A novel action of terpendole E on the motor activity of mitotic Kinesin Eg5

Chem Biol. 2003 Feb;10(2):131-7. doi: 10.1016/s1074-5521(03)00020-6.


To reveal the mechanism of mitosis, the development of M phase-specific inhibitors is an important strategy. We have been screening microbial products to find specific M phase inhibitors that do not directly target tubulins, and rediscovered terpendole E (TerE) as a novel Eg5 inhibitor. TerE did not affect microtubule integrity in interphase, but induced formation of a monoastral spindle in M phase. TerE inhibited both motor and microtubule-stimulated ATPase activities of human Eg5, but did not affect conventional kinesin from either Drosophila or bovine brain. Although terpendoles have been reported as inhibitors of acyl-CoA:cholesterol O-acyltransferase (ACAT), the Eg5 inhibitory activity of TerE was independent of ACAT inhibition. Taken together, we demonstrate that TerE is a novel Eg5 inhibitor isolated from a fungal strain.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / metabolism
  • Animals
  • Antineoplastic Agents / pharmacology*
  • Brain / enzymology
  • Cattle
  • Cell Cycle / drug effects
  • Diterpenes / pharmacology*
  • Escherichia coli
  • Flow Cytometry
  • Fluorescent Antibody Technique
  • Golgi Apparatus / drug effects
  • Indoles / pharmacology*
  • Kinesin / antagonists & inhibitors*
  • Kinesin / genetics
  • Metaphase / drug effects
  • Microtubules / drug effects
  • Mitosis / drug effects*
  • Phenotype
  • Sterol O-Acyltransferase / antagonists & inhibitors
  • Tubulin / biosynthesis
  • Xenopus Proteins / antagonists & inhibitors*
  • Xenopus Proteins / genetics


  • Antineoplastic Agents
  • Diterpenes
  • Indoles
  • KIF11 protein, Xenopus
  • Tubulin
  • Xenopus Proteins
  • terpendole E
  • Sterol O-Acyltransferase
  • Adenosine Triphosphatases
  • Kinesin