Post-Golgi biosynthetic trafficking

1997 ◽  
Vol 110 (24) ◽  
pp. 3001-3009 ◽  
Author(s):  
P. Keller ◽  
K. Simons
Keyword(s):  
Cell Surface ◽  
Golgi Complex ◽  
Cell Types ◽  
Bulk Flow ◽  
Eukaryotic Cells ◽  
Flow Process ◽  
Trans Golgi Network ◽  
Golgi Network ◽  
Different Cell Types

Eukaryotic cells have developed complex machineries to distribute proteins and lipids from the Golgi complex. Contrary to what has originally been postulated, delivery of proteins to the cell surface is not a simple bulk flow process but involves sorting into distinct pathways from the trans-Golgi network. Here we describe the various routes emerging from the trans-Golgi network in different cell types, and we discuss the mechanisms that mediate sorting into these pathways. While much remains to be learned about these sorting mechanisms, it is apparent that a number of pathways previously believed to be restricted to certain cell types might be used more commonly.

scholarly journals Kinesin-5/Eg5 is important for transport of CARTS from the trans-Golgi network to the cell surface

2013 ◽  
Vol 202 (2) ◽  
pp. 241-250 ◽  
Author(s):  
Yuichi Wakana ◽  
Julien Villeneuve ◽  
Josse van Galen ◽  
David Cruz-Garcia ◽  
Mitsuo Tagaya ◽  
...  
Keyword(s):  
Cell Surface ◽  
Vesicular Stomatitis Virus ◽  
Golgi Complex ◽  
Protein Transport ◽  
S2 Cells ◽  
Trans Golgi Network ◽  
Drosophila S2 Cells ◽  
Vesicular Stomatitis ◽  
Golgi Network

Here we report that the kinesin-5 motor Klp61F, which is known for its role in bipolar spindle formation in mitosis, is required for protein transport from the Golgi complex to the cell surface in Drosophila S2 cells. Disrupting the function of its mammalian orthologue, Eg5, in HeLa cells inhibited secretion of a protein called pancreatic adenocarcinoma up-regulated factor (PAUF) but, surprisingly, not the trafficking of vesicular stomatitis virus G protein (VSV-G) to the cell surface. We have previously reported that PAUF is transported from the trans-Golgi network (TGN) to the cell surface in specific carriers called CARTS that exclude VSV-G. Inhibition of Eg5 function did not affect the biogenesis of CARTS; however, their migration was delayed and they accumulated near the Golgi complex. Altogether, our findings reveal a surprising new role of Eg5 in nonmitotic cells in the facilitation of the transport of specific carriers, CARTS, from the TGN to the cell surface.

scholarly journals The morphology but not the function of endosomes and lysosomes is altered by brefeldin A.

1992 ◽  
Vol 119 (2) ◽  
pp. 273-285 ◽  
Author(s):  
S A Wood ◽  
W J Brown
Keyword(s):  
Brefeldin A ◽  
Cell Types ◽  
Trans Golgi Network ◽  
Testicular Cells ◽  
Early Endosomes ◽  
Golgi Network ◽  
Endocytic Traffic ◽  
Energy Dependent ◽  
Different Cell Types ◽  
Compact Cluster

Brefeldin A (BFA) induces the formation of an extensively fused network of membranes derived from the trans-Golgi network (TGN) and early endosomes (EE). We describe in detail here the unaffected passage of endocytosed material through the fused TGN/EE compartments to lysosomes in BFA-treated cells. We also confirmed that BFA caused the formation of tubular lysosomes, although the kinetics and extent of tubulation varied greatly between different cell types. The BFA-induced tubular lysosomes were often seen to form simple networks. Formation of tubular lysosomes was microtubule-mediated and energy-dependent; interestingly, however, maintenance of the tubulated lysosomes only required microtubules and was insensitive to energy poisons. Upon removal of BFA, the tubular lysosomes rapidly recovered in an energy-dependent process. In most cell types examined, the extensive TGN/EE network is ephemeral, eventually collapsing into a compact cluster of tubulo-vesicular membranes in a process that precedes the formation of tubular lysosomes. However, in primary bovine testicular cells, the BFA-induced TGN/EE network was remarkably stable (for > 12 h). During this time, the TGN/EE network coexisted with tubular lysosomes, however, the two compartments remained completely separate. These results show that BFA has multiple, profound effects on the morphology of various compartments of the endosome-lysosome system. In spite of these changes, endocytic traffic can continue through the altered compartments suggesting that transport occurs through noncoated vesicles or through vesicles that are insensitive to BFA.

