A role for ADP‐ribosylation factor 1, but not COP I, in secretory vesicle biogenesis from the trans‐Golgi network

Barr, Francis A.; Huttner, Wieland B.

doi:10.1016/0014-5793(96)00285-2

Cited by 39 publications

(25 citation statements)

References 39 publications

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“…Alternatively, this peptide may have a nonspecific disruptive effect on Golgi membranes (38). It has also been reported that an amino-terminal mARF1 peptide facilitates AP-1 recruitment onto immature secretory granules in the TGN (35) and stimulates the formation of secretory vesicles (34,36). In these studies high levels of myristoylated peptide were required for optimal activity (100 M) (34,35), raising the possibility that the effect was due to some residual activity in the amino terminus of ARF1.…”

Section: Fig 7 Ap-1 and Coatomer Bindingmentioning

confidence: 80%

Different Domains of Mammalian ADP-ribosylation Factor 1 Mediate Interaction with Selected Target Proteins

Liang¹,

Sung²,

Morris³

et al. 1997

Journal of Biological Chemistry

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Mammalian ADP-ribosylation factor 1 (mARF1) is a small GTP-binding protein that is activated by a Golgi guanine nucleotide exchange factor. Once bound to the Golgi membranes in the GTP form, mARF1 initiates the recruitment of the adaptor protein 1 (AP-1) complex and coatomer (COPI) onto these membranes and activates phospholipase D1 (PLD1). To map the domains of mARF1 that are important for these activities, we constructed chimeras between mARF1 and Saccharomyces cerevisiae ARF2, which functions poorly in all of these processes except COPI recruitment.The carboxyl half of mARF1 (amino acids 95-181) was essential for activation by the Golgi guanine nucleotide exchange factor, whereas a separate domain (residues 35-94) was required to effectively activate PLD1 and to promote efficient AP-1 recruitment. Since residues 35-94 of mARF1 are critical for optimal activity in both PLD1 activation and AP-1 recruitment, we hypothesize that this region of ARF contains residues that interact with effector molecules.

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Section: Fig 7 Ap-1 and Coatomer Bindingmentioning

confidence: 80%

Different Domains of Mammalian ADP-ribosylation Factor 1 Mediate Interaction with Selected Target Proteins

Liang¹,

Sung²,

Morris³

et al. 1997

Journal of Biological Chemistry

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“…Thus, microinjection of anticoatomer antibodies into cells was found to prevent transport of the VSV-G protein from the endoplasmic reticulum to the Golgi, but not to affect its delivery from the TGN to the cell surface (17). Another study found that a cytosol depleted of coatomer fully supported the formation of secretory vesicles from a TGN-containing membrane preparation of PC12 cells (12). Recently, it was also observed that, after purification, post-Golgi vesicles generated in vitro from MDCK Golgi fractions containing the VSV-G protein contained no detectable levels of the COPI polypeptide ␤COP (18).…”

mentioning

confidence: 86%

“…14), and are primarily concentrated at the entry face of the Golgi apparatus, but are also localized in the TGN (15) and on endosomes (16). However, several reports (12,17,18) have concluded that coatomer coats are not involved in the production of TGN-derived exocytic vesicles. Thus, microinjection of anticoatomer antibodies into cells was found to prevent transport of the VSV-G protein from the endoplasmic reticulum to the Golgi, but not to affect its delivery from the TGN to the cell surface (17).…”

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confidence: 99%

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Coatomer, but not P200/myosin II, is required for the in vitro formation of trans-Golgi network-derived vesicles containing the envelope glycoprotein of vesicular stomatitis virus

Simon

Shen

Ivanov

et al. 1998

Proc. Natl. Acad. Sci. U.S.A.

