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Vol. 11, Issue 11, 3791-3803, November 2000
Department of Genetics, Cell Biology, and Development, University
of Minnesota, St. Paul, Minnesota 55108
The microtubule motor cytoplasmic dynein performs multiple cellular
functions; however, the regulation and targeting of the motor to
different cargoes is not well understood. A biochemical interaction
between the dynein intermediate chain subunit and the p150-Glued
component of the dynein regulatory complex, dynactin, has supported the
hypothesis that the intermediate chain is a key modulator of dynein
attachment to cellular cargoes. In this report, we identify multiple
intermediate chain polypeptides that cosediment with the 19S dynein
complex and two differentially expressed transcripts derived from the
single cytoplasmic dynein intermediate chain (Cdic) gene
that differ in the 3' untranslated region sequence. These results
support previous observations of multiple Cdic gene
products that may contribute to the specialization of dynein function.
Most significantly, we provide genetic evidence that the interaction
between the dynein intermediate chain and p150-Glued is functionally
relevant. We use a genomic Cdic transgene to show that
extra copies of the dynein intermediate chain gene act to suppress the
rough eye phenotype of the mutant Glued1, a
mutation in the p150-Glued subunit of dynactin. Furthermore, we show
that the interaction between the dynein intermediate chain and
p150-Glued is dependent on the dosage of the Cdic gene.
This result suggests that the dynein intermediate chain may be a
limiting component in the assembly of the dynein complex and that the
regulation of the interaction between the dynein intermediate chain and
dynactin is critical for dynein function.
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