Stepwise assembly of functionally active transport vesicles

Ostermann, Joachim; Orci, Lelio; Tani, Kazuhide; Amherdt, M; Ravazzola, Mariella; Elazar, Zvulun; Rothman, James E.

doi:10.1016/0092-8674(93)90545-2

Cited by 289 publications

(254 citation statements)

References 63 publications

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“…Moreover, COPI-coated vesicles can be formed from salt-washed Golgi membranes, a treatment that removes ARF-GAP activity. This experimental setup has actually allowed the accumulation of COPI-coated