scholarly journals DKWSLLL, a Versatile DXXXLL-Type Signal with Distinct Roles in the Cu+-Regulated Trafficking of ATP7B

Traffic ◽  
2014 ◽  
Vol 15 (8) ◽  
pp. 839-860 ◽  
Author(s):  
Vasiliki Lalioti ◽  
Sonia Hernandez-Tiedra ◽  
Ignacio V. Sandoval
Keyword(s):  
Regulated Trafficking

scholarly journals SNARE phosphorylation: a control mechanism for insulin-stimulated glucose transport and other regulated exocytic events

2017 ◽  
Vol 45 (6) ◽  
pp. 1271-1277 ◽  
Author(s):  
Kamilla M.E. Laidlaw ◽  
Rachel Livingstone ◽  
Mohammed Al-Tobi ◽  
Nia J. Bryant ◽  
Gwyn W. Gould
Keyword(s):  
Membrane Fusion ◽  
Molecular Mechanisms ◽  
Membrane Receptors ◽  
Multivesicular Bodies ◽  
Attachment Protein ◽  
Protein Receptor ◽  
Sensitive Factor ◽  
Plasma Membrane Receptors ◽  
Regulated Trafficking ◽  
Receptor Family

Trafficking within eukaryotic cells is a complex and highly regulated process; events such as recycling of plasma membrane receptors, formation of multivesicular bodies, regulated release of hormones and delivery of proteins to membranes all require directionality and specificity. The underpinning processes, including cargo selection, membrane fusion, trafficking flow and timing, are controlled by a variety of molecular mechanisms and engage multiple families of lipids and proteins. Here, we will focus on control of trafficking processes via the action of the SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) family of proteins, in particular their regulation by phosphorylation. We will describe how these proteins are controlled in a range of regulated trafficking events, with particular emphasis on the insulin-stimulated delivery of glucose transporters to the surface of adipose and muscle cells. Here, we focus on a few examples of SNARE phosphorylation which exemplify distinct ways in which SNARE machinery phosphorylation may regulate membrane fusion.

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.

Developmentally regulated trafficking of the lysosomal membrane protein p67 in Trypanosoma brucei

2002 ◽  
Vol 115 (16) ◽  
pp. 3253-3263 ◽  
Author(s):  
David L. Alexander ◽  
Kevin J. Schwartz ◽  
Andrew E. Balber ◽  
James D. Bangs
Keyword(s):  
Cell Surface ◽  
Trypanosoma Brucei ◽  
Membrane Glycoprotein ◽  
Type I ◽  
Developmentally Regulated ◽  
Lysosomal Membrane Protein ◽  
Targeting Signals ◽  
Lysosomal Targeting ◽  
Endocytic Activity ◽  
Regulated Trafficking

p67 is a lysosomal type I membrane glycoprotein of Trypanosoma brucei. In procyclic stage cells p67 trafficks to the lysosome without modification, but in the bloodstream stage Golgi processing adds poly-N-acetyllactosamine to N-glycans. In both stages proteolytic fragmentation occurs in the lysosome, but turnover is approximately nine times faster in bloodstream cells. Trafficking of wildtype p67 and mutants missing the cytoplasmic (p67ΔCD) or cytoplasmic/transmembrane domains (p67ΔTM) was monitored by pulse-chase,surface biotinylation and immunofluorescence. Overexpressed wildtype p67 trafficks normally in procyclics, but some leaks to the cell surface suggesting that the targeting machinery is saturable. p67ΔCD and p67ΔTM are delivered to the cell surface and secreted, respectively. The membrane/cytoplasmic domains function correctly in procyclic cells when fused to GFP indicating that these domains are sufficient for stage-specific lysosomal targeting. In contrast, p67 wildtype and deletion reporters are overwhelmingly targeted to the lysosome and degraded in bloodstream cells. These findings suggest that either redundant developmentally regulated targeting signals/machinery are operative in this stage or that the increased endocytic activity of bloodstream cells prevents export of the deletion reporters.

scholarly journals Golgin-160 Is Required for the Golgi Membrane Sorting of the Insulin-responsive Glucose Transporter GLUT4 in Adipocytes

2006 ◽  
Vol 17 (12) ◽  
pp. 5346-5355 ◽  
Author(s):  
Dumaine Williams ◽  
Stuart W. Hicks ◽  
Carolyn E. Machamer ◽  
Jeffrey E. Pessin
Keyword(s):  
Plasma Membrane ◽  
Membrane Trafficking ◽  
Glucose Transporter ◽  
General Distribution ◽  
Amino Terminal ◽  
Vesicular Stomatitis ◽  
Glucose Transporter Glut4 ◽  
Golgi Network ◽  
Interfering Rna ◽  
Regulated Trafficking

