Subcellular Localization and Sequence of Sea Urchin Kinesin Heavy Chain: Evidence for Its Association with Membranes in the Mitotic Apparatus and Interphase Cytoplasm

• Published in: The Journal of cell biology Vol. 113; no. 4; pp. 817 - 833
• Main Authors: Wright, Brent D., Henson, John H., Wedaman, Karen P., Willy, Patricia J., Morand, Janice N., Scholey, Jonathan M.
• Format: Journal Article
• Language: English
• Published: New York, NY Rockefeller University Press 01.05.1991; The Rockefeller University Press
• Subjects: Adenosine Triphosphatases - genetics; Adenosine Triphosphatases - metabolism; Amino Acid Sequence; Animals; Antibodies; Antibodies, Monoclonal - immunology; biochemical analysis; Biological and medical sciences; Blotting, Western; Calsequestrin - metabolism; Cell Compartmentation; cell constituents; cell division; Cell physiology; Cells; Cleavage Stage, Ovum; Cloning, Molecular; Complementary DNA; cytology; Cytoplasm; Detergents; DNA - genetics; Echinoidea; Eggs; Embryos; Fundamental and applied biological sciences. Psychology; Interphase; Intracellular Membranes - metabolism; Kinesin; Marine; Microtubules - metabolism; mitosis; Mitotic spindle apparatus; Molecular and cellular biology; Molecular Sequence Data; Nocodazole - pharmacology; Peritoneal Cavity - cytology; Polymerase chain reaction; Restriction Mapping; Sea urchins; Sea Urchins - cytology; Sea Urchins - ultrastructure; Spindle Apparatus - metabolism; Spindle Apparatus - ultrastructure; Tubulin - metabolism; Echinodermata; heavy-Peptide chain; Plasma membrane; Molecular association; Mitotic apparatus; Echinoidea; Invertebrata; Localization; Sea urchin; Cytoplasm
• ISSN: 0021-9525; 1540-8140
• DOI: 10.1083/jcb.113.4.817

Kinesin was previously immunolocalized to mitotic apparatuses (MAs) of early sea urchin blastomeres. 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.