scholarly journals Dual pulse-chase microscopy reveals early divergence in the biosynthetic trafficking of the Na,K-ATPase and E-cadherin

2015 ◽  
Vol 26 (24) ◽  
pp. 4401-4411 ◽  
Author(s):  
Glen A. Farr ◽  
Michael Hull ◽  
Emily H. Stoops ◽  
Rosalie Bateson ◽  
Michael J. Caplan
Keyword(s):  
Plasma Membrane ◽  
Epithelial Cells ◽  
Cell Surface ◽  
Golgi Complex ◽  
Plasma Membranes ◽  
Secretory Pathway ◽  
Trans Golgi Network ◽  
Polarized Epithelial Cells ◽  
Golgi Network ◽  
E Cadherin

Recent evidence indicates that newly synthesized membrane proteins that share the same distributions in the plasma membranes of polarized epithelial cells can pursue a variety of distinct trafficking routes as they travel from the Golgi complex to their common destination at the cell surface. In most polarized epithelial cells, both the Na,K-ATPase and E-cadherin are localized to the basolateral domains of the plasma membrane. To examine the itineraries pursued by newly synthesized Na,K-ATPase and E-cadherin in polarized MDCK epithelial cells, we used the SNAP and CLIP labeling systems to fluorescently tag temporally defined cohorts of these proteins and observe their behaviors simultaneously as they traverse the secretory pathway. These experiments reveal that E-cadherin is delivered to the cell surface substantially faster than is the Na,K-ATPase. Furthermore, the surface delivery of newly synthesized E-cadherin to the plasma membrane was not prevented by the 19°C temperature block that inhibits the trafficking of most proteins, including the Na,K-ATPase, out of the trans-Golgi network. Consistent with these distinct behaviors, populations of newly synthesized E-cadherin and Na,K-ATPase become separated from one another within the trans-Golgi network, suggesting that they are sorted into different carrier vesicles that mediate their post-Golgi trafficking.

VAMP4 cycles from the cell surface to the trans-Golgi network via sorting and recycling endosomes

2007 ◽  
Vol 120 (6) ◽  
pp. 1028-1041 ◽  
Author(s):  
T. H. T. Tran ◽  
Q. Zeng ◽  
W. Hong
Keyword(s):  
Cell Surface ◽  
Recycling Endosomes ◽  
Trans Golgi Network ◽  
Golgi Network

scholarly journals GLUT4 Recycles via a trans-Golgi Network (TGN) Subdomain Enriched in Syntaxins 6 and 16 But Not TGN38: Involvement of an Acidic Targeting Motif

2003 ◽  
Vol 14 (3) ◽  
pp. 973-986 ◽  
Author(s):  
Annette M. Shewan ◽  
Ellen M. van Dam ◽  
Sally Martin ◽  
Tang Bor Luen ◽  
Wanjin Hong ◽  
...  
Keyword(s):  
Cell Surface ◽  
Glucose Transporter ◽  
Adipocyte Differentiation ◽  
Attachment Protein ◽  
Trans Golgi Network ◽  
Sensitive Factor ◽  
Protein Receptors ◽  
Glucose Transporter Glut4 ◽  
Golgi Network ◽  
Endosomal System

Insulin stimulates glucose transport in fat and muscle cells by triggering exocytosis of the glucose transporter GLUT4. To define the intracellular trafficking of GLUT4, we have studied the internalization of an epitope-tagged version of GLUT4 from the cell surface. GLUT4 rapidly traversed the endosomal system en route to a perinuclear location. This perinuclear GLUT4 compartment did not colocalize with endosomal markers (endosomal antigen 1 protein, transferrin) or TGN38, but showed significant overlap with the TGN target (t)-solubleN-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) Syntaxins 6 and 16. These results were confirmed by vesicle immunoisolation. Consistent with a role for Syntaxins 6 and 16 in GLUT4 trafficking we found that their expression was up-regulated significantly during adipocyte differentiation and insulin stimulated their movement to the cell surface. GLUT4 trafficking between endosomes and trans-Golgi network was regulated via an acidic targeting motif in the carboxy terminus of GLUT4, because a mutant lacking this motif was retained in endosomes. We conclude that GLUT4 is rapidly transported from the cell surface to a subdomain of thetrans-Golgi network that is enriched in the t-SNAREs Syntaxins 6 and 16 and that an acidic targeting motif in the C-terminal tail of GLUT4 plays an important role in this process.

