scholarly journals Membrane protein trafficking through the common apical endosome compartment of polarized Caco-2 cells.

1995 ◽  
Vol 6 (5) ◽  
pp. 597-610 ◽  
Author(s):  
A Knight ◽  
E Hughson ◽  
C R Hopkins ◽  
D F Cutler
Keyword(s):  
Membrane Protein ◽  
Protein Trafficking ◽  
Apical Plasma Membrane ◽  
Apical Surface ◽  
Egf Receptors ◽  
Differential Distribution ◽  
Apical Cytoplasm ◽  
Membrane Protein Trafficking ◽  
Pass Through ◽  
Gain Access

By raising monoclonal antibodies to the apical surface of Caco-2 cells we have identified a membrane protein (p100) that internalizes and recycles constitutively between the apical plasma membrane and endosomes in the apical cytoplasm. By applying tracers bound to the transferrin receptor, which internalizes and recycles back to the basolateral border, we demonstrate that the apical endosomes containing p100 include a subset of multivesticular bodies (MVB), which are also accessible to proteins arriving from the basolateral endosome. Tracers bound to EGF receptors and alpha-2-macroglobulin, which internalize from the basolateral border and are degraded, probably in lysosomes, also pass through the p100-containing MVB. These studies therefore suggest that the apical cytoplasm of Caco-2 cells contains a population of MVB capable of receiving membrane proteins trafficking in from both apical and basolateral borders and then routing them to a variety of cell surface and intracellular destinations. The differential distribution of apical and basolateral tracers within the 50-nm-diameter tubules connected to these p100-positive apical MVB suggests that the destination of proteins trafficking from the MVB back to apical and basolateral surfaces is determined by the tubules to which they gain access.

The transcytotic pathway of an apical plasma membrane protein (B10) in hepatocytes is similar to that of IgA and occurs via a tubular pericentriolar compartment

1996 ◽  
Vol 109 (6) ◽  
pp. 1215-1227 ◽  
Author(s):  
I. Hemery ◽  
A.M. Durand-Schneider ◽  
G. Feldmann ◽  
J.P. Vaerman ◽  
M. Maurice
Keyword(s):  
Electron Microscopy ◽  
Plasma Membrane ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Apical Membrane ◽  
Rat Hepatocytes ◽  
Apical Plasma Membrane ◽  
Apical Surface ◽  
Plasma Membrane Protein ◽  
Microtubule Disruption

In hepatocytes, newly synthesized apical plasma membrane proteins are first delivered to the basolateral surface and are supposed to reach the apical surface by transcytosis. The transcytotic pathway of apical membrane proteins and its relationship with other endosomal pathways has not been demonstrated morphologically. We compared the intracellular route of an apical plasma membrane protein, B10, with that of polymeric IgA (pIgA), which is transcytosed, transferrin (Tf) which is recycled, and asialoorosomucoid (ASOR) which is delivered to lysosomes. Ligands and anti-B10 monoclonal IgG were linked to fluorochromes or with peroxidase. The fate of each ligand was followed by confocal and electron microscopy in polarized primary monolayers of rat hepatocytes. When fluorescent anti-B10 IgG and fluorescent pIgA were simultaneously endocytosed for 15–30 minutes, they both uniformly labelled a juxtanuclear compartment. By 30–60 minutes, they reached the bile canaliculi. Tf and ASOR were also routed to the juxtanuclear area, but their fluorescence patterns were more punctate. Microtubule disruption prevented all ligands from reaching the juxtanuclear area. This area corresponded, at least partially, to the localization of the mannose 6-phosphate receptor, an endosomal marker. By electron microscopy, the juxtanuclear compartment was made up of anastomosing tubules connected to vacuoles, and was organized around the centrioles. B10 and pIgA were mainly found in the tubules, whereas ASOR was segregated inside the vacuolar elements and Tf within thinner, recycling tubules. In conclusion, transcytosis of the apical membrane protein B10 occurs inside tubules similar to those carrying pIgA, and involves passage via the pericentriolar area. In the pericentriolar area, the transcytotic tubules appear to maintain connections with other endosomal elements where sorting between recycled and degraded ligands occurs.

