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J. Cell Biol.,
Volume 141, Number 2, April 20, 1998 443-454
* Howard Hughes Medical Institute, Division of Cellular and Molecular Medicine, Department of Pharmacology, University of
California, San Diego, La Jolla, California 92093-0683; 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 (. 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.
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
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