scholarly journals Oligomerization of atrans-Golgi/trans-Golgi Network Retained Protein Occurs in the Golgi Complex and May Be Part of Its Retention

1995 ◽  
Vol 270 (15) ◽  
pp. 8815-8821 ◽  
Author(s):  
Jacomine Krijnse Locker ◽  
Dirk-Jan E. Opstelten ◽  
Maria Ericsson ◽  
Marian C. Horzinek ◽  
Peter J. M. Rottier
Keyword(s):  
Golgi Complex ◽  
Trans Golgi Network ◽  
Golgi Network

The steady state distribution of humTGN46 is not significantly altered in cells defective in clathrin-mediated endocytosis

1998 ◽  
Vol 111 (23) ◽  
pp. 3451-3458 ◽  
Author(s):  
G. Banting ◽  
R. Maile ◽  
E.P. Roquemore
Keyword(s):  
Steady State ◽  
Cell Surface ◽  
Dominant Negative ◽  
Type I ◽  
Steady State Distribution ◽  
State Distribution ◽  
Trans Golgi Network ◽  
Defective Mutant ◽  
Dynamin I ◽  
Golgi Network

It has been shown previously that whilst the rat type I integral membrane protein TGN38 (ratTGN38) is predominantly localised to the trans-Golgi network this protein does reach the cell surface from where it is internalised and delivered back to the trans-Golgi network. This protein thus provides a suitable tool for the investigation of trafficking pathways between the trans-Golgi network and the cell surface and back again. The human orthologue of ratTGN38, humTGN46, behaves in a similar fashion. These proteins are internalised from the cell surface via clathrin mediated endocytosis, a process which is dependent upon the GTPase activity of dynamin. We thus reasoned that humTGN46 would accumulate at the surface of cells rendered defective in clathrin mediated endocytosis by virtue of the fact that they express a GTPase defective mutant of dynamin I. It did not. In fact, expression of a dominant negative GTPase defective mutant of dynamin I had no detectable effect on the steady state distribution of humTGN46. One explanation for this observation is that humTGN46 does not travel directly to the cell surface from the trans-Golgi network. Further studies on cells expressing the dominant negative GTPase defective mutant of dynamin I indicate that the major recycling pathway for humTGN46 is in fact between the trans-Golgi network and the early endosome.

scholarly journals Polarization of myelinating Schwann cell surface membranes: role of microtubules and the trans-Golgi network

1995 ◽  
Vol 15 (3) ◽  
pp. 1797-1807 ◽  
Author(s):  
BD Trapp ◽  
GJ Kidd ◽  
P Hauer ◽  
E Mulrenin ◽  
CA Haney ◽  
...  
Keyword(s):  
Schwann Cell ◽  
Cell Surface ◽  
Trans Golgi Network ◽  
Myelinating Schwann Cell ◽  
Golgi Network

scholarly journals Listeria monocytogenes Possesses Adhesins for Fibronectin

1999 ◽  
Vol 67 (12) ◽  
pp. 6698-6701 ◽  
Author(s):  
Philippe Gilot ◽  
Paul André ◽  
Jean Content
Keyword(s):  
Extracellular Matrix ◽  
Listeria Monocytogenes ◽  
Cell Surface ◽  
Bacterial Cell ◽  
Cell Types ◽  
Eukaryotic Cell ◽  
Eukaryotic Cells ◽  
Food Borne ◽  
Human Fibronectin ◽  
Fibronectin Binding

ABSTRACT Listeria monocytogenes is a gram-positive, nonsporulating, food-borne pathogen of humans and animals that is able to invade many eukaryotic cells. Several listerial surface components have been reported to interact with eukaryotic cell receptors, but the complete mechanism by which the bacteria interact with all of these cell types remains largely unknown. In this work, we found thatL. monocytogenes binds to human fibronectin, a 450,000-Da dimeric glycoprotein found in body fluids, on the surface of cells and in an insoluble component of the extracellular matrix. The binding of fibronectin to L. monocytogenes was found to be saturable and dependent on proteinaceous receptors. Five fibronectin-binding proteins of 55.3, 48.6, 46.7, 42.4, and 26.8 kDa were identified. The 55.3-kDa protein was proved to be present at the bacterial cell surface. The binding of L. monocytogenes to fibronectin adds to the number of molecules to which the bacterium is able to adhere and emphasizes the complexity of host-pathogen interactions.

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