scholarly journals Retrograde transport of γ-secretase from endosomes to the trans-Golgi network regulates Aβ42 production

2018 ◽  
Vol 147 (1) ◽  
pp. 110-123 ◽  
Author(s):  
Kunihiko Kanatsu ◽  
Yukiko Hori ◽  
Ihori Ebinuma ◽  
Yung Wen Chiu ◽  
Taisuke Tomita
Keyword(s):  
Retrograde Transport ◽  
Trans Golgi Network ◽  
Golgi Network

GGA proteins regulate retrograde transport of BACE1 from endosomes to the trans-Golgi network

2005 ◽  
Vol 29 (3) ◽  
pp. 453-461 ◽  
Author(s):  
Tina Wahle ◽  
Kai Prager ◽  
Nikolai Raffler ◽  
Christian Haass ◽  
Michael Famulok ◽  
...  
Keyword(s):  
Retrograde Transport ◽  
Trans Golgi Network ◽  
Golgi Network

scholarly journals A new role for RINT-1 in SNARE complex assembly at the trans-Golgi network in coordination with the COG complex

2013 ◽  
Vol 24 (18) ◽  
pp. 2907-2917 ◽  
Author(s):  
Kohei Arasaki ◽  
Daichi Takagi ◽  
Akiko Furuno ◽  
Miwa Sohda ◽  
Yoshio Misumi ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Membrane Trafficking ◽  
Retrograde Transport ◽  
Snare Complex ◽  
Initial Contact ◽  
Complex Assembly ◽  
Trans Golgi Network ◽  
Cog Complex ◽  
Protein Receptor ◽  
Golgi Network

Docking and fusion of transport vesicles/carriers with the target membrane involve a tethering factor–mediated initial contact followed by soluble N-ethylmaleimide–sensitive factor attachment protein receptor (SNARE)–catalyzed membrane fusion. The multisubunit tethering CATCHR family complexes (Dsl1, COG, exocyst, and GARP complexes) share very low sequence homology among subunits despite likely evolving from a common ancestor and participate in fundamentally different membrane trafficking pathways. Yeast Tip20, as a subunit of the Dsl1 complex, has been implicated in retrograde transport from the Golgi apparatus to the endoplasmic reticulum. Our previous study showed that RINT-1, the mammalian counterpart of yeast Tip20, mediates the association of ZW10 (mammalian Dsl1) with endoplasmic reticulum–localized SNARE proteins. In the present study, we show that RINT-1 is also required for endosome-to–trans-Golgi network trafficking. RINT-1 uncomplexed with ZW10 interacts with the COG complex, another member of the CATCHR family complex, and regulates SNARE complex assembly at the trans-Golgi network. This additional role for RINT-1 may in part reflect adaptation to the demand for more diverse transport routes from endosomes to the trans-Golgi network in mammals compared with those in a unicellular organism, yeast. The present findings highlight a new role of RINT-1 in coordination with the COG complex.

scholarly journals Insulin-responsive amino peptidase follows the Glut4 pathway but is dispensable for the formation and translocation of insulin-responsive vesicles

2019 ◽  
Vol 30 (12) ◽  
pp. 1536-1543 ◽  
Author(s):  
Xiang Pan ◽  
Anatoli Meriin ◽  
Guanrong Huang ◽  
Konstantin V. Kandror
Keyword(s):  
Skeletal Muscle ◽  
Glucose Transporter ◽  
Muscle Cells ◽  
Retrograde Transport ◽  
Skeletal Muscle Cells ◽  
Glucose Transporter 4 ◽  
Trans Golgi Network ◽  
Insulin Responsiveness ◽  
Golgi Network ◽  
Component Protein

In fat and skeletal muscle cells, insulin-responsive amino peptidase (IRAP) along with glucose transporter 4 (Glut4) and sortilin, represents a major component protein of the insulin-responsive vesicles (IRVs). Here, we show that IRAP, similar to Glut4 and sortilin, is retrieved from endosomes to the trans-Golgi network by retromer. Unlike Glut4, retrograde transport of IRAP does not require sortilin, as retromer can directly bind to the cytoplasmic tail of IRAP. Ablation of IRAP in 3T3-L1 adipocytes shifts the endosomal pool of Glut4 to more acidic endosomes, but does not affect IRV targeting, stability, and insulin responsiveness of Glut4.

A hypothesis on the traffic of MG160, a medial Golgi sialoglycoprotein, from the trans-Golgi network to the Golgi cisternae

1994 ◽  
Vol 107 (3) ◽  
pp. 529-537 ◽  
Author(s):  
P.A. Johnston ◽  
A. Stieber ◽  
N.K. Gonatas
Keyword(s):  
Sialic Acid ◽  
Golgi Apparatus ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Brefeldin A ◽  
Retrograde Transport ◽  
Transport Pathway ◽  
Trans Golgi Network ◽  
Covalently Linked ◽  
Golgi Network

We have reported that MG160, an intrinsic membrane sialoglycoprotein of the Golgi apparatus (GA), resides in the medial cisternae of the organelle (Gonatas et al. (1989) J. Biol. Chem. 264, 646–653). In order to resolve the question whether MG160 acquires sialic acid residues in the trans cisternae or trans-Golgi network (TGN) prior to its retrograde transport, we have examined the effects of brefeldin A (BFA) on the post-translational processing of MG160, and the distribution of internalized wheat germ agglutinin covalently linked with HRP (WGA-HRP), which labels the TGN (Gonatas et al. (1977) J. Cell Biol. 73, 1–13). In BFA-treated PC12 cells, MG160 acquires resistance to endo H, but fails to be sialylated. This effect occurs in parallel with the redistribution of MG160 into an ER compartment dispersed throughout the cytoplasm including the nuclear envelope, and the collapse of the WGA-HRP-labelled TGN into vesicles and tubules surrounding the centriole. These results suggest that MG160 is not sialylated in BFA-treated cells because it is sequestered from the sialyltransferase enzyme(s), presumably located in the TGN, and provide evidence supporting the hypothesis for a retrograde transport pathway that recycles resident GA proteins, including MG160, between the Golgi cisternae and the TGN. To examine further the above hypothesis we studied cells treated with BFA and then allowed to recover from the effect of the drug for various lengths of time. After 15 minutes of recovery, cisternae of the Golgi apparatus, typically found in the pericentriolar region, are labeled by both MG160 and WGA-HRP.(ABSTRACT TRUNCATED AT 250 WORDS)

Intracellular Trafficking of Factor V Subsequent to Its Endocytosis by Megakaryocytes.

Blood ◽  
2005 ◽  
Vol 106 (11) ◽  
pp. 1031-1031
Author(s):  
Lorna W. Seifert ◽  
Alexa Wahle-Ritchie ◽  
Beth A. Bouchard ◽  
Paula B. Tracy
Keyword(s):  
Intracellular Trafficking ◽  
Retrograde Transport ◽  
Factor V ◽  
Structural Element ◽  
Trans Golgi Network ◽  
Granule Protein ◽  
Fluorescent Markers ◽  
Early Endosomes ◽  
Golgi Network ◽  
Acidic Organelles

Abstract Recent studies by our laboratory have identified physical and functional differences between plasma- and platelet-derived factor V. Additional studies indicate that the platelet-derived molecule originates from megakaryocyte endocytosis of the plasma-derived cofactor via a receptor-mediated, clathrin-dependent mechanism, and is subsequently packaged and stored in platelet α-granules. We hypothesize that plasma-derived factor V is modified intracellularly following its endocytosis by megakarycytes to generate the unique platelet-derived cofactor molecule. Thus, the time-dependent, intracellular trafficking of fluorescently-labeled factor V by the megakaryocyte-like cell line, CMK, was determined by confocal microscopy using various organelle-specific, fluorescent markers. Previously, we had demonstrated that subsequent to its endocytosis factor V partially co-localizes with two other proteins known to be endocytosed by megakaryocytes, fibrinogen, an α -granule protein, and transferrin, an iron transport protein. In the current study, we demonstrated that subsequent to their endocytosis, factor V and transferrin partially co-localized to early endosomes as determined using an antibody directed against Rab5. Complete co-localization of anti-Rab5 with an antibody against early endosomal antigen-1 (EEA-1) confirmed the specificity of the anti-Rab5 antibody for early endosomes. Endocytosed factor V was also shown to partially co-localize with von Willebrand factor, an α -granule protein that is synthesized by megakaryocytes. Its synthesis by megakaryocytes was confirmed by partial co-localization of this antibody with anti-Golgi antibodies against GM130, a structural element of the Golgi apparatus, and p230 trans, a protein involved in vesicular transport from the trans-Golgi network. Factor V also partially co-localized with these Golgi markers, consistent with the hypothesis that factor V is modified intracellularly subsequent to its endocytosis. Co-localization studies were also performed using LysoSensor Blue, which partitions into acidic organelles with a pH ~5.1 exhibiting an increase in fluorescence intensity upon acidification. Neither factor V nor transferrin co-localized with LysoSensor Blue confirming that they are not trafficked to lysosomes subsequent to their endocytosis. In conclusion, these combined observations suggest that subsequent to its endocytosis by megakaryocytes factor V is trafficked through early endosomes and ultimately stored in the α -granule with vWF and fibrinogen. Further, these data suggest that prior to its packaging into α -granules factor V may undergo retrograde transport through and O-linked glycosylation in the trans-Golgi network, which is consistent with our previous observations that purified, platelet-derived factor V contains an N-acetyl glucosamine or galactosamine at Thr402 that is not observed in its plasma counterpart.

scholarly journals Action of Arl1 GTPase and golgin Imh1 in Ypt6-independent retrograde transport from endosomes to the trans-Golgi network

2019 ◽  
Vol 30 (8) ◽  
pp. 1008-1019 ◽  
Author(s):  
Yan-Ting Chen ◽  
I-Hao Wang ◽  
Yi-Hsun Wang ◽  
Wan-Yun Chiu ◽  
Jen-Hao Hu ◽  
...  
Keyword(s):  
Membrane Traffic ◽  
Retrograde Transport ◽  
Vesicle Formation ◽  
Ample Evidence ◽  
Trans Golgi Network ◽  
Growth Defects ◽  
Trafficking Defects ◽  
Golgi Network ◽  
Lipid Flippase ◽  
Garp Complex

The Arf and Rab/Ypt GTPases coordinately regulate membrane traffic and organelle structure by regulating vesicle formation and fusion. Ample evidence has indicated that proteins in these two families may function in parallel or complementarily; however, the manner in which Arf and Rab/Ypt proteins perform interchangeable functions remains unclear. In this study, we report that a Golgi-localized Arf, Arl1, could suppress Ypt6 dysfunction via its effector golgin, Imh1, but not via the lipid flippase Drs2. Ypt6 is critical for the retrograde transport of vesicles from endosomes to the trans-Golgi network (TGN), and its mutation leads to severe protein mislocalization and growth defects. We first overexpress the components of the Arl3-Syt1-Arl1-Imh1 cascade and show that only Arl1 and Imh1 can restore endosome-to-TGN trafficking in ypt6-deleted cells. Interestingly, increased abundance of Arl1 or Imh1 restores localization of the tethering factor Golgi associated retrograde–protein (GARP) complex to the TGN in the absence of Ypt6. We further show that the N-terminal domain of Imh1 is critical for restoring GARP localization and endosome-to-TGN transport in ypt6-deleted cells. Together, our results reveal the mechanism by which Arl1-Imh1 facilitates the recruitment of GARP to the TGN and compensates for the endosome-to-TGN trafficking defects in dysfunctional Ypt6 conditions.

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