Role of the α subunit of heterotrimeric G-protein in probenazole-inducing defense signaling in rice

2003 ◽  
Vol 69 (1) ◽  
pp. 83-86 ◽  
Author(s):  
Michiaki Iwata ◽  
Kenji Umemura ◽  
Takeshi Teraoka ◽  
Hideki Usami ◽  
Yukiko Fujisawa ◽  
...  
2012 ◽  
Vol 550-553 ◽  
pp. 1196-1199
Author(s):  
Yuan Hua Zhang

By means of pharmacological approach and stomatal analysis,the role of G protein in light-regulated stomatal movement in Vicia faba L. was studied. The result shows that CTX, the activator of heterotrimeric G protein α-subunit, induced stomatal closure under light, but this effect can be reversed by ascorbic acid(Vc) and catalase(CAT). It indicated that G protein was blunted by light, and H2O2 may be one downsteam signal molecule in G protein participated light-regulated stomatal movement.


2004 ◽  
Vol 72 (12) ◽  
pp. 6826-6835 ◽  
Author(s):  
Ken Teter ◽  
Michael G. Jobling ◽  
Randall K. Holmes

ABSTRACT Cholera toxin (CT) moves from the cell surface to the endoplasmic reticulum (ER) by retrograde vesicular transport. The catalytic A1 polypeptide of CT (CTA1) then crosses the ER membrane, enters the cytosol, ADP-ribosylates the stimulatory α subunit of the heterotrimeric G protein (Gsα) at the cytoplasmic face of the plasma membrane, and activates adenylate cyclase. The cytosolic pool of CTA1 may reach the plasma membrane and its Gsα target by traveling on anterograde-directed transport vesicles. We examined this possibility with the use of a plasmid-based transfection system that directed newly synthesized CTA1 to either the ER lumen or the cytosol of CHO cells. Such a system allowed us to bypass the CT retrograde trafficking itinerary from the cell surface to the ER. Previous work has shown that the ER-localized pool of CTA1 is rapidly exported from the ER to the cytosol. Expression of CTA1 in either the ER or the cytosol led to the activation of Gsα, and Gsα activation was not inhibited in transfected cells exposed to drugs that inhibit vesicular traffic. Thus, anterograde transport from the ER to the plasma membrane is not required for the cytotoxic action of CTA1.


2016 ◽  
Vol 110 (3) ◽  
pp. 380a
Author(s):  
Ersoy Cholak ◽  
Ines Karmous ◽  
Bihter Avşar ◽  
Zehra Sayers

2000 ◽  
Vol 275 (3) ◽  
pp. 2157-2164 ◽  
Author(s):  
Jingzhen Yuan ◽  
Lee Slice ◽  
John H. Walsh ◽  
Enrique Rozengurt

2003 ◽  
Vol 131 (4) ◽  
pp. 1623-1627 ◽  
Author(s):  
Alan M. Jones ◽  
Joseph R. Ecker ◽  
Jin-Gui Chen

2019 ◽  
Vol 294 (15) ◽  
pp. 5747-5758 ◽  
Author(s):  
Davide Malfacini ◽  
Julian Patt ◽  
Suvi Annala ◽  
Kasper Harpsøe ◽  
Funda Eryilmaz ◽  
...  

Biochemistry ◽  
2006 ◽  
Vol 45 (43) ◽  
pp. 12986-12997 ◽  
Author(s):  
Najmoutin G. Abdulaev ◽  
Tony Ngo ◽  
Eva Ramon ◽  
Danielle M. Brabazon ◽  
John P. Marino ◽  
...  

2000 ◽  
Vol 78 (5) ◽  
pp. 537-550 ◽  
Author(s):  
Barbara Vanderbeld ◽  
Gregory M Kelly

Heterotrimeric G proteins are involved in numerous biological processes, where they mediate signal transduction from agonist-bound G-protein-coupled receptors to a variety of intracellular effector molecules and ion channels. G proteins consist of two signaling moieties: a GTP-bound α subunit and a βγ heterodimer. The βγ dimer, recently credited as a significant modulator of G-protein-mediated cellular responses, is postulated to be a major determinant of signaling fidelity between G-protein-coupled receptors and downstream effectors. In this review we have focused on the role of βγ signaling and have included examples to demonstrate the heterogeneity in the heterodimer composition and its implications in signaling fidelity. We also present an overview of some of the effectors regulated by βγ and draw attention to the fact that, although G proteins and their associated receptors play an instrumental role in development, there is rather limited information on βγ signaling in embryogenesis.Key words: G protein, βγ subunit, G-protein-coupled receptor, signal transduction, adenylyl cyclase.


2018 ◽  
Vol 41 (2) ◽  
pp. 451-468 ◽  
Author(s):  
Ángel Ferrero-Serrano ◽  
Zhao Su ◽  
Sarah M. Assmann

2009 ◽  
Vol 84 (1) ◽  
pp. 35-42 ◽  
Author(s):  
Katsuyuki Oki ◽  
Noriko Inaba ◽  
Hidemi Kitano ◽  
Sachiko Takahashi ◽  
Yukiko Fujisawa ◽  
...  

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