scholarly journals Temporal Ordering in Endocytic Clathrin-Coated Vesicle Formation via AP2 Phosphorylation

2020 ◽  
Vol 52 (5) ◽  
pp. 673
Author(s):  
Antoni G. Wrobel ◽  
Zuzana Kadlecova ◽  
Jan Kamenicky ◽  
Ji-Chun Yang ◽  
Torsten Herrmann ◽  
...  
2019 ◽  
Vol 50 (4) ◽  
pp. 494-508.e11 ◽  
Author(s):  
Antoni G. Wrobel ◽  
Zuzana Kadlecova ◽  
Jan Kamenicky ◽  
Ji-Chun Yang ◽  
Torsten Herrmann ◽  
...  

1994 ◽  
Vol 5 (2) ◽  
pp. 237-252 ◽  
Author(s):  
T C Taylor ◽  
M Kanstein ◽  
P Weidman ◽  
P Melançon

We investigated the role of ADP-ribosylation factors (ARFs) in Golgi function using biochemical and morphological cell-free assays. An ARF-free cytosol produced from soluble Chinese hamster ovary (CHO) extracts supports intra-Golgi transport by a mechanism that is biochemically indistinguishable from control transport reactions: ARF-free transport reactions are NSF-dependent, remain sensitive to the donor Golgi-specific inhibitor ilimaquinone, and exhibit kinetics that are identical to that of control reactions containing ARFs. In contrast, ARF-free cytosol does not support the formation of coated vesicles on Golgi cisternae. However, vesicle formation is reconstituted upon the addition of ARF1. These data suggest that neither soluble ARFs nor coated vesicle formation are essential for transport. We conclude that cell-free intra-Golgi transport proceeds via a coated vesicle-independent mechanism regardless of vesicle formation on Golgi cisternae.


Cell ◽  
1998 ◽  
Vol 93 (2) ◽  
pp. 263-275 ◽  
Author(s):  
Ken Matsuoka ◽  
Lelio Orci ◽  
Mylène Amherdt ◽  
Sebastian Y Bednarek ◽  
Susan Hamamoto ◽  
...  

2021 ◽  
Vol 478 (16) ◽  
pp. 3099-3123
Author(s):  
Katherine M. Wood ◽  
Corinne J. Smith

Clathrin is best known for its contribution to clathrin-mediated endocytosis yet it also participates to a diverse range of cellular functions. Key to this is clathrin's ability to assemble into polyhedral lattices that include curved football or basket shapes, flat lattices or even tubular structures. In this review, we discuss clathrin structure and coated vesicle formation, how clathrin is utilised within different cellular processes including synaptic vesicle recycling, hormone desensitisation, spermiogenesis, cell migration and mitosis, and how clathrin's remarkable ‘shapeshifting’ ability to form diverse lattice structures might contribute to its multiple cellular functions.


2002 ◽  
Vol 361 (3) ◽  
pp. 653-661
Author(s):  
Abdelkarim ABOUSALHAM ◽  
Tom C. HOBMAN ◽  
Jay DEWALD ◽  
Michael GARBUTT ◽  
David N. BRINDLEY

Differential effects of acetyl(C2-) ceramide (N-acetylsphingosine) were studied on coated vesicle formation from Golgi-enriched membranes of Chinese hamster ovary (CHO) and Madin—Darby canine kidney (MDCK) cells. C2-ceramide blocked the translocation of ADP-ribosylation factor-1 (ARF-1) and protein kinase C-α (PKC-α) to the membranes from CHO cells, but not those of MDCK cells. Consequently, C2-ceramide blocked the stimulation of phospholipase D1 (PLD1) by the cytosol and guanosine 5′-[γ-thio]triphosphate (GTP[S]) in membranes from CHO cells. Basal specific activity of PLD1 and the concentration of ARF-1 were 3–4 times higher in Golgi-enriched membranes from MDCK cells compared with CHO cells. Moreover, PLD1 activity in MDCK cells was stimulated less by cytosol and GTP[S]. PLD2 was not detectable in the Golgi-enriched membranes. Incubation of intact CHO cells or their Golgi-enriched membranes with C2-ceramide also inhibited COP1 vesicle formation by membranes from CHO, but not MDCK, cells. Specificity was demonstrated, since dihydro-C2-ceramide had no significant effect on ARF-1 translocation, PLD1 activation or vesicle formation in membranes from both cell types. C2-ceramide also decreased the secretion of virus-like particles to a greater extent in CHO compared with MDCK cells, whereas dihydro-C2-ceramide had no significant effect. The results demonstrate a biological effect of C2-ceramide in CHO cells by decreasing ARF-1 and PKC-α binding to Golgi-enriched membranes, thereby preventing COP1 vesicle formation.


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