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Vol. 9, Issue 2, 333-343, February 1998
and
*Institute of Protein Research, Russian Academy of Sciences, Moscow
117334, Russia; and
The motor protein kinesin is implicated in the intracellular
transport of organelles along microtubules. Kinesin light chains (KLCs)
have been suggested to mediate the selective binding of kinesin to its
cargo. To test this hypothesis, we isolated KLC cDNA clones from a
CHO-K1 expression library. Using sequence analysis, they were found to
encode five distinct isoforms of KLCs. The primary region of
variability lies at the carboxyl termini, which were identical or
highly homologous to carboxyl-terminal regions of rat KLC B and C,
human KLCs, sea urchin KLC isoforms 1-3, and squid KLCs. To examine
whether the KLC isoforms associate with different cytoplasmic
organelles, we made an antibody specific for a 10-amino acid sequence
unique to B and C isoforms. In an indirect immunofluorescence assay,
this antibody specifically labeled mitochondria in cultured CV-1 cells
and human skin fibroblasts. On Western blots of total cell homogenates,
it recognized a single KLC isoform, which copurified with mitochondria.
Taken together, these data indicate a specific association of a
particular KLC (B type) with mitochondria, revealing that different KLC
isoforms can target kinesin to different cargoes.
Division of Molecular Medicine,
Wadsworth Center, New York State Department of Health, Albany, New York
12201-0509
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