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Publication : Two kinesin light chain genes in mice. Identification and characterization of the encoded proteins.

First Author  Rahman A Year  1998
Journal  J Biol Chem Volume  273
Issue  25 Pages  15395-403
PubMed ID  9624122 Mgi Jnum  J:48183
Mgi Id  MGI:1266918 Doi  10.1074/jbc.273.25.15395
Citation  Rahman A, et al. (1998) Two kinesin light chain genes in mice. Identification and characterization of the encoded proteins. (Erratum pg. 24280). J Biol Chem 273(25):15395-403
abstractText  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,, HomBooher, 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.
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