scholarly journals Secretory Vesicle Budding from the Trans-Golgi Network Is Mediated by Phosphatidic Acid Levels

1998 ◽  
Vol 273 (29) ◽  
pp. 17995-17998 ◽  
Author(s):  
Anirban Siddhanta ◽  
Dennis Shields
Keyword(s):  
Phosphatidic Acid ◽  
Secretory Vesicle ◽  
Vesicle Budding ◽  
Trans Golgi Network ◽  
Golgi Network

scholarly journals Formation of secretory vesicles in permeabilized cells: a salt extract from yeast membranes promotes budding of nascent secretory vesicles from the trans-Golgi network of endocrine cells

1996 ◽  
Vol 314 (3) ◽  
pp. 723-726 ◽  
Author(s):  
Wai Lam W. LING ◽  
Dennis SHIELDS
Keyword(s):  
Mammalian Cells ◽  
Endocrine Cells ◽  
Secretory Vesicle ◽  
Gh3 Cells ◽  
Vesicle Formation ◽  
Secretory Vesicles ◽  
Vesicle Budding ◽  
Trans Golgi Network ◽  
Golgi Network ◽  
Salt Extract

The mechanism of secretory-vesicle formation from the trans-Golgi network (TGN) of endocrine cells is poorly understood. To identify cytosolic activities that facilitate the formation and fission of nascent secretory vesicles, we treated permeabilized pituitary GH3 cells with high salt to remove endogenous budding factors. Using this cell preparation, secretory-vesicle budding from the TGN required addition of exogenous cytosol and energy. Mammalian cytosols (GH3 cells and bovine brain) promoted post-TGN vesicle formation. Most significantly, a salt extract of membranes from the yeast Saccharomyces cerevisiae, a cell lacking a regulated secretory pathway, stimulated secretory vesicle budding in the absence of mammalian cytosolic factors. These results demonstrate that the factors which promote secretory-vesicle release from the TGN are conserved between yeast and mammalian cells.

scholarly journals Ride the wave: Retrograde trafficking becomes Ca2+ dependent with BAIAP3

2017 ◽  
Vol 216 (7) ◽  
pp. 1887-1889 ◽  
Author(s):  
Jakob B. Sørensen
Keyword(s):  
Angiogenesis Inhibitor ◽  
Secretory Vesicle ◽  
Vesicle Formation ◽  
Retrograde Trafficking ◽  
Trans Golgi Network ◽  
Cell Biol ◽  
Golgi Network

The functions of four of the five proteins in the mammalian uncoordinated-13 (Munc13) family have been identified as priming factors in SNARE-dependent exocytosis. In this issue, Zhang et al. (2017. J. Cell Biol. https://doi.org/10.1083/jcb.201702099) show that the fifth member, BAIAP3 (brain-specific angiogenesis inhibitor I–associated protein 3), acts in retrograde trafficking by returning secretory vesicle material to the trans-Golgi network. In its absence, secretory vesicle formation is impaired, leading to accumulation of immature vesicles, or lysosomal vesicle degradation.

scholarly journals P4-ATPase Requirement for AP-1/Clathrin Function in Protein Transport from the trans-Golgi Network and Early Endosomes

2008 ◽  
Vol 19 (8) ◽  
pp. 3526-3535 ◽  
Author(s):  
Ke Liu ◽  
Kavitha Surendhran ◽  
Steven F. Nothwehr ◽  
Todd R. Graham
Keyword(s):  
Protein Transport ◽  
Early Endosome ◽  
Coated Vesicle ◽  
Transport Pathways ◽  
Vesicle Budding ◽  
Trans Golgi Network ◽  
Conditional Allele ◽  
Early Endosomes ◽  
Clathrin Adaptor ◽  
Golgi Network

Drs2p is a resident type 4 P-type ATPase (P4-ATPase) and potential phospholipid translocase of the trans-Golgi network (TGN) where it has been implicated in clathrin function. However, precise protein transport pathways requiring Drs2p and how it contributes to clathrin-coated vesicle budding remain unclear. Here we show a functional codependence between Drs2p and the AP-1 clathrin adaptor in protein sorting at the TGN and early endosomes of Saccharomyces cerevisiae. Genetic criteria indicate that Drs2p and AP-1 operate in the same pathway and that AP-1 requires Drs2p for function. In addition, we show that loss of AP-1 markedly increases Drs2p trafficking to the plasma membrane, but does not perturb retrieval of Drs2p from the early endosome back to the TGN. Thus AP-1 is required at the TGN to sort Drs2p out of the exocytic pathway, presumably for delivery to the early endosome. Moreover, a conditional allele that inactivates Drs2p phospholipid translocase (flippase) activity disrupts its own transport in this AP-1 pathway. Drs2p physically interacts with AP-1; however, AP-1 and clathrin are both recruited normally to the TGN in drs2Δ cells. These results imply that Drs2p acts independently of coat recruitment to facilitate AP-1/clathrin-coated vesicle budding from the TGN.

scholarly journals The Arf GAP SMAP2 is necessary for organized vesicle budding from the trans-Golgi network and subsequent acrosome formation in spermiogenesis

2013 ◽  
Vol 24 (17) ◽  
pp. 2633-2644 ◽  
Author(s):  
Tomo Funaki ◽  
Shunsuke Kon ◽  
Kenji Tanabe ◽  
Waka Natsume ◽  
Sayaka Sato ◽  
...  
Keyword(s):  
Membrane Vesicles ◽  
Round Spermatid ◽  
Snare Complex ◽  
Coated Vesicle ◽  
Vesicle Budding ◽  
Trans Golgi Network ◽  
Protein Receptor ◽  
Acrosome Formation ◽  
Golgi Network ◽  
Coated Membrane

The trans-Golgi network (TGN) functions as a hub organelle in the exocytosis of clathrin-coated membrane vesicles, and SMAP2 is an Arf GTPase-activating protein that binds to both clathrin and the clathrin assembly protein (CALM). In the present study, SMAP2 is detected on the TGN in the pachytene spermatocyte to the round spermatid stages of spermatogenesis. Gene targeting reveals that SMAP2-deficient male mice are healthy and survive to adulthood but are infertile and exhibit globozoospermia. In SMAP2-deficient spermatids, the diameter of proacrosomal vesicles budding from TGN increases, TGN structures are distorted, acrosome formation is severely impaired, and reorganization of the nucleus does not proceed properly. CALM functions to regulate vesicle sizes, and this study shows that CALM is not recruited to the TGN in the absence of SMAP2. Furthermore, syntaxin2, a component of the soluble N-ethylmaleimide–sensitive factor attachment protein receptor (SNARE) complex, is not properly concentrated at the site of acrosome formation. Thus this study reveals a link between SMAP2 and CALM/syntaxin2 in clathrin-coated vesicle formation from the TGN and subsequent acrosome formation. SMAP2-deficient mice provide a model for globozoospermia in humans.

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