Abstract
Replacement of β6/α5 region at the C-terminus on Gα16 with Gαz-specific residues has been shown to broaden the promiscuity of Gα16. Here, we substituted the last 44 residues of Gα16 with the corresponding region from either Gαi2 or GαoA (16i44 and 16o44). 16i44 and 16o44 chimeras were more effective than Gα16 at coupling to Gi-linked δ-opioid, μ-opioid, and Xenopus melatonin MT1c receptors when coexpressed in green monkey fibroblast (COS-7) cells. 16i44, but not 16o44, also enhanced the formyl peptide-induced stimulation of phospholipase C activity. Both chimeras were resistant to pertussis toxin-catalyzed [32P]ADP-ribosylation, despite the fact that pertussis toxin partially inhibited the chimera-mediated stimulation of phospholipase Cβ. The use of Gαt1 as a Gβγ scavenger revealed that the pertussis toxin-sensitivity can be attributed to endogenous Gβγ subunits released from Gi/o. Although incorporation of a Gαi-like β6/α5 region into the C-terminus of Gα16 increases its promiscuity, this region is not sufficient to support recognition by pertussis toxin.
Published Version
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
