Pamela M. Sternweis

TL;DR: Members of the regulators of G protein signaling (RGS) family stimulate the intrinsic guanosine triphosphatase (GTPase) activity of the α subunits of certain heterotrimeric guanine nucleotide–binding proteins (G proteins).

TL;DR: In vitro analysis revealed that GRK2 possesses weak GAP activity toward Gαq that is dependent on the presence of a G protein-coupled receptor, and data suggest that a subfamily of the GRKs may be bifunctional regulators of G Protein-Coupled receptors signaling operating directly on both receptors and G proteins.

TL;DR: A mechanism for activation of the nucleotide exchange activity of p115 RhoGEF that involves direct and coordinate interaction of Gα13 to both its RGS and DH domains is suggested.

TL;DR: It is concluded that α, PLCβ2, P LCβ3, and adenylyl cyclase II share an interaction on the top surface of β, and the importance of individual residues is different for α binding and for effector activation and differs even between closely related isoforms of the same effector.

TL;DR: The present study made mutations in each of the outer β strands of the G protein β1 propeller, as well as mutations in the loops that connect the outer strands to the adjacent β strands, suggesting that activation of PLCβ2 involves residues in theouter strands of blades 2, 6, and 7 of the propeller.