scholarly journals A rapid and affordable screening platform for membrane protein trafficking

BMC Biology ◽  
2015 ◽  
Vol 13 (1) ◽  
Author(s):  
Joshua C. Snyder ◽  
Thomas F. Pack ◽  
Lauren K. Rochelle ◽  
Subhasish K. Chakraborty ◽  
Ming Zhang ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Protein Trafficking ◽  
Membrane Protein Trafficking ◽  
Screening Platform

Ethanol and Membrane Protein Trafficking: Diverse Mechanisms of Ethanol Action

2002 ◽  
Vol 26 (2) ◽  
pp. 287-293 ◽  
Author(s):  
Laura E. Nagy ◽  
M. Raj Lakshman ◽  
Carol A. Casey ◽  
Cynthia F. Bearer
Keyword(s):  
Membrane Protein ◽  
Protein Trafficking ◽  
Membrane Protein Trafficking

scholarly journals Kv2.1 cell surface clusters are insertion platforms for ion channel delivery to the plasma membrane

2012 ◽  
Vol 23 (15) ◽  
pp. 2917-2929 ◽  
Author(s):  
Emily Deutsch ◽  
Aubrey V. Weigel ◽  
Elizabeth J. Akin ◽  
Phil Fox ◽  
Gentry Hansen ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Cell Surface ◽  
Ion Channel ◽  
Protein Trafficking ◽  
Hippocampal Neurons ◽  
Surface Membrane ◽  
Cell Types ◽  
Homogeneous Surface ◽  
Hek Cells ◽  
Membrane Protein Trafficking

Voltage-gated K+ (Kv) channels regulate membrane potential in many cell types. Although the channel surface density and location must be well controlled, little is known about Kv channel delivery and retrieval on the cell surface. The Kv2.1 channel localizes to micron-sized clusters in neurons and transfected human embryonic kidney (HEK) cells, where it is nonconducting. Because Kv2.1 is postulated to be involved in soluble N-ethylmaleimide–sensitive factor attachment protein receptor–mediated membrane fusion, we examined the hypothesis that these surface clusters are specialized platforms involved in membrane protein trafficking. Total internal reflection–based fluorescence recovery after photobleaching studies and quantum dot imaging of single Kv2.1 channels revealed that Kv2.1-containing vesicles deliver cargo at the Kv2.1 surface clusters in both transfected HEK cells and hippocampal neurons. More than 85% of cytoplasmic and recycling Kv2.1 channels was delivered to the cell surface at the cluster perimeter in both cell types. At least 85% of recycling Kv1.4, which, unlike Kv2.1, has a homogeneous surface distribution, is also delivered here. Actin depolymerization resulted in Kv2.1 exocytosis at cluster-free surface membrane. These results indicate that one nonconducting function of Kv2.1 is to form microdomains involved in membrane protein trafficking. This study is the first to identify stable cell surface platforms involved in ion channel trafficking.

scholarly journals Fluorogenic Probing of Membrane Protein Trafficking

2018 ◽  
Vol 29 (6) ◽  
pp. 1823-1828 ◽  
Author(s):  
Chenge Li ◽  
Aurélien Mourton ◽  
Marie-Aude Plamont ◽  
Vanessa Rodrigues ◽  
Isabelle Aujard ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Protein Trafficking ◽  
Membrane Protein Trafficking

scholarly journals Regulation of ciliary membrane protein trafficking and signalling by kinesin motor proteins

FEBS Journal ◽  
2018 ◽  
Vol 285 (24) ◽  
pp. 4535-4564 ◽  
Author(s):  
Stine Kjær Morthorst ◽  
Søren Tvorup Christensen ◽  
Lotte Bang Pedersen
Keyword(s):  
Membrane Protein ◽  
Protein Trafficking ◽  
Motor Proteins ◽  
Kinesin Motor ◽  
Ciliary Membrane ◽  
Membrane Protein Trafficking ◽  
Kinesin Motor Proteins
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