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Vol. 57, Issue 1, 13-23, January 2000
z-Specific Sequence at the
Carboxyl Terminus Increases the Promiscuity of G16
toward Gi-Coupled Receptors
Department of Biology and the Biotechnology Research Institute,
Hong Kong University of Science and Technology, Clear Water Bay,
Kowloon, Hong Kong, China
Although the promiscuous nature of G16 allows it to
interact with numerous G protein-coupled receptors, several
Gi-linked receptors are incapable of activating
phospholipase C via G16. A series of chimeras between
G
16 and Gz were constructed and assayed
for their ability to mediate receptor-induced stimulation of
phospholipase C. Two G16/z chimeras harboring 25 or 44 Gz-specific sequences at their C termini (named 16z25
and 16z44) were capable of responding to 14 different
Gi-coupled receptors tested, including those that were
either unable to associate with G16 (melatonin Mel1c) or
activate G16 weakly (µ-opioid and type 1 somatostatin). Agonist-induced stimulation of phospholipase C was more
efficiently mediated (higher maximal and lower EC50 value)
by 16z44 than by G16. Both 16z25 and 16z44 were also
coupled to Gs- and Gq-linked receptors.
Incorporation of Gz sequence at the N terminus of G16 did not further enhance the ability of the chimeras
to interact with Gi-coupled receptors. Expression of the
various chimeras was verified by immunodetection and functional
analysis of their constitutively activated mutants. These results show
that the incorporation of 4/
6 and 5 regions of
Gz into a G16 backbone can improve the
recognition of Gi-coupled receptors. G16/z
chimeras with expanded capability to interact with
Gi-linked receptors may be used to link orphan receptors to
the stimulation of phospholipase C.
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