|
KMID : 0545120040140051031
|
|
Journal of Microbiology and Biotechnology
2004 Volume.14 No. 5 p.1031 ~ p.1037
|
|
|
Characterization of Segments of Gα16 Subunit Required for Efficient Coupling with Chemoattractant C5a, IL-8, and fMLP Receptors
|
|
Ha JH
Lee CH/Lee CH
|
|
|
Abstract
|
|
|
|
The interaction of chemoattractant receptors and Gα16 was studied to provide the molecular basis to elucidate the interaction of chemoattractant receptors with Gα16 subunit thereby possibly contributing to finding novel targets for designing new type of G protein antagonists with anti-inflammatory effects. Experiments were performed to characterize the Gα16 subunit domains responsible for efficient coupling to chemoattractant receptors. Thus a series of chimeric Gα11/Gα16 and Gα16/Gα11 cDNA constructs were expressed and the ability of chimeric proteins to mediate C5a IL-8 and fMLP-induced release of inositol phosphate in transfected Cos-7 cells was tested. The results showed that short stretches of residues 154 to residue 167 and from residue 174 to residue 195 of Gα16 contribute to efficient coupling to the C5a receptor. On the other hand a stretch of amino acid residues 220- 240 of Gα16 that is necessary for interacting with C5a receptor did not play any role in the interaction with IL-8 receptor. However a stretch from residue 155 to residue 195 of Gα16 was found to be crucial for efficient coupling to IL-8 receptor in concert with C-terminal 30 amino acid residues of this α subunit. Coupling profiles of a variety of chimeras composed of Gα11 and Gα16 to fMLP receptor indicate that the C-terminal 30 amino acids are most critical for the coupling of Gα16 to fMLP receptor. Taken together Gα16 subunit recruits multiple and distinctive coupling regions depending on the type of receptors to interact.
|
|
|
KEYWORD
|
|
|
|
|
|
FullTexts / Linksout information
|
|
|
|
|
|
Listed journal information
|
|
  
|