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Science 24 March 1995:
Vol. 267. no. 5205, pp. 1834 - 1837
DOI: 10.1126/science.7892610
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Articles

Science, Vol 267, Issue 5205, 1834-1837
Copyright © 1995 by American Association for the Advancement of Science

articles

Kinectin, an essential anchor for kinesin-driven vesicle motility

J Kumar, H Yu, and MP Sheetz

Department of Cell Biology, Duke University Medical Center, Durham, NC 27710.

The membrane anchor for the molecular motor kinesin is a critical site involved in intracellular membrane trafficking. Monoclonal antibodies specific for the cytoplasmic surface of chick brain microsomes were used to define proteins involved in microtubule-dependent transport. One of four antibodies tested inhibited plus-end-directed vesicle motility by approximately 90 percent even as a monovalent Fab fragment and reduced kinesin binding to vesicles. This antibody bound to the cytoplasmic domain of kinectin, an integral membrane protein of the endoplasmic reticulum that binds to kinesin. Thus, kinectin acted as a membrane anchor protein for kinesin-driven vesicle motility.


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