The peripheral Golgi protein golgin-160 is induced during 3T3L1 adipogenesis and is primarily localized to the Golgi cisternae distinct from the trans-Golgi network (TGN) in a general distribution similar to p115. Small interfering RNA (siRNA)-mediated reduction in golgin-160 protein resulted in an increase accumulation of the insulin-responsive amino peptidase (IRAP) and the insulin-regulated glucose transporter (GLUT4) at the plasma membrane concomitant with enhanced glucose uptake in the basal state. The redistribution of GLUT4 was rescued by expression of a siRNA-resistant golgin-160 cDNA. The basal state accumulation of plasma membrane GLUT4 occurred due to an increased rate of exocytosis without any significant effect on the rate of endocytosis. This GLUT4 trafficking to the plasma membrane in the absence of golgin-160 was independent of TGN/Golgi sorting, because it was no longer inhibited by the expression of a dominant-interfering Golgi-localized, γ-ear–containing ARF-binding protein mutant and displayed reduced binding to the lectin wheat germ agglutinin. Moreover, expression of the amino terminal head domain (amino acids 1–393) had no significant effect on the distribution or insulin-regulated trafficking of GLUT4 or IRAP. In contrast, expression of carboxyl α helical region (393–1498) inhibited insulin-stimulated GLUT4 and IRAP translocation, but it had no effect on the sorting of constitutive membrane trafficking proteins, the transferrin receptor, or vesicular stomatitis virus G protein. Together, these data demonstrate that golgin-160 plays an important role in directing insulin-regulated trafficking proteins toward the insulin-responsive compartment in adipocytes.

scholarly journals A Combined Transgenic Proteomic Analysis and Regulated Trafficking of Neuroligin-2

2014 ◽  
Vol 289 (42) ◽  
pp. 29350-29364 ◽  
Author(s):  
Yunhee Kang ◽  
Yuan Ge ◽  
Robert M. Cassidy ◽  
Vivian Lam ◽  
Lin Luo ◽  
...  
Keyword(s):  
Proteomic Analysis ◽  
Regulated Trafficking

scholarly journals Maintaining protein homeostasis: early and late endosomal dual recycling for the maintenance of intracellular pools of the plasma membrane protein Chs3

2016 ◽  
Vol 27 (25) ◽  
pp. 4021-4032 ◽  
Author(s):  
Irene Arcones ◽  
Carlos Sacristán ◽  
Cesar Roncero
Keyword(s):  
Plasma Membrane ◽  
Yeast Cells ◽  
Protein Homeostasis ◽  
Intracellular Traffic ◽  
Escrt Machinery ◽  
Retromer Complex ◽  
Combined Action ◽  
Golgi Network ◽  
Regulated Trafficking ◽  
Timely Delivery

The major chitin synthase activity in yeast cells, Chs3, has become a paradigm in the study of the intracellular traffic of transmembrane proteins due to its tightly regulated trafficking. This includes an efficient mechanism for the maintenance of an extensive reservoir of Chs3 at the trans-Golgi network/EE, which allows for the timely delivery of the protein to the plasma membrane. Here we show that this intracellular reservoir of Chs3 is maintained not only by its efficient AP-1–mediated recycling, but also by recycling through the retromer complex, which interacts with Chs3 at a defined region in its N-terminal cytosolic domain. Moreover, the N-terminal ubiquitination of Chs3 at the plasma membrane by Rsp5/Art4 distinctly labels the protein and regulates its retromer-mediated recycling by enabling Chs3 to be recognized by the ESCRT machinery and degraded in the vacuole. Therefore the combined action of two independent but redundant endocytic recycling mechanisms, together with distinct labels for vacuolar degradation, determines the final fate of the intracellular traffic of the Chs3 protein, allowing yeast cells to regulate morphogenesis, depending on environmental constraints.

scholarly journals Activity-regulated trafficking of the palmitoyl-acyl transferase DHHC5

2015 ◽  
Vol 6 (1) ◽  
Author(s):  
G. Stefano Brigidi ◽  
Brendan Santyr ◽  
Jordan Shimell ◽  
Blair Jovellar ◽  
Shernaz X. Bamji
Keyword(s):  
Acyl Transferase ◽  
Regulated Trafficking

scholarly journals Activation-induced subcellular redistribution of Gs alpha.

1996 ◽  
Vol 7 (8) ◽  
pp. 1225-1233 ◽  
Author(s):  
P B Wedegaertner ◽  
H R Bourne ◽  
M von Zastrow
Keyword(s):  
Plasma Membrane ◽  
G Protein ◽  
Adrenergic Receptor ◽  
Immunofluorescence Microscopy ◽  
Hek293 Cells ◽  
Wild Type ◽  
Gs Alpha ◽  
The Relationship ◽  
Regulated Trafficking ◽  
Receptor Beta

We have examined the subcellular distribution of alpha s, the alpha subunit of the heterotrimeric G protein Gs, by using immunofluorescence microscopy. In transiently transfected HEK293 cells, wild-type alpha s localizes to the plasma membrane. However, a mutationally activated alpha s (alpha sR201C) is diffusely distributed throughout the cytoplasm. Similarly, cholera toxin activation of alpha s causes it to redistribute from the plasma membrane to cytoplasm in stably transfected cells. In HEK293 cells stably transfected with alpha s and the beta 2-adrenergic receptor (beta-AR), stimulation of the beta-AR by the agonist isoproterenol also causes a translocation of alpha s from the plasma membrane to cytoplasm. Replacing the agonist with antagonist allows alpha s to return to the plasma membrane, demonstrating the reversibility of alpha s translocation. Receptor-activated alpha s does not colocalize with internalized beta-AR at endosomes. Incubation of cells in hypertonic sucrose to inhibit clathrin-coated pit-mediated endocytosis of agonist-activated beta-AR failed to block agonist-stimulated redistribution of alpha s. These findings demonstrate that activated alpha s reversibly undergoes a translocation from the plasma membrane to cytoplasm and begin to address the relationship between regulated trafficking of a seven-transmembrane receptor and its cognate G protein.

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