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KMID : 0613820100200081166
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Journal of Life Science
2010 Volume.20 No. 8 p.1166 ~ p.1172
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The β Subunit of Heterotrimeric G Protein Interacts Directly with Kinesin Heavy Chains, Kinesin-I
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Seog Dae-Hyun
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Abstract
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Kinesin-I exists as a tetramer of two heavy chains (KHCs, also called KIF5s), which contain the amino (N)-terminal motor domain and carboxyl (C)-terminal domain, as well as two light chains (KLCs), which bind to the KIF5s (KIF5A, KIF5B and KIF5C) stalk region. To identify the interaction proteins for KIF5A, yeast two-hybrid screening was performed and a specific interaction with the β subunit of heterotrimeric G proteins (Gβ) was found. G bound to the amino acid residues between 808 and 935 of KIF5A and to other KIF5 members in the yeast two-hybrid assay. The WD40 repeat motif of Gβwas essential for interaction with KIF5A. In addition, these proteins showed specific interactions in the glutathione S-transferase (GST) pull-down assay. An antibody to KIF5s specifically co-immunoprecipitated KIF5s associated with heterotrimeric G proteins from mouse brain extracts. These results suggest that kinesin-I motor protein transports heteroterimeric G protein attachment vesicles along microtubules in the cell.
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KEYWORD
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Kinesin-I, molecular motors, heterotrimeric G protein, binding protein
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