scholarly journals Visualization of Protein Sorting at the Trans-Golgi Network and Endosomes Through Super-Resolution Imaging

2019 ◽  
Vol 7 ◽  
Author(s):  
Yan Huang ◽  
Tianji Ma ◽  
Pik Ki Lau ◽  
Jinhui Wang ◽  
Teng Zhao ◽  
...  
Keyword(s):  
Protein Sorting ◽  
Super Resolution ◽  
Trans Golgi Network ◽  
Resolution Imaging ◽  
Golgi Network

scholarly journals Dynamic Behavior of the trans-Golgi Network in Root Tissues of Arabidopsis Revealed by Super-Resolution Live Imaging

2014 ◽  
Vol 55 (4) ◽  
pp. 694-703 ◽  
Author(s):  
Tomohiro Uemura ◽  
Yasuyuki Suda ◽  
Takashi Ueda ◽  
Akihiko Nakano
Keyword(s):  
Dynamic Behavior ◽  
Super Resolution ◽  
Live Imaging ◽  
Trans Golgi Network ◽  
Root Tissues ◽  
Golgi Network

scholarly journals Influenza M2 Proton Channel Activity Selectively Inhibits Trans-Golgi Network Release of Apical Membrane and Secreted Proteins in Polarized Madin-Darby Canine Kidney Cells

2000 ◽  
Vol 148 (3) ◽  
pp. 495-504 ◽  
Author(s):  
Jennifer R. Henkel ◽  
Gregory A. Gibson ◽  
Paul A. Poland ◽  
Mark A. Ellis ◽  
Rebecca P. Hughey ◽  
...  
Keyword(s):  
Ion Channel ◽  
Apical Membrane ◽  
Mdck Cells ◽  
Protein Sorting ◽  
Madin Darby Canine Kidney ◽  
Trans Golgi Network ◽  
Golgi Network ◽  
Kinetics Of ◽  
Darby Canine Kidney ◽  
Canine Kidney

The function of acidification in protein sorting along the biosynthetic pathway has been difficult to elucidate, in part because reagents used to alter organelle pH affect all acidified compartments and are poorly reversible. We have used a novel approach to examine the role of acidification in protein sorting in polarized Madin-Darby canine kidney (MDCK) cells. We expressed the influenza virus M2 protein, an acid-activated ion channel that equilibrates lumenal and cytosolic pH, in polarized MDCK cells and examined the consequences on the targeting and delivery of apical and basolateral proteins. M2 activity affects the pH of only a subset of acidified organelles, and its activity can be rapidly reversed using ion channel blockers (Henkel, J.R., G. Apodaca, Y. Altschuler, S. Hardy, and O.A. Weisz. 1998. Mol. Biol. Cell. 8:2477–2490; Henkel, J.R., J.L. Popovich, G.A. Gibson, S.C. Watkins, and O.A. Weisz. 1999. J. Biol. Chem. 274:9854–9860). M2 expression significantly decreased the kinetics of cell surface delivery of the apical membrane protein influenza hemagglutinin, but not of the basolaterally delivered polymeric immunoglobulin receptor. Similarly, the kinetics of apical secretion of a soluble form of γ-glutamyltranspeptidase were reduced with no effect on the basolaterally secreted fraction. Interestingly, M2 activity had no effect on the rate of secretion of a nonglycosylated protein (human growth hormone [hGH]) that was secreted equally from both surfaces. However, M2 slowed apical secretion of a glycosylated mutant of hGH that was secreted predominantly apically. Our results suggest a role for acidic trans-Golgi network pH in signal-mediated loading of apical cargo into forming vesicles.

scholarly journals The Adaptor Complex AP-4 Regulates Vacuolar Protein Sorting at the trans-Golgi Network by Interacting with VACUOLAR SORTING RECEPTOR1

2015 ◽  
Vol 170 (1) ◽  
pp. 211-219 ◽  
Author(s):  
Kentaro Fuji ◽  
Makoto Shirakawa ◽  
Yuki Shimono ◽  
Tadashi Kunieda ◽  
Yoichiro Fukao ◽  
...  
Keyword(s):  
Protein Sorting ◽  
Vacuolar Protein Sorting ◽  
Trans Golgi Network ◽  
Vacuolar Sorting ◽  
Vacuolar Protein ◽  
Golgi Network

scholarly journals CONTINUOUS VASCULAR RING (COV1) is a trans-Golgi Network-Localized Membrane Protein Required for Golgi Morphology and Vacuolar Protein Sorting

2014 ◽  
Vol 55 (4) ◽  
pp. 764-772 ◽  
Author(s):  
Makoto Shirakawa ◽  
Haruko Ueda ◽  
Yasuko Koumoto ◽  
Kentaro Fuji ◽  
Chiaki Nishiyama ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Protein Sorting ◽  
Vascular Ring ◽  
Vacuolar Protein Sorting ◽  
Trans Golgi Network ◽  
Vacuolar Protein ◽  
Golgi Network

scholarly journals Synthetic Genetic Interactions With Temperature-Sensitive Clathrin in Saccharomyces cerevisiae: Roles for Synaptojanin-Like Inp53p and Dynamin-Related Vps1p in Clathrin-Dependent Protein Sorting at the trans-Golgi Network

Genetics ◽  
2000 ◽  
Vol 154 (1) ◽  
pp. 83-97
Author(s):  
Eric S Bensen ◽  
Giancarlo Costaguta ◽  
Gregory S Payne
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Molecular Mechanisms ◽  
Protein Transport ◽  
Protein Sorting ◽  
Genetic Interactions ◽  
Carboxypeptidase Y ◽  
Temperature Sensitive ◽  
Trans Golgi Network ◽  
Vacuolar Protein ◽  
Golgi Network

Abstract Clathrin is involved in selective protein transport at the Golgi apparatus and the plasma membrane. To further understand the molecular mechanisms underlying clathrin-mediated protein transport pathways, we initiated a genetic screen for mutations that display synthetic growth defects when combined with a temperature-sensitive allele of the clathrin heavy chain gene (chc1-521) in Saccharomyces cerevisiae. Mutations, when present in cells with wild-type clathrin, were analyzed for effects on mating pheromone α-factor precursor maturation and sorting of the vacuolar protein carboxypeptidase Y as measures of protein sorting at the yeast trans-Golgi network (TGN) compartment. By these criteria, two classes of mutants were obtained, those with and those without defects in protein sorting at the TGN. One mutant with unaltered protein sorting at the TGN contains a mutation in PTC1, a type 2c serine/threonine phosphatase with widespread influences. The collection of mutants displaying TGN sorting defects includes members with mutations in previously identified vacuolar protein sorting genes (VPS), including the dynamin family member VPS1. Striking genetic interactions were observed by combining temperature-sensitive alleles of CHC1 and VPS1, supporting the model that Vps1p is involved in clathrin-mediated vesicle formation at the TGN. Also in the spectrum of mutants with TGN sorting defects are isolates with mutations in the following: RIC1, encoding a product originally proposed to participate in ribosome biogenesis; LUV1, encoding a product potentially involved in vacuole and microtubule organization; and INP53, encoding a synaptojanin-like inositol polyphosphate 5-phosphatase. Disruption of INP53, but not the related INP51 and INP52 genes, resulted in α-factor maturation defects and exacerbated α-factor maturation defects when combined with chc1-521. Our findings implicate a wide variety of proteins in clathrin-dependent processes and provide evidence for the selective involvement of Inp53p in clathrin-mediated protein sorting at the TGN.

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