Gタンパク質調節タンパク質、RGSタンパク質

WordNet

any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"
the 18th letter of the Roman alphabet (同)r

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蛋白(たんばく)質
resistance / 17歳以下父兄同伴映画の表示 / rook

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/02/09 21:04:11」(JST)

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Regulators of G protein signaling (or RGS) are protein structural domains that activate GTPases for heterotrimeric G-protein alpha-subunits.

RGS proteins are multi-functional, GTPase-accelerating proteins that promote GTP hydrolysis by the alpha subunit of heterotrimeric G proteins, thereby inactivating the G protein and rapidly switching off G protein-coupled receptor signaling pathways.^[2] Upon activation by receptors, G proteins exchange GDP for GTP, are released from the receptor, and dissociate into a free, active GTP-bound alpha subunit and beta-gamma dimer, both of which activate downstream effectors. The response is terminated upon GTP hydrolysis by the alpha subunit (IPR001019), which can then re-bind the beta-gamma dimer (IPR001632 IPR001770) and the receptor. RGS proteins markedly reduce the lifespan of GTP-bound alpha subunits by stabilising the G protein transition state. Whereas receptors stimulate GTP binding, RGS proteins stimulate GTP hydrolysis.

RGS proteins have been conserved in evolution. The first to be identified was Sst2 ("SuperSensiTivity to pheromone") in yeast (Saccharomyces cerevisiae).^[3] All RGS proteins contain an RGS-box (or RGS domain), which is required for activity. Some small RGS proteins such as RGS1 and RGS4 are little more than an RGS domain, while others also contain additional domains that confer further functionality.^[4]

RGS domains can be found within the same protein in combination with a variety of other domains, including: DEP for membrane targeting (IPR000591), PDZ for binding to GPCRs (IPR001478), PTB for phosphotyrosine-binding (IPR006020), RBD for Ras-binding (IPR003116), GoLoco for guanine nucleotide inhibitor activity (IPR003109), PX for phosphoinositide-binding (IPR001683), PXA that is associated with PX (IPR003114), PH for phosphatidylinositol-binding (IPR001849), and GGL (G protein gamma subunit-like) for binding G protein beta subunits (IPR001770 Those RGS proteins that contain GGL domains can interact with G protein beta subunits to form novel dimers that prevent G protein gamma subunit binding and G protein alpha subunit association, thereby preventing heterotrimer formation.

Examples

Human proteins containing this domain include:

ADRBK1, ADRBK2, AXIN1, AXIN2
GRK1, GRK4, GRK5, GRK6, GRK7,
RGS1, RGS2, RGS3, RGS4, RGS5, RGS6, RGS7, RGS8, RGS9, RGS10, RGS11, RGS12, RGS13, RGS14, RGS16, RGS17, RGS18, RGS19, RGS20, RGS21
RK
SNX13

References

^ Coleman DE, Berghuis AM, Lee E, Linder ME, Gilman AG, Sprang SR (September 1994). "Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis". Science 265 (5177): 1405–12. doi:10.1126/science.8073283. PMID 8073283.
^ De Vries L, Farquhar MG, Zheng B, Fischer T, Elenko E (2000). "The regulator of G protein signaling family". Annu. Rev. Pharmacol. Toxicol. 40: 235–271. doi:10.1146/annurev.pharmtox.40.1.235. PMID 10836135.
^ Dohlman HG (2009). "RGS proteins the early days". Prog. Mol. Biol. Transl. Sci. 86: 1–14. doi:10.1016/S1877-1173(09)86001-8. PMID 20374711.
^ Burchett SA (2000). "Regulators of G protein signaling: a bestiary of modular protein binding domains". J. Neurochem. 75 (4): 1335–1351. doi:10.1046/j.1471-4159.2000.0751335.x. PMID 10987813.

External links

[1] in PROSITE

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English Journal

Reversible inhibitors of regulators of G-protein signaling identified in a high-throughput cell-based calcium signaling assay.

