scholarly journals Comparative Activity of ADP-ribosylation Factor Family Members in the Early Steps of Coated Vesicle Formation on Rat Liver Golgi Membranes

1997 ◽  
Vol 272 (7) ◽  
pp. 4141-4148 ◽  
Author(s):  
Jennifer Ostrom Liang ◽  
Stuart Kornfeld
Keyword(s):  
Rat Liver ◽  
Family Members ◽  
Coated Vesicle ◽  
Vesicle Formation ◽  
Adp Ribosylation ◽  
Golgi Membranes ◽  
Adp Ribosylation Factor ◽  
Comparative Activity

scholarly journals Several ADP-ribosylation Factor (Arf) Isoforms Support COPI Vesicle Formation

2011 ◽  
Vol 286 (41) ◽  
pp. 35634-35642 ◽  
Author(s):  
Vincent Popoff ◽  
Julian D. Langer ◽  
Ingeborg Reckmann ◽  
Andrea Hellwig ◽  
Richard A. Kahn ◽  
...  
Keyword(s):  
Secretory Pathway ◽  
Initial Step ◽  
Coated Vesicle ◽  
Vesicle Formation ◽  
Adp Ribosylation ◽  
Golgi Membranes ◽  
Vesicular Carriers ◽  
Vesicle Biogenesis ◽  
Copi Vesicle

Newly synthesized proteins and lipids are transported in vesicular carriers along the secretory pathway. Arfs (ADP-ribosylation factors), a family of highly conserved GTPases within the Ras superfamily, control recruitment of molecular coats to membranes, the initial step of coated vesicle biogenesis. Arf1 and coatomer constitute the minimal cytosolic machinery leading to COPI vesicle formation from Golgi membranes. Although some functional redundancies have been suggested, other Arf isoforms have been poorly analyzed in this context. In this study, we found that Arf1, Arf4, and Arf5, but not Arf3 and Arf6, associate with COPI vesicles generated in vitro from Golgi membranes and purified cytosol. Using recombinant myristoylated proteins, we show that Arf1, Arf4, and Arf5 each support COPI vesicle formation individually. Unexpectedly, we found that Arf3 could also mediate vesicle biogenesis. However, Arf3 was excluded from the vesicle fraction in the presence of the other isoforms, highlighting a functional competition between the different Arf members.

scholarly journals Effect of Protein Kinase A Activity on the Association of ADP-ribosylation Factor 1 to Golgi Membranes

2000 ◽  
Vol 275 (25) ◽  
pp. 19050-19059 ◽  
Author(s):  
Maria Esther Martı́n ◽  
Josefina Hidalgo ◽  
Jose Luis Rosa ◽  
Pascal Crottet ◽  
Angel Velasco
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Adp Ribosylation ◽  
Golgi Membranes ◽  
Adp Ribosylation Factor ◽  
Kinase A

Cell-permeable ceramides preferentially inhibit coated vesicle formation and exocytosis in Chinese hamster ovary compared with Madin–Darby canine kidney cells by preventing the membrane association of ADP-ribosylation factor

2002 ◽  
Vol 361 (3) ◽  
pp. 653-661
Author(s):  
Abdelkarim ABOUSALHAM ◽  
Tom C. HOBMAN ◽  
Jay DEWALD ◽  
Michael GARBUTT ◽  
David N. BRINDLEY
Keyword(s):  
Chinese Hamster Ovary ◽  
Cho Cells ◽  
Mdck Cells ◽  
Chinese Hamster ◽  
Coated Vesicle ◽  
Vesicle Formation ◽  
Madin Darby Canine Kidney ◽  
Adp Ribosylation Factor ◽  
Darby Canine Kidney ◽  
Canine Kidney

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.

scholarly journals Nuclear ADP-ribosylation Factor (ARF)- and Oleate-dependent Phospholipase D (PLD) in Rat Liver Cells

1997 ◽  
Vol 272 (8) ◽  
pp. 5208-5213 ◽  
Author(s):  
Yoshiko Banno ◽  
Keiko Tamiya-Koizumi ◽  
Hideko Oshima ◽  
Akemi Morikawa ◽  
Shonen Yoshida ◽  
...  
Keyword(s):  
Rat Liver ◽  
Phospholipase D ◽  
Liver Cells ◽  
Adp Ribosylation ◽  
Rat Liver Cells ◽  
Adp Ribosylation Factor

scholarly journals A role for ADP ribosylation factor in the control of cargo uptake during COPI-coated vesicle biogenesis

FEBS Letters ◽  
1999 ◽  
Vol 462 (3) ◽  
pp. 267-272 ◽  
Author(s):  
Jörg Malsam ◽  
Daniel Gommel ◽  
Felix T. Wieland ◽  
Walter Nickel
Keyword(s):  
Coated Vesicle ◽  
Adp Ribosylation ◽  
Vesicle Biogenesis ◽  
Adp Ribosylation Factor
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