Your browser version may not work well with NCBI's Web applications. More information here...
1: Mol Biol Cell. 2005 Feb;16(2):483-96. Epub 2004 Nov 24.
Related Articles, Links
Click here to read Click here to read
The Caenorhabditis elegans UNC-14 RUN domain protein binds to the kinesin-1 and UNC-16 complex and regulates synaptic vesicle localization.

Sakamoto R, Byrd DT, Brown HM, Hisamoto N, Matsumoto K, Jin Y.

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.

Kinesin-1 is a heterotetramer composed of kinesin heavy chain (KHC) and kinesin light chain (KLC). The Caenorhabditis 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.

Publication Types:
PMID: 15563606 [PubMed - indexed for MEDLINE]

PMCID: PMC545882