JLP associates with kinesin light chain 1 through a novel leucine zipper-like domain

doi:10.1074/jbc.M505499200

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Papers In Press, published online ahead of print June 29, 2005
J. Biol. Chem, 10.1074/jbc.M505499200
Submitted on May 19, 2005
Accepted on June 29, 2005

JLP associates with kinesin light chain 1 through a novel leucine zipper-like domain

Quang Nguyen, Clement M. Lee, Ahn Lee, and E. Premkumar Reddy

Fels Institute for Cancer Research and Molecular Biology, Temple University, Philadelphia, PA 19140

Corresponding Author: clement{at}temple.edu

Scaffolding proteins exist in eukaryotes to properly assemble signaling proteins into specific multimeric functional complexes. JLP is a novel leucine zipper protein belonging to a family of scaffolding proteins that assemble JNK signaling modules. JLP is a proline-rich protein that contains two leucine zipper domains and a highly conserved C-terminal domain. We have identified kinesin light chain 1 (KLC1) as a binding partner for the second leucine zipper domain of JLP using yeast two-hybrid screening. The interaction domain of KLC1 was mapped to its tetratripeptide repeat (TPR) which contains a novel leucine zipper-like domain that is crucial for the interaction with JLP. Mutations of L276, L283, V290, and L297 within this domain of KLC1 disrupted its ability to associate with JLP. Immuno-fluorescence studies showed that JLP and KLC1 co-localized in the cytoplasm and that the localization of JLP was dependent on its second leucine zipper. Ectopic expression of a dominant negative form of KLC1 resulted in the mislocalization of endogenous JLP. Moreover, the association between JLP and KLC1 occurred in vivo and was important in the formation of ternary complex with JNK1. These results identify a novel protein-protein interaction between KLC1 and JLP that involves leucine zipper-like domains, and support the role of motor proteins in the spatial regulation of signaling modules

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