Francis S. Willard

TL;DR: In this paper, the authors revisited classical heterotrimeric G-protein signaling and explored these new, non-canonical Gprotein signaling pathways, including a receptor-independent Gα nucleotide cycle that regulates cell division.

TL;DR: More recent discoveries that have highlighted newly-appreciated roles for RGS proteins beyond mere negative regulators of 7TM signaling are reviewed, including the RGS-box-containing, RhoA-specific guanine nucleotide exchange factors (RGS-RhoGEFs) that serve as Gα effectors to couple 7TM and semaphorin receptor signaling to RHoA activation.

TL;DR: An RGS protein (AtRGS1) in Arabidopsis that has a predicted structure similar to a GPCR as well as an RGS box with GTPase accelerating activity is identified, suggesting that AtRGS 1 is a critical modulator of plant cell proliferation.

TL;DR: The extent of net pulling forces may depend on cortical Gα activity, which is regulated by anterior-posterior polarity cues through GPR-1/2, which was found to interact with guanosine diphosphate-bound GOA-1 and were enriched on the posterior cortex in a par-3– and par-2–dependent manner.

TL;DR: The crystal structure of human PRMT5 in complex with MEP50, bound to an S-adenosylmethionine analog and a peptide substrate derived from histone H4 is determined and the structure of the surprising hetero-octameric complex reveals the close interaction between the seven-bladed β-propeller MEP50 and the N-terminal domain ofPRMT5, and delineates the structural elements of substrate recognition.