Microtubules / chemistry
  • Microtubules / enzymology*
  • Mutagenesis, Site-Directed / physiology
  • Protein Binding / physiology
  • Protein Structure, Tertiary

Substances

  • Bacterial Proteins
  • Adenosine Triphosphatases
  • Kinesin