Elementary auxin response chains at the plasma membrane involve external abp1 and multiple electrogenic ion transport proteins

1996 ◽  
Vol 18 (1-2) ◽  
pp. 23-28 ◽  
Author(s):  
H�l�ne Barbier-Brygoo ◽  
Sabine Zimmermann ◽  
S�bastien Thomine ◽  
Ian R. White ◽  
Paul Millner ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Ion Transport ◽  
Transport Proteins ◽  
Auxin Response ◽  
Electrogenic Ion Transport ◽  
Response Chains

A PANI supported lipid bilayer that contains NhaA transporter proteins provides a basis for a biomimetic biocapacitor

2019 ◽  
Vol 55 (87) ◽  
pp. 13152-13155
Author(s):  
Awatef Ben Tahar ◽  
Abdelkader Zebda ◽  
Jean-Pierre Alcaraz ◽  
Landry Gayet ◽  
Abderrahim Boualam ◽  
...  
Keyword(s):  
Ion Transport ◽  
Lipid Bilayer ◽  
High Speed ◽  
Membrane System ◽  
Transport Proteins ◽  
Biological Engineering ◽  
Supported Lipid Bilayer ◽  
Transporter Proteins ◽  
Electrogenic Ion Transport ◽  
Biomimetic Membrane

This biomimetic membrane system of Na+/H+ transport proteins in a lipid bilayer supported by polyanaline has controllable electrogenic ion transport to function as a high-speed rechargeable biocapacitor for use in bioinspired biological engineering.

Role of membrane trafficking in plasma membrane solute transport

1994 ◽  
Vol 267 (1) ◽  
pp. C1-C24 ◽  
Author(s):  
N. A. Bradbury ◽  
R. J. Bridges
Keyword(s):  
Plasma Membrane ◽  
Solute Transport ◽  
Membrane Trafficking ◽  
Molecular Mechanisms ◽  
Glucose Transporter ◽  
Water Channel ◽  
Transport Proteins ◽  
Transmembrane Conductance Regulator ◽  
Transmembrane Conductance ◽  
Regulated Trafficking

Cells can rapidly and reversibly alter solute transport rates by changing the kinetics of transport proteins resident within the plasma membrane. Most notably, this can be brought about by reversible phosphorylation of the transporter. An additional mechanism for acute regulation of plasma membrane transport rates is by the regulated exocytic insertion of transport proteins from intracellular vesicles into the plasma membrane and their subsequent regulated endocytic retrieval. Over the past few years, the number of transporters undergoing this regulated trafficking has increased dramatically, such that what was once an interesting translocation of a few transporters has now become a widespread modality for regulating plasma membrane solute permeabilities. The aim of this article is to review the models proposed for the regulated trafficking of transport proteins and what lines of evidence should be obtained to document regulated exocytic insertion and endocytic retrieval of transport proteins. We highlight four transporters, the insulin-responsive glucose transporter, the antidiuretic hormone-responsive water channel, the urinary bladder H(+)-ATPase, and the cystic fibrosis transmembrane conductance regulator Cl- channel, and discuss the various approaches taken to document their regulated trafficking. Finally, we discuss areas of uncertainty that remain to be investigated concerning the molecular mechanisms involved in regulating the trafficking of proteins.

scholarly journals Enterohemorrhagic E. coli (EHEC)—Secreted Serine Protease EspP Stimulates Electrogenic Ion Transport in Human Colonoid Monolayers

Toxins ◽  
2018 ◽  
Vol 10 (9) ◽  
pp. 351 ◽  
Author(s):  
C. Tse ◽  
Julie In ◽  
Jianyi Yin ◽  
Mark Donowitz ◽  
Michele Doucet ◽  
...  
Keyword(s):  
Ion Transport ◽  
Serine Protease ◽  
Shiga Toxin ◽  
Short Circuit ◽  
Ussing Chamber ◽  
Adult Stem Cell ◽  
Short Circuit Current ◽  
Watery Diarrhea ◽  
E Coli ◽  
Electrogenic Ion Transport

One of the characteristic manifestations of Shiga-toxin-producing Escherichia coli (E. coli) infection in humans, including EHEC and Enteroaggregative E. coli O104:H4, is watery diarrhea. However, neither Shiga toxin nor numerous components of the type-3 secretion system have been found to independently elicit fluid secretion. We used the adult stem-cell-derived human colonoid monolayers (HCM) to test whether EHEC-secreted extracellular serine protease P (EspP), a member of the serine protease family broadly expressed by diarrheagenic E. coli can act as an enterotoxin. We applied the Ussing chamber/voltage clamp technique to determine whether EspP stimulates electrogenic ion transport indicated by a change in short-circuit current (Isc). EspP stimulates Isc in HCM. The EspP-stimulated Isc does not require protease activity, is not cystic fibrosis transmembrane conductance regulator (CFTR)-mediated, but is partially Ca2+-dependent. EspP neutralization with a specific antibody reduces its potency in stimulating Isc. Serine Protease A, secreted by Enteroaggregative E. coli, also stimulates Isc in HCM, but this current is CFTR-dependent. In conclusion, EspP stimulates colonic CFTR-independent active ion transport and may be involved in the pathophysiology of EHEC diarrhea. Serine protease toxins from E. coli pathogens appear to serve as enterotoxins, potentially significantly contributing to watery diarrhea.

Evidence for an electrogenic ion transport pump in cells of higher plants

1970 ◽  
Vol 3 (1) ◽  
pp. 210-222 ◽  
Author(s):  
N. Higinbotham ◽  
J. S. Graves ◽  
R. F. Davis
Keyword(s):  
Ion Transport ◽  
Higher Plants ◽  
Electrogenic Ion Transport ◽  
In Cells

Electrogenic Ion Transport along the Human Duodenum in Childhood

1997 ◽  
Vol 32 (9) ◽  
pp. 894-899 ◽  
Author(s):  
A. Reims ◽  
S. Redfors ◽  
M. Hemlin ◽  
A. Mellander ◽  
B. Strandvik
Keyword(s):  
Ion Transport ◽  
Electrogenic Ion Transport

Use of plasma membrane vesicles

1980 ◽  
Vol 238 (3) ◽  
pp. G151-G164 ◽  
Author(s):  
G. Sachs ◽  
R. J. Jackson ◽  
E. C. Rabon
Keyword(s):  
Plasma Membrane ◽  
Membrane Vesicles ◽  
Transport Proteins ◽  
Plasma Membrane Vesicles

A summary of current methodologies employed to obtain and characterize epithelial plasma membrane vesicles is presented. Particular emphasis is placed on techniques to evaluate such parameters as homogeneity, tightness, orientation, and the percentage of active vesicles in a given vesicular population. Examples of isotopic, osmotic, and various probe techniques useful for quantitation of transport events and associated electrical phenomena are illustrated. Finally, the unique problems intrinsic to purification and reconstitution of transport proteins are briefly discussed.

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