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KMID : 0613820170270101191
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Journal of Life Science
2017 Volume.27 No. 10 p.1191 ~ p.1198
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Interaction of Ras-GTPase-activating Protein SH3 Domain-binding Proteins 2, G3BP2, With the C-terminal Tail Region of KIF5A
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Joung Young-Ju
Jang Won-Hee
Lee Won-Hee
Kim Moo-Seong
Kim Sang-Jin
Urm Sang-Hwa
Moon Il-Soo
Seog Dae-Hyun
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Abstract
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Vesicles and organelles are transported along microtubule and delivered to appropriate compartments in cells. The intracellular transport process is mediated by molecular motor proteins, kinesin, and dynein. Kinesin is a plus-end-directed molecular motor protein that moves the various cargoes along microtubule tracks. Kinesin 1 is first isolated from squid axoplasm is a dimer of two heavy chains (KHCs, also called KIF5s), each of which is associated with the light chain (KLC). KIF5s interact with many different binding proteins through their carboxyl (C)-terminal tail region, but their binding proteins have yet to be specified. To identify the interacting proteins for KIF5A, we performed the yeast two-hybrid screening and found a specific interaction with Ras-GTPase-activating protein (GAP) Src homology3 (SH3)-domain-binding protein 2 (G3BP2), which is involved in stress granule formation and mRNA-protein (mRNP) localization. G3BP2 bound to the C-terminal 73 amino acids of KIF5A but did not interact with the KIF5B, nor the KIF5C in the yeast two-hybrid assay. The arginine-glycine-glycine (RGG)/Gly-rich region domain of G3BP2 is a minimal binding domain for interaction with KIF5A. However, G3BP1 did not interact with KIF5A. When co-expressed in HEK-293T cells, G3BP2 co-localized with KIF5A and was co-immunoprecipitated with KIF5A. These results indicate that G3BP2, which was originally identified as a Ras-GAP SH3 domain-binding protein, is a protein that interacts with KIF5A.
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KEYWORD
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Binding protein, kinesin, microtubule, Ras signaling, SH3 domain
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