scholarly journals Modulatory ATP binding to the E2 state of maize plasma membrane H+-ATPase indicated by the kinetics of vanadate inhibition

FEBS Journal ◽  
2013 ◽  
Vol 280 (19) ◽  
pp. 4793-4806 ◽  
Author(s):  
Xiaozhi Wang ◽  
Xiaoqing Qian ◽  
Beate Stumpf ◽  
Ammara Fatima ◽  
Ke Feng ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Atp Binding ◽  
Vanadate Inhibition ◽  
Kinetics Of

scholarly journals Overexpression in Escherichia coli and purification of an ATP-binding peptide from the yeast plasma membrane H(+)-ATPase.

1993 ◽  
Vol 268 (29) ◽  
pp. 21895-21900
Author(s):  
E Capieaux ◽  
C Rapin ◽  
D Thinès ◽  
Y Dupont ◽  
A Goffeau
Keyword(s):  
Escherichia Coli ◽  
Plasma Membrane ◽  
Atp Binding ◽  
Binding Peptide ◽  
Yeast Plasma Membrane

scholarly journals Insulin Stimulates Membrane Fusion and GLUT4 Accumulation in Clathrin Coats on Adipocyte Plasma Membranes

2007 ◽  
Vol 27 (9) ◽  
pp. 3456-3469 ◽  
Author(s):  
Shaohui Huang ◽  
Larry M. Lifshitz ◽  
Christine Jones ◽  
Karl D. Bellve ◽  
Clive Standley ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Membrane Fusion ◽  
Insulin Signaling ◽  
Plasma Membranes ◽  
Glucose Transporter ◽  
Fluorescent Protein ◽  
Fluorescent Proteins ◽  
Tirf Microscopy ◽  
Adipocyte Plasma Membranes ◽  
Kinetics Of

ABSTRACT Total internal reflection fluorescence (TIRF) microscopy reveals highly mobile structures containing enhanced green fluorescent protein-tagged glucose transporter 4 (GLUT4) within a zone about 100 nm beneath the plasma membrane of 3T3-L1 adipocytes. We developed a computer program (Fusion Assistant) that enables direct analysis of the docking/fusion kinetics of hundreds of exocytic fusion events. Insulin stimulation increases the fusion frequency of exocytic GLUT4 vesicles by ∼4-fold, increasing GLUT4 content in the plasma membrane. Remarkably, insulin signaling modulates the kinetics of the fusion process, decreasing the vesicle tethering/docking duration prior to membrane fusion. In contrast, the kinetics of GLUT4 molecules spreading out in the plasma membrane from exocytic fusion sites is unchanged by insulin. As GLUT4 accumulates in the plasma membrane, it is also immobilized in punctate structures on the cell surface. A previous report suggested these structures are exocytic fusion sites (Lizunov et al., J. Cell Biol. 169:481-489, 2005). However, two-color TIRF microscopy using fluorescent proteins fused to clathrin light chain or GLUT4 reveals these structures are clathrin-coated patches. Taken together, these data show that insulin signaling accelerates the transition from docking of GLUT4-containing vesicles to their fusion with the plasma membrane and promotes GLUT4 accumulation in clathrin-based endocytic structures on the plasma membrane.

The effects of acetylcholine and atropine on the 22Na+ permeability of intestinal smooth muscle vesicles

1978 ◽  
Vol 56 (6) ◽  
pp. 921-925
Author(s):  
L. Spero
Keyword(s):  
Smooth Muscle ◽  
Plasma Membrane ◽  
Membrane Vesicles ◽  
Intestinal Smooth Muscle ◽  
Erythrocyte Ghosts ◽  
Muscarinic Agonists ◽  
Plasma Membrane Vesicles ◽  
Muscle Plasma Membrane ◽  
Whole Muscle ◽  
Kinetics Of

A technique is described which has enabled us to measure changes in 22Na+ efflux from smooth muscle plasma membrane vesicles. The resting 22Na+ efflux from these sealed vesicles showed a concentration-dependent increase in response to acetylcholine and other muscarinic agonists, in similar concentrations to those which increased 42K+ efflux in whole muscle. The kinetics of this efflux were complex and could not be described by less than three exponential processes. The response to agonists has, therefore, been characterized by measurement of the half-life of 22Na+ efflux (t1/2). The acetylcholine effect was inhibited by atropine, but unlike the situation in the whole muscle, this inhibition was noncompetitive. Tubocuraine (a nicotinic antagonist) had no effect on this acetylcholine response. Atropine has no effect by itself on the resting 22Na+ efflux, neither did tetrodotoxin or ouabain. 22Na+ efflux from erythrocyte ghosts and liposomes, prepared from lipid extracts of the smooth muscle plasma membrane, was not modified by acetylcholine or atropine.

scholarly journals Two B-type ATP-binding cassette (ABC) transporters localize to the plasma membrane in Thalictrum minus

2015 ◽  
Vol 32 (3) ◽  
pp. 243-247 ◽  
Author(s):  
Nobukazu Shitan ◽  
Kazuyoshi Terasaka ◽  
Hirobumi Yamamoto ◽  
Fumihiko Sato ◽  
Kazufumi Yazaki
Keyword(s):  
Plasma Membrane ◽  
Abc Transporters ◽  
Atp Binding ◽  
Thalictrum Minus ◽  
Atp Binding Cassette

Distribution of plasma membrane rosettes and kinetics of cellulose formation in xylem development of higher plants

PROTOPLASMA ◽  
1986 ◽  
Vol 131 (2) ◽  
pp. 142-152 ◽  
Author(s):  
B. Schneider ◽  
W. Herth
Keyword(s):  
Plasma Membrane ◽  
Higher Plants ◽  
Xylem Development ◽  
Kinetics Of

The Kinetics of Quinine Blockade of the Maxi Cation Channel in the Plasma Membrane of Rye Roots

1998 ◽  
Vol 164 (3) ◽  
pp. 275-281 ◽  
Author(s):  
P.J. White
Keyword(s):  
Plasma Membrane ◽  
Cation Channel ◽  
Kinetics Of

scholarly journals Kinetics of activation of thymocyte plasma membrane adenylate cyclase by AMP-PPS and by other stimulatory agents

FEBS Letters ◽  
1978 ◽  
Vol 90 (1) ◽  
pp. 157-161 ◽  
Author(s):  
Ariane Monneron ◽  
Jacques d'Alayer
Keyword(s):  
Plasma Membrane ◽  
Adenylate Cyclase ◽  
Kinetics Of
Sign in / Sign up

Export Citation Format

Share Document