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MBC in Press, published online ahead of print November 24, 2004
Mol. Biol. Cell 10.1091/mbc.E04-07-0553

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Submitted on July 4, 2004
Accepted on November 10, 2004

The C. elegans UNC-14 RUN Domain Protein Binds to the Kinesin-1/UNC-16 Complex and Regulates Synaptic Vesicle Localization

Rie Sakamoto,*{dagger} Dana T. Byrd,{dagger}{ddagger}{sect} Heather M. Brown,{ddagger} Naoki Hisamoto,* Kunihiro Matsumoto,*|| and Yishi Jin{ddagger}||

*Department of Molecular Biology, Graduate School of Science, Nagoya University and Core Research for Evolutional Science and Technology, Japan Science and Technology Corporation, Nagoya 464-8602, Japan; {ddagger}Department of Molecular Cell and Development Biology, Sinsheimer Laboratories, Howard Hughes Medical Institute, University of California, Santa Cruz, CA 95064

Monitoring Editor: Suzanne Pfeffer

Kinesin-1 is a heterotetramer composed of kinesin heavy chain (KHC) and kinesin light chain (KLC). The C. elegans genome has a single KHC, encoded by the unc-116 gene, and two KLCs, encoded by the klc-1 and klc-2 genes. We show here that UNC-116/KHC and KLC-2 form a complex orthologous to conventional kinesin-1. KLC-2 also binds UNC-16, the C. elegans JIP3/JSAP1 JNK-signaling scaffold protein, and the UNC-14 RUN domain protein. The localization of UNC-16 and UNC-14 depends on kinesin-1 (UNC-116 and KLC-2). Furthermore, mutations in unc-16, klc-2, unc-116, and unc-14 all alter the localization of cargos containing synaptic vesicle markers. Double mutant analysis is consistent with these four genes functioning in the same pathway. Our data support a model whereby UNC-16 and UNC-14 function together as kinesin-1 cargos and regulators for the transport or localization of synaptic vesicle components.

{dagger}These authors contributed equally to this work.

{sect}Present address: Howard Hughes Medical Institute, Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706.

||Corresponding authors. E-mail: g44177a{at}nucc.cc.nagoya-u.ac.jp E-mail: Jin{at}biology.ucsc.edu






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