نتایج جستجو برای: rgs proteins

تعداد نتایج: 556426  

2005
Xin Li Lei Chen Chaoneng Ji Bing Liu Jiefeng Gu Jian Xu Xianqiong Zou Shaohua Gu Yumin Mao

Regulators of G-protein signaling (RGS) proteins are known for the RGS domain that is composed of a conserved stretch of 120 amino acids, which binds directly to activated G-protein α subunits and acts as a GTPase-activating protein (GAP), leading to their deactivation and termination of downstream signals. In this study, a novel human RGS cDNA (RGS21), 1795 bp long and encoding a 152-amino aci...

Journal: :The Journal of biological chemistry 1999
O Saitoh Y Kubo M Odagiri M Ichikawa K Yamagata T Sekine

The recently discovered family of RGS (regulators of G protein signaling) proteins acts as GTPase activating proteins which bind to alpha subunits of heterotrimeric G proteins. We previously showed that a brain-specific RGS, RGS8 speeds up the activation and deactivation kinetics of the G protein-coupled inward rectifier K+ channel (GIRK) upon receptor stimulation (Saitoh, O., Kubo, Y., Miyatan...

Journal: :Acta biochimica Polonica 2005
Xin Li Lei Chen Chaoneng Ji Bing Liu Jiefeng Gu Jian Xu Xianqiong Zou Shaohua Gu Yumin Mao

Regulators of G-protein signaling (RGS) proteins are known for the RGS domain that is composed of a conserved stretch of 120 amino acids, which binds directly to activated G-protein alpha subunits and acts as a GTPase-activating protein (GAP), leading to their deactivation and termination of downstream signals. In this study, a novel human RGS cDNA (RGS21), 1795 bp long and encoding a 152-amino...

2016
Nicole E. Brown Nevin A. Lambert John R. Hepler

RGS14 is a multifunctional scaffolding protein possessing two distinct G protein interaction sites including a regulator of G protein signaling (RGS) domain that acts as a GTPase activating protein (GAP) to deactivate Gαi/o-GTP proteins, and a G protein regulatory (GPR) motif that binds inactive Gαi1/3-GDP proteins independent of Gβγ. GPR interactions with Gαi recruit RGS14 to the plasma membra...

Journal: :Cell 1996
David M Berman Thomas M Wilkie Alfred G Gilman

terized G protein GAP is phospholipase C-b, which is Summary both a GAP for Gqa and the effector that is activated by that G protein (Berstein et al., 1992; Biddlecome et al., A novel class of regulators of G protein signaling (RGS) 1996). The GTPase activity of the a subunit of transducin proteins has been identified recently. Genetic eviis also stimulated by its effector, the g subunit of a r...

Journal: :American journal of physiology. Heart and circulatory physiology 2007
Ying Fu Xinyan Huang Lin Piao Anatoli N Lopatin Richard R Neubig

G protein-coupled receptors play a pivotal role in regulating cardiac automaticity. Their function is controlled by regulator of G protein signaling (RGS) proteins acting as GTPase-activating proteins for Galpha subunits to suppress Galpha(i) and Galpha(q) signaling. Using knock-in mice in which Galpha(i2)-RGS binding and negative regulation are disrupted by a genomic Galpha(i2)G184S (GS) point...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1996
C K Chen T Wieland M I Simon

G proteins regulate intracellular signaling by coupling a cycle of guanine nucleotide binding and hydrolysis to transient changes of cellular functions. The mechanisms that control the recycling of transducin, the "pacesetting" G protein that regulates mammalian phototransduction, are unclear. We show that a novel retinal specific RGS-motif protein specifically binds to an intermediate conforma...

2001
Masaru Ishii Atsushi Inanobe Satoru Fujita Yasunaka Makino Yukio Hosoya Yoshihisa Kurachi

Regulators of G protein signaling (RGS), which act as GTPase activators, are a family of cytosolic proteins emerging rapidly as an important means of controlling G protein–mediated cell signals. The importance of RGS action has been verified in vitro for various kinds of cell function. Their in situ modes of action in intact cells are, however, poorly understood. Here we show that an increase i...

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