BMB Reports

생화학분자생물학회 (Korean Society for Biochemistry and Molecular Biology)
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Affinity between TBC1D4 (AS160) phosphotyrosine-binding domain and insulin-regulated aminopeptidase cytoplasmic domain measured by isothermal titration calorimetry

  • Park, Sang-Youn (School of Systems Biomedical Science, Soongsil University) ;
  • Kim, Keon-Young (School of Systems Biomedical Science, Soongsil University) ;
  • Kim, Sun-Min (School of Systems Biomedical Science, Soongsil University) ;
  • Yu, Young-Seok (School of Systems Biomedical Science, Soongsil University)
  • 투고 : 2012.02.09
  • 심사 : 2012.03.12
  • 발행 : 2012.06.30
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초록

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 GTPases-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 ${\sim}{\mu}M$ 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.

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참고문헌

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  2. The carboxy-terminal region of the TBC1D4 (AS160) RabGAP mediates protein homodimerization vol.103, 2017, https://doi.org/10.1016/j.ijbiomac.2017.05.119
  3. AKT and AMP-activated protein kinase regulate TBC1D1 through phosphorylation and its interaction with the cytosolic tail of insulin-regulated aminopeptidase IRAP vol.293, pp.46, 2018, https://doi.org/10.1074/jbc.RA118.005040