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Using a cytosol and nucleotide dependent assay that we previously developed, we have investigated the requirement for coat proteins in the in vitro production of trans-Golgi network (TGN)-derived vesicles from a MadinDarby canine kidney (MDCK) cell Golgi fraction that contains the 35 S-labeled, terminally glycosylated, envelope glycoprotein of vesicular stomatitis virus (VSV-G) accumulated in the TGN. We found that the TGN-derived vesicles, like those involved in intra-Golgi transport and in retrograde transport to the endoplasmic reticulum, contain a coatomer coat and that coatomer is required for their formation. Thus, after they are produced with GTP␥S, the coated vesicles could be captured on beads containing anticoatomer antibody. Moreover, a cytosolic protein fraction depleted of coatomer could not support vesicle formation but it did so after purified coatomer was added. We also determined that P200͞myosin II does not play an essential role in the in vitro generation of TGN-derived vesicles. Thus, removal of this protein from the cytosol, by differential salt precipitation or binding to phalloidin-induced actin filaments, had no effect on vesicle generation. Nevertheless, immunodepletion of cytosol using the anti-P200͞myosin II AD7 antibody abolished vesicle generation and that antibody was capable of effectively immunocapturing coated vesicles, even when these were generated in the absence of P200͞myosin II. These effects, however, are explained by the unexpected finding that the AD7 antibody interacts with undenatured coatomer.

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“…ARF1 also localizes to the TGN in plants (Robinson et al, 2011) and has been demonstrated to have the capacity to mediate COPI-independent vesicle formation at the TGN in a cell-free system derived from PC12 cells (pheochromocytoma of the rat adrenal medulla) (Barr and Huttner, 1996). Interestingly, inhibiting BIG1-4 function does not affect COPI localization (Richter et al, 2014).…”

Section: Arf1 Gtpases Mediate Ethylene-regulated Hook Development Andmentioning

confidence: 99%

Ethylene Regulates Differential Growth via BIG ARF-GEF-Dependent Post-Golgi Secretory Trafficking in Arabidopsis

et al. 2017

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During early seedling development, the shoot apical meristem is protected from damage as the seedling emerges from soil by the formation of apical hook. Hook formation requires differential growth across the epidermis below the meristem in the hypocotyl. The plant hormones ethylene and auxin play key roles during apical hook development by controlling differential growth. We provide genetic and cell biological evidence for the role of ADP-ribosylation factor 1 (ARF1)-GTPase and its effector ARF-guanine-exchange factors (GEFs) of the Brefeldin A-inhibited GEF (BIG) family and GNOM in ethylene-and auxin-mediated control of hook development. We show that ARF-GEF GNOM acts early, whereas BIG ARF-GEFs act at a later stage of apical hook development. We show that the localization of ARF1 and BIG4 at the trans-Golgi network (TGN) depends on ECHIDNA (ECH), a plant homolog of yeast Triacylglycerol lipase (TLG2/SYP4) interacting protein Tgl2-Vesicle Protein 23 (TVP23). BIGs together with ECH and ARF1 mediate the secretion of AUX1 influx carrier to the plasma membrane from the TGN during hook development and defects in BIG or ARF1 result in insensitivity to ethylene. Thus, our data indicate a division of labor within the ARF-GEF family in mediating differential growth with GNOM acting during the formation phase whereas BIGs act during the hook maintenance phase downstream of plant hormone ethylene.

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A role for ADP‐ribosylation factor 1, but not COP I, in secretory vesicle biogenesis from the trans‐Golgi network

Cited by 39 publications

References 39 publications

Different Domains of Mammalian ADP-ribosylation Factor 1 Mediate Interaction with Selected Target Proteins

Different Domains of Mammalian ADP-ribosylation Factor 1 Mediate Interaction with Selected Target Proteins

Coatomer, but not P200/myosin II, is required for the in vitro formation of trans-Golgi network-derived vesicles containing the envelope glycoprotein of vesicular stomatitis virus

Ethylene Regulates Differential Growth via BIG ARF-GEF-Dependent Post-Golgi Secretory Trafficking in Arabidopsis

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