The America Invents Act implementation.

The Leahy-Smith America Invents Act (AIA) is by far the most comprehensive change to the patent law in at least half a century. Implementation of the AIA has been ongoing, but the final and most critical provisions went into effect on March 16, 2013. Although, it will take several years before we fully understand the law's impact, the new law is likely to fundamentally change the way innovation is protected within the United States.

Novel activity of RGS14 on Goalpha and Gialpha nucleotide binding and hydrolysis distinct from its RGS domain and GDI activity.

The bifunctional protein RGS14 is both a GTPase activating protein (GAP) for Gialpha and Goalphaand a guanine nucleotide dissociation inhibitor (GDI) for Gialpha. This GDI activity is isolated to a region of the protein distinct from the RGS domain that contains an additional G protein-binding domain (RBD/GL). Here, we report that RGS14 missing its RGS domain (R14-RBD/GL) binds directly to Go and Gi to modulate nucleotide binding and hydrolysis by mechanisms distinct from its defined GDI activity.

Methods for measuring RGS protein phosphorylation by G protein-regulated kinases.

Little is known about cellular regulation of the regulators of G protein signaling (RGS) proteins, principal players in G protein signaling. These proteins are known for their capacity to negatively regulate G protein signals, however, their chief cellular functions may expand beyond this limited role. Comprehensive understanding of cellular roles of RGS proteins requires knowledge of their regulation by short latency and inducible signals, such as kinase activation by G proteins.

Phosphorylation of RGS14 by protein kinase A potentiates its activity toward G alpha i.

Regulators of G protein signaling (RGS proteins) modulate Galpha-directed signals because of the GTPase activating protein (GAP) activity of their conserved RGS domain. RGS14 and RGS12 are unique among RGS proteins in that they also regulate Galpha(i) signals because of the guanine nucleotide dissociation inhibitor (GDI) activity of a GoLoco motif near their carboxy-termini. Little is known about cellular regulation of RGS proteins, although several are phosphorylated in response to G-protein directed signals.

Cellular regulation of RGS proteins: modulators and integrators of G protein signaling.

Regulators of G protein signaling (RGS) and RGS-like proteins are a family (>30 members) of highly diverse, multifunctional signaling proteins that bind directly to activated G alpha subunits. Family members are defined by a shared RGS domain, which is responsible for G alpha binding and markedly stimulates the GTPase activity of G alpha subunits leading to their deactivation and termination of downstream signals. Although much has been learned in recent years about the biochemistry of RGS/G alpha interactions, considerably less is known about the broader cellular roles and regulation of RGS proteins.