Storaska AJ, Mei JP, Wu M, Li M, Wade SM, Blazer LL, Sjögren B, Hopkins CR, Lindsley CW, Lin Z, Babcock JJ, McManus OB, Neubig RR.SourceDepartment of Pharmacology, University of Michigan, Ann Arbor, MI 48109, USA.
Cellular signalling.Cell Signal.2013 Dec;25(12):2848-55. doi: 10.1016/j.cellsig.2013.09.007. Epub 2013 Sep 14.
Regulator of G-protein signaling (RGS) proteins potently suppress G-protein coupled receptor (GPCR) signal transduction by accelerating GTP hydrolysis on activated heterotrimeric G-protein α subunits. RGS4 is enriched in the CNS and is proposed as a therapeutic target for treatment of neuropatholog
PMID 24041654

Activation of Gαq subunits up-regulates the expression of the tumor suppressor Fhit.

Zuo H, Chan AS, Ammer H, Wong YH.SourceDivision of Life Sciences, and the Biotechnology Research Institute, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong. Electronic address: hzuo@ust.hk.
Cellular signalling.Cell Signal.2013 Dec;25(12):2440-52. doi: 10.1016/j.cellsig.2013.08.019. Epub 2013 Aug 30.
The tumor suppressor Fhit protein is defective or absent in many tumor cells due to methylation, mutation or deletion of the FHIT gene. Despite numerous attempts to unravel the functions of Fhit, the mechanisms by which the function and expression of Fhit are regulated remain poorly understood. We h
PMID 23993961

Characterization of heterotrimeric G-protein complex and its regulator from the green alga Chara braunii expands the evolutionarily breadth of plant G-protein signaling.

Hackenberg D, Sakayama H, Nishiyama T, Pandey S.Source1 Donald Danforth Plant Science Center, 975 North Warson Road, St. Louis, MO, 63132, USA;
Plant physiology.Plant Physiol.2013 Oct 31. [Epub ahead of print]
The lack of heterotrimeric G-protein homologs in the sequenced genomes of green algae has led to the hypothesis that in plants, this signaling mechanism co-evolved with the embryophytic life cycle and acquisition of terrestrial habitat. Given the large evolutionary gap that exists between the chloro
PMID 24179134

Japanese Journal

Newly Identified Molecules Related to Podocyte Injury Induced by Adriamycin

WANG JUAN,ASANUMA KATSUHIKO,HIDAKA TERUO,SASAKI YU,TANAKA ERIKO,TAKAGI-AKIBA MIYUKI,ALEJANDRO OLIVA TREJO JUAN,TOMINO YASUHIKO
順天堂醫事雑誌 61(1), 34-40, 2015
… Two genes, Fos-like antigen 1 (FOSL1) and Regulator of G-protein signaling 2 (RGS2) were selected as candidate genes because their levels showed the most significant changes after ADR-induced podocyte injury. … To confirm the changes in mRNA levels and their protein expression, ADR was added to cultured mouse podocytes and analyzed at 1, 2, 6, and 24 hours using real-time PCR and immunofluorescence. …
NAID 130005085651

Roles of Accessory Proteins for Heterotrimeric G-Protein in the Development of Cardiovascular Diseases

SATO Motohiko
Circulation journal : official journal of the Japanese Circulation Society 77(10), 2455-2461, 2013-09-25
NAID 10031191778

Roles of Accessory Proteins for Heterotrimeric G-Protein in the Development of Cardiovascular Diseases

Sato Motohiko
Circulation Journal 77(10), 2455-2461, 2013
… The heterotrimeric G-protein signaling system includes the G-protein-coupled receptor (GPCR), heterotrimeric G-proteins, and effectors. … Such accessory proteins for heterotrimeric G-protein can provide additional signal input to the G-protein signaling system, or may act as alternative binding partners of G-protein subunits serving as yet unknown roles in cells. …
NAID 130003361866

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「RGSタンパク質」

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Regulator of G-Protein Signaling Domain
	Structure of active conformation of Gi-alpha1
Identifiers
Symbol	RGS
Pfam	PF00615
InterPro	IPR000342
SMART	RGS
PROSITE	PDOC50132
SCOP	1gia
SUPERFAMILY	1gia
OPM protein	2bcj
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary