Affinity between TBC1D4 (AS 160) phosphotyrosine-binding domain and insulin-regulated aminopeptidase cytoplasmic domain measured by isothermal titration calorimetry
- Authors
- Park, SangYoun; Kim, Keon Young; Kim, Sunmin; Yu, Young Seok
- Issue Date
- 30-Jun-2012
- Publisher
- KOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY
- Keywords
- IRAP; Isothermal titration calorimetry; Protein-protein interaction; PTB domain; TBC1D4 (AS160)
- Citation
- BMB REPORTS, v.45, no.6, pp.360 - 364
- Journal Title
- BMB REPORTS
- Volume
- 45
- Number
- 6
- Start Page
- 360
- End Page
- 364
- URI
- http://scholarworks.bwise.kr/ssu/handle/2018.sw.ssu/12402
- DOI
- 10.5483/BMBRep.2012.45.6.030
- ISSN
- 1976-6696
- Abstract
- Uptake of circulating glucose into the cells happens via the insulin-mediated signalling pathway, which translocates the glucose transporter 4 (GLUT4) vesicles from the intracellular compartment to the plasma membrane. Rab . GTPases are involved in this vesicle trafficking, where Rab . GTPase-activating proteins (RabGAP) enhance the GTP to GDP hydrolysis. TBC1D4 (AS160) and TBC1D1 are functional RabGAPs in the adipocytes and the skeletonal myocytes, respectively. These proteins contain two phosphotyrosine-binding domains (PTBs) at the amino-terminus of the catalytic RabGAP domain. The second PTB has been shown to interact with the cytoplasmic region of the insulin-regulated aminopeptidase (IRAP) of the GLUT4 vesicle. In this study, we quantitatively measured the similar to mu M affinity (K-D) between TBC1D4 PTB and IRAP using isothermal titration calorimetry, and further showed that IRAP residues 1-49 are the major region mediating this interaction. We also demonstrated that the IRAP residues 1-15 are necessary but not sufficient for the PTB interaction. [BMB Reports 2012; 45(6): 360-364]
- Files in This Item
-
Go to Link
- Appears in
Collections - College of Natural Sciences > School of Systems and Biomedical Science > 1. Journal Articles
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.