Molecular Interaction Between Interleukin-8 Receptor and G$_\alpha$16 subunit G protein

Interleukin-8 수용체와 G$_\alpha$ 16 subunit G protein 간의 분자상호 작용에 관한 연구

  • 하지희 (한양대학교 의과대학 약리학교실 및 의과학 연구소) ;
  • 강주섭 (한양대학교 의과대학 약리학교실 및 의과학 연구소) ;
  • 고현철 (한양대학교 의과대학 약리학교실 및 의과학 연구소) ;
  • 신인철 (한양대학교 의과대학 약리학교실 및 의과학 연구소) ;
  • 이창호 (한양대학교 의과대학 약리학교실 및 의과학 연구소)
  • Published : 2000.09.01

Abstract

In order to identify the domains of the G$_{\alpha}$16 subunit G protein that are responsible for its activation by the Interleukin-8 receptor, a serious of chimeras between G$_{\alpha}$16 and G$_{\alpha}$11 were assessed for their abilities to be activated by these receptors. Co-expression of IL-8 receptor and chimeras in which the carboxyl-terminal regions of G$_{\alpha}$11 were replaced from 30 up to 156 amino acid residues with the corresponding regions of G$_{\alpha}$16 demonstrated that C-terminal 156 amino acid residues of the G$_{\alpha}$16 were not sufficient to confer IL-8 receptor interaction specificity. Testing of a reciprocal serious of chimeras composed of G$_{\alpha}$16 sequences at the amino terminus and G$_{\alpha}$11 sequences at the carboxyl terminals revealed that sequences extending from the amino tar- minus to amino acid 209 of G$_{\alpha}$16 were sufficient to 7ndow the chimera with 75-80% of interaction specificity for 7-8-induced activation. These results suggest th,.7t combined interactions of the C-terminal 30 amino acid residues and certain domains extending from the arts.ino terminus to amino acid 209 of Gal 6 protein may be involved in its couplings to IL-8 receptor.tain domains extending from the arts.ino terminus to amino acid 209 of Gal 6 protein may be involved in its couplings to IL-8 receptor.