Identification of kinesin-C, a calmodulin-binding carboxy-terminal kinesin in animal (Strongylocentrotus purpuratus) cells

Gregory C. Rogers, Cynthia L. Hart, Karen P. Wedaman, Jonathan M. Scholey

Research output: Contribution to journalArticlepeer-review

27 Scopus citations


Several novel members of the kinesin superfamily, until now identified only in plants, are unique in their ability to bind calmodulin in the presence of Ca2+. Here, we identify the first such kinesin in an animal system. Sequence analysis of this new motor, called kinesin-C, predicts that it is a large carboxy-terminal kinesin, 1624 amino acid residues in length, with a predicted molecular mass of 181 kDa. Kinesin-C is predicted to contain a kinesin motor domain at its carboxy terminus, linked to a segment of alpha-helical coiled-coil 950 amino acid residues long, ending with an amino-terminal proline-rich tail domain. A putative calmodulin-binding domain resides at the extreme carboxy terminus of the motor polypeptide, and recombinant kinesin-C binds to a calmodulin-affinity column in a Ca2+-dependent fashion. The presence of this novel calmodulin-binding motor in sea urchin embryos suggests that it plays a critical role in Ca2+-dependent events during early sea urchin development.

Original languageEnglish (US)
Pages (from-to)1-8
Number of pages8
JournalJournal of Molecular Biology
Issue number1
StatePublished - Nov 19 1999


  • Calmodulin
  • Carboxy-terminal motor
  • Kinesin
  • Microtubule
  • Sea urchin

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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