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 journalArticle

26 Scopus citations

Abstract

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
Volume294
Issue number1
DOIs
StatePublished - Nov 19 1999

Keywords

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

ASJC Scopus subject areas

  • Virology

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