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© The Rockefeller University Press, 0021-9525/1998//443 $5.00
The Journal of Cell Biology, Volume 141, Number 2, , 1998 443-454

Articles

Kinesin Light Chains Are Essential for Axonal Transport in Drosophila



Joseph G. Gindhart, Jr.*, Chand J. Desai{ddagger}, Sven Beushausen§, Kai Zinn{ddagger}, and Lawrence S.B. Goldstein*

* Howard Hughes Medical Institute, Division of Cellular and Molecular Medicine, Department of Pharmacology, University of California, San Diego, La Jolla, California 92093-0683; {ddagger} Division of Biology, California Institute of Technology, Pasadena, California 91125; and § Laboratory of Neurobiology, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland 20892

Kinesin is a heterotetramer composed of two 115-kD heavy chains and two 58-kD light chains. The microtubule motor activity of kinesin is performed by the heavy chains, but the functions of the light chains are poorly understood. Mutations were generated in the Drosophila gene Kinesin light chain (Klc), and the phenotypic consequences of loss of Klc function were analyzed at the behavioral and cellular levels. Loss of Klc function results in progressive lethargy, crawling defects, and paralysis followed by death at the end of the second larval instar. Klc mutant axons contain large aggregates of membranous organelles in segmental nerve axons. These aggregates, or organelle jams (Hurd, D.D., and W.M. Saxton. 1996. Genetics. 144: 1075–1085), contain synaptic vesicle precursors as well as organelles that may be transported by kinesin, kinesin-like protein 68D, and cytoplasmic dynein, thus providing evidence that the loss of Klc function blocks multiple pathways of axonal transport. The similarity of the Klc and Khc (Saxton et al. 1991. Cell 64:1093–1102; Hurd, D.D., and W.M. Saxton. 1996. Genetics 144: 1075–1085) mutant phenotypes indicates that KLC is essential for kinesin function, perhaps by tethering KHC to intracellular cargos or by activating the kinesin motor.

Abbreviations used in this paper: CSP, cysteine string protein; DHC, dynein heavy chain; KHC, kinesin heavy chain; KLC, kinesin light chain; TPR, tetratricopeptide repeat; KLH, keyhole limpet hemocyanin; SYT, synaptotagmin; TPR, tetratrico peptide repeat.

This research was supported by National Institutes of Health grants to L.S.B. Goldstein and K. Zinn. L.SB. Goldstein is an investigator of the Howard Hughes Medical Institute. J.G. Gindhart was supported by a National Institutes of Health postdoctoral fellowship. C.J. Desai was supported by an American Cancer Society postdoctoral fellowship.

Address all correspondence to Lawrence S.B. Goldstein, Howard Hughes Medical Institute, Division of Cellular and Molecular Medicine, Department of Pharmacology, University of California, San Diego, La Jolla, CA 92093-0683. Phone: 619-534-9702; FAX: 619-534-9701. E-mail: lgoldstein{at}ucsd.edu

The current address of Joseph G. Gindhart is Department of Biology, University of Massachusetts Boston, 100 Morrissey Blvd., Boston, MA 02125. The current address of Chand J. Desai is Center for Molecular Neuroscience, 406 MBRI, Vanderbilt University Medical Center, 1211 22nd Ave. S., Nashville, TN 37232.


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