scholarly journals Post-cocaine changes in regulator of G-protein signaling (RGS) proteins in the dorsal striatum: Relevance for cocaine-seeking and protein kinase C-mediated phosphorylation

Synapse ◽  
2016 ◽  
Vol 70 (10) ◽  
pp. 432-440 ◽  
Author(s):  
Jenna Bilodeau ◽  
Marek Schwendt
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
G Protein ◽  
Dorsal Striatum ◽  
G Protein Signaling ◽  
Rgs Proteins ◽  
Protein Signaling ◽  
Kinase C ◽  
Cocaine Seeking

Protein Kinase C-η and Phospholipase D2 Pathway Regulates Foam Cell Formation via Regulator of G Protein Signaling 2

2010 ◽  
Vol 78 (3) ◽  
pp. 478-485 ◽  
Author(s):  
Hyung-Kyoung Lee ◽  
Seungeun Yeo ◽  
Jin-Sik Kim ◽  
Jin-Gu Lee ◽  
Yoe-Sik Bae ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
G Protein ◽  
Foam Cell ◽  
Cell Formation ◽  
Foam Cell Formation ◽  
G Protein Signaling ◽  
Protein Signaling ◽  
Kinase C ◽  
Phospholipase D2

Established and Emerging Fluorescence-Based Assays for G-Protein Function: Heterotrimeric G-Protein Alpha Subunits and Regulator of G-Protein Signaling (RGS) Proteins

2003 ◽  
Vol 6 (4) ◽  
pp. 399-407 ◽  
Author(s):  
Randall Kimple ◽  
Miller Jones ◽  
Adam Shutes ◽  
Benjamin Yerxa ◽  
David Siderovski ◽  
...  
Keyword(s):  
G Protein ◽  
Protein Function ◽  
G Protein Signaling ◽  
Rgs Proteins ◽  
Protein Signaling ◽  
Heterotrimeric G Protein ◽  
Alpha Subunits

scholarly journals Mechanism of inhibition of adenylate cyclase by phospholipase C-catalyzed hydrolysis of phosphatidylcholine. Involvement of a pertussis toxin-sensitive G protein and protein kinase C.

1991 ◽  
Vol 266 (2) ◽  
pp. 1170-1176
Author(s):  
I Diaz-Laviada ◽  
P Larrodera ◽  
J L Nieto ◽  
M E Cornet ◽  
M T Diaz-Meco ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Adenylate Cyclase ◽  
Phospholipase C ◽  
G Protein ◽  
Pertussis Toxin ◽  
Kinase C ◽  
Mechanism Of Inhibition ◽  
Hydrolysis Of

scholarly journals Identification of an Integration Center for Cross-talk between Protein Kinase C and G Protein Modulation of N-type Calcium Channels

1999 ◽  
Vol 274 (10) ◽  
pp. 6195-6202 ◽  
Author(s):  
Jawed Hamid ◽  
Donald Nelson ◽  
Renee Spaetgens ◽  
Stefan J. Dubel ◽  
Terry P. Snutch ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Calcium Channels ◽  
G Protein ◽  
Cross Talk ◽  
Kinase C

scholarly journals A Regulator of G Protein Signaling-containing Kinase Is Important for Chemotaxis and Multicellular Development inDictyostelium

2003 ◽  
Vol 14 (4) ◽  
pp. 1727-1743 ◽  
Author(s):  
Binggang Sun ◽  
Richard A. Firtel
Keyword(s):  
Protein Kinase ◽  
G Protein ◽  
Kinase Activity ◽  
Site Directed Mutagenesis ◽  
Membrane Localization ◽  
Pleckstrin Homology Domain ◽  
G Protein Signaling ◽  
Protein Signaling ◽  
Wild Type ◽  
Gene Encoding

We have identified a gene encoding RGS domain-containing protein kinase (RCK1), a novel regulator of G protein signaling domain-containing protein kinase. RCK1 mutant strains exhibit strong aggregation and chemotaxis defects. rck1 null cells chemotax ∼50% faster than wild-type cells, suggesting RCK1 plays a negative regulatory role in chemotaxis. Consistent with this finding, overexpression of wild-type RCK1 reduces chemotaxis speed by ∼40%. On cAMP stimulation, RCK1 transiently translocates to the membrane/cortex region with membrane localization peaking at ∼10 s, similar to the kinetics of membrane localization of the pleckstrin homology domain-containing proteins CRAC, Akt/PKB, and PhdA. RCK1 kinase activity also increases dramatically. The RCK1 kinase activity does not rapidly adapt, but decreases after the cAMP stimulus is removed. This is particularly novel considering that most other chemoattractant-activated kinases (e.g., Akt/PKB, ERK1, ERK2, and PAKa) rapidly adapt after activation. Using site-directed mutagenesis, we further show that both the RGS and kinase domains are required for RCK1 function and that RCK1 kinase activity is required for the delocalization of RCK1 from the plasma membrane. Genetic evidence suggests RCK1 function lies downstream from Gα2, the heterotrimeric G protein that couples to the cAMP chemoattractant receptors. We suggest that RCK1 might be part of an adaptation pathway that regulates aspects of chemotaxis in Dictyostelium.

scholarly journals Modulation of human erg K+channel gating by activation of a G protein-coupled receptor and protein kinase C

1998 ◽  
Vol 511 (2) ◽  
pp. 333-346 ◽  
Author(s):  
Francisco Barros ◽  
David Gómez-Varela ◽  
Cristina G. Viloria ◽  
Teresa Palomero ◽  
Teresa Giráldez ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
G Protein ◽  
Channel Gating ◽  
K Channel ◽  
G Protein Coupled Receptor ◽  
Kinase C ◽  
G Protein Coupled

scholarly journals Regulators of G protein Signaling (RGS) proteins (version 2020.4) in the IUPHAR/BPS Guide to Pharmacology Database

2020 ◽  
Vol 2020 (4) ◽  
Author(s):  
Katelin E. Ahlers-Dannen ◽  
Mohammed Alqinyah ◽  
Christopher Bodle ◽  
Josephine Bou Dagher ◽  
Bandana Chakravarti ◽  
...  
Keyword(s):  
G Protein ◽  
G Protein Coupled Receptors ◽  
Signaling Cascades ◽  
G Protein Signaling ◽  
Rgs Proteins ◽  
Protein Signaling ◽  
Heterotrimeric G Proteins ◽  
Gtp Hydrolysis ◽  
Rgs Domain ◽  
G Protein Coupled

Regulator of G protein Signaling, or RGS, proteins serve an important regulatory role in signaling mediated by G protein-coupled receptors (GPCRs). They all share a common RGS domain that directly interacts with active, GTP-bound Gα subunits of heterotrimeric G proteins. RGS proteins stabilize the transition state for GTP hydrolysis on Gα and thus induce a conformational change in the Gα subunit that accelerates GTP hydrolysis, thereby effectively turning off signaling cascades mediated by GPCRs. This GTPase accelerating protein (GAP) activity is the canonical mechanism of action for RGS proteins, although many also possess additional functions and domains. RGS proteins are divided into four families, R4, R7, R12 and RZ based on sequence homology, domain structure as well as specificity towards Gα subunits. For reviews on RGS proteins and their potential as therapeutic targets, see e.g. [160, 377, 411, 415, 416, 512, 519, 312, 6].

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