Novel heterotrimeric kinesin-related protein purified from sea urchin eggs

D. G. Cole, S. W. Chinn, K. P. Wedaman, K. Hall, T. Vuong, J. M. Scholey

Research output: Contribution to journalArticlepeer-review

217 Scopus citations

Abstract

KINESIN heavy chain and kinesin-related polypeptides (KRPs) comprise a family of motor proteins with diverse intracellular transport functions1-7. Using pan-kinesin peptide antibodies that react with these proteins8,9, we have previously purified from sea urchin eggs a trimeric microtubule-binding and bundling protein, KRP(85/95) (ref. 8) comprising subunits of Mr 115,000 (115K), 95K and 85K. We report here that kinesin-related genes encode the 85K and 95K subunits, and that the protein can be immunoprecipitated from cytosol as a trimeric complex using an 85K monoclonal antibody. We also find that purified KRP(85/95) directs movements towards the 'plus' ends of microtubules. To our knowledge, this protein is the first kinesin-related motor to be purified from its natural host cell in a native multimeric state.

Original languageEnglish (US)
Pages (from-to)268-270
Number of pages3
JournalNature
Volume366
Issue number6452
StatePublished - Nov 18 1993

ASJC Scopus subject areas

  • General

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