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KMID : 0613820070170070889
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Journal of Life Science
2007 Volume.17 No. 7 p.889 ~ p.895
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JSAP1 Interacts with Kinesin Light Chain 1 through Conserved Binding Segments
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Kim Sang-Jin
Lee Chul-Hee
Park Hye-Young
Yea Sung-Su
Jang Won-Hee
Lee Sang-Kyeong
Park Yeong-Hong
Cha Ok-Soo
Moon Il-Soo
Seog Dae-Hyun
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Abstract
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A conventional kinesin, KIF5/kinesin-I, is composed of two kinesin heavy chains (KHCs) and two kinesin light chains (KLCs) and binds directly to microtubules. KIF5 motor mediates the transport of various membranous organelles, but the mechanism how they recognize and bind to a specific cargo has not yet been completely elucidated. Here, we used the yeast two-hybrid system to identify the neuronal protein(s) that interacts with the tetratricopeptide repeats (TRP) of KLC1 and found a specific interaction with JNK/stress-activated protein kinase-associated protein 1 (JSAP1/JIP3). The yeast two-hybrid assay demonstrated that the TRP 1, 2 domain-containing region of KLC1 mediated binding to the leucine zipper domain of JSAP1. JSAP1 also bound to the TRP region of KLC2 but not to neuronal KIF5A, KIF5C and ubiquitous KIF5B in the yeast two-hybrid assay. In addition, these proteins showed specific interactions in the GST pull-down assay and by co-immunoprecipitation. KLC1 and KIF5B interacted with GST-JSAP1 fusion proteins, but not with GST alone. An antibody to JSAP1 specifically co-immunoprecipitated KIF5s associated with JSAP1 from mouse brain extracts. These results suggest that JSAP1, as KLC1 receptor, is involved in the KIF5 mediated transport.
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KEYWORD
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Kinesin, kinesin light chain, molecular motors, protein-protein interaction, adaptor proteins
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