Subcellular localization and sequence of sea urchin kinesin heavy chain: Evidence for its association with membranes in the mitotic apparatus and interphase cytoplasm

Brent D. Wright, John H. Henson, Karen P. Wedaman, Patricia J. Willy, Janice N. Morand, Jonathan M. Scholey

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Abstract

Kinesin was previously immunolocalized to mitotic apparatuses (MAs) of early sea urchin blastomeres (Scholey, J. M., M. E. Porter, P. M. Grissom, and J. R. McIntosh. 1985. Nature [Lond.]. 318:483-486). Here we report evidence that this MA-associated motor protein is a conventional membrane-bound kinesin, rather than a kinesin-like protein. Our evidence includes the observation that the deduced amino acid sequence of this sea urchin kinesin heavy chain is characteristic of a conventional kinesin. In addition, immunolocalizations using antibodies that distinguish kinesin from kinesin-like proteins confirm that conventional kinesin is concentrated in MAs. Finally, our immunocytochemical data further suggest that conventional kinesin is associated with membranes which accumulate in MAs and interphase asters of early sea urchin embryos, and with vesicles that are distributed in the perinuclear region of coelomocytes. Thus kinesin may function as a microtubule-based vesicle motor in some MAs, as well as in the interphase cytoplasm.

Original languageEnglish (US)
Pages (from-to)817-833
Number of pages17
JournalJournal of Cell Biology
Volume113
Issue number4
StatePublished - May 1991

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ASJC Scopus subject areas

  • Cell Biology

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