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J Biol Chem, Vol. 273, Issue 25, 15395-15403, June 19, 1998
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From the Native kinesin consists of two light chains and
two heavy chains in a 1:1 stoichiometric ratio. To date, only one gene
for kinesin light chain has been characterized, while a second gene was
identified in a genomic sequencing study but not analyzed biochemically. Here we describe new genes encoding kinesin light chains
in mouse. One of these light chains is neuronally enriched, while
another shows ubiquitous expression. The presence of multiple kinesin
light chain genes in mice is especially interesting, since there are
two kinesin heavy chain genes in humans (Niclas, J., Navone, F.,
Hom-Booher, N., and Vale, R. D. (1994) Neuron 12, 1059-1072). To assess the selectivity of kinesin light chain
interaction with the heavy chains, we performed immunoprecipitation
experiments. The data suggested that the light chains form homodimers
with no specificity in their interaction with the two heavy chains. Immunofluorescence and biochemical subfractionation suggested differences in the subcellular localization of the two kinesin light
chain gene products. Although both kinesin light chains are distributed
throughout the central and peripheral nervous systems, there is
enrichment of one in sciatic nerve axons, while the other shows
elevated levels in olfactory bulb glomeruli. These results indicate
that the mammalian nervous system contains multiple kinesin light chain
gene products with potentially distinct functions.
Howard Hughes Medical Institute, Division of
Cellular and Molecular Medicine, Program in Biomedical Sciences and
Department of Pharmacology, University of California San Diego, La
Jolla, California 92093-0683 and the § Department of
Pharmacology and Biochemistry, University of California,
San Francisco, California 94143
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