The carboxy-terminal region of the TBC1D4 (AS160) RabGAP mediates protein homodimerization
- Authors
- Woo, Ju Rang; Kim, Soon-Jong; Kim, Keon Young; Jang, Hyonchol; Shoelson, Steven E.; Park, SangYoun
- Issue Date
- Oct-2017
- Publisher
- ELSEVIER SCIENCE BV
- Keywords
- TBC1D4; AS160; TBC1D1; Dimerization; Coiled-coil; RabGAP
- Citation
- INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, v.103, pp.965 - 971
- Journal Title
- INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
- Volume
- 103
- Start Page
- 965
- End Page
- 971
- URI
- http://scholarworks.bwise.kr/ssu/handle/2018.sw.ssu/6224
- DOI
- 10.1016/j.ijbiomac.2017.05.119
- ISSN
- 0141-8130
- Abstract
- TBC1D4 (also known as AS160) is a Rab GTPase-activating protein (RabGAP) which functions in insulin signaling. TBC1D4 is critical for translocation of glucose transporter 4 (GLUT4), from an inactive, intra-cellular, vesicle-bound site to the plasma membrane, where it promotes glucose entry into cells. The TBC1D4 protein is structurally subdivided into two N-terminal phosphotyrosine-binding (PTB) domains, a C-terminal catalytic RabGAP domain, and a disordered segment in between containing potential Akt phosphorylation sites. Structural predictions further suggest that a region C-terminal to the RabGAP domain adopts a coiled-coil motif. We show that C-terminal region (CTR) region is largely a-helical and mediates TBC1D4 RabGAP dimerization. RabGAP catalytic activity and thermal stability appear to be independent of CTR-mediated dimerization. (C) 2017 Elsevier B.V. All rights reserved.
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Collections - College of Natural Sciences > School of Systems and Biomedical Science > 1. Journal Articles
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