A G protein is a protein switch whose activity depends on the bound guanine nucleotide. The three-subunit G proteins coupled to G protein-coupled receptors relay activation to other proteins; they are distinct from the receptors themselves. See the Alberts reference under G protein-coupled receptor.
A small-molecule inhibitor that stabilizes a GDP-bound arrangement of Gαq and inhibits nucleotide exchange.[ref]
A small GTPase is a relatively small nucleotide-switch protein that cycles between GDP- and GTP-bound states. Ras family proteins illustrate signaling mechanisms distinct from the three-subunit organization of a heterotrimeric G protein.
A Rab-family regulator associated with late endosomal and degradative trafficking.
A Rab-family regulator associated with early endosomal membrane domains.
Replacement of an early Rab-regulated membrane identity by a later one, exemplified by Rab5 loss and Rab7 acquisition during endosome maturation.
A heterotrimeric G protein is a signaling assembly with , and subunits. Receptor-promoted nucleotide exchange on regulates interactions with and effectors; both signaling components can contribute downstream.
The associated β and γ subunits of a heterotrimeric G protein. Their interactions with downstream effectors transmit signals as well as support heterotrimer assembly.
The guanine-nucleotide-binding subunit of a heterotrimeric G protein. Nucleotide state changes its interactions with receptors, Gβγ and effectors.
A Gα family member that can inhibit adenylyl cyclase.
A Gα family member that can stimulate adenylyl cyclase.
A Gα family member that activates phospholipase C signalling.
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