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A more recent version of this article appeared on August 1, 2003
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Submitted on December 9, 2002
Revised on March 31, 2003
Accepted on April 4, 2003
1 Biology Department, University of Massachusetts Boston, 100 Morrissey Blvd., Boston, MA 02125
2 Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655
3 Biology Department, University of Massachusetts Boston, 100 Morrissey Blvd., Boston, MA 02125 (present address: AstraZeneca R and D Boston, 35 Gatehouse Drive, Waltham, MA 02451)
* Corresponding author. E-mail address: joseph.gindhart{at}umb.edu.
Kinesin-I is essential for the transport of membrane-bound organelles in neural and non-neural cells. However, the means by which kinesin interacts with its intracellular cargoes, and the means by which kinesin-cargo interactions are regulated in response to cellular transport requirements are not fully understood. The C-terminus of the Drosophila kinesin heavy chain (KHC) was used in a two-hybrid screen of a Drosophila cDNA library to identify proteins that bind specifically to the kinesin tail domain. UNC-76 is an evolutionarily conserved cytosolic protein that binds to the tail domain of KHC in two-hybrid and co-purification assays, indicating that kinesin and UNC-76 form a stable complex in vivo. Loss of Drosophila Unc-76 function results in locomotion and axonal transport defects reminiscent of the phenotypes observed in kinesin mutants, suggesting that UNC-76 is required for kinesin-dependent axonal transport. Unc-76 exhibits dosage-sensitive genetic relationships with Khc and Kinesin light chain (Klc) mutations, further supporting the hypothesis that UNC-76 and kinesin-I work in a common transport pathway. Given the interaction of FEZ1, the mammalian homolog of UNC-76, with PKC
, and the role of FEZ1 in axon outgrowth, we propose that UNC-76 helps integrate kinesin activity in response to transport requirements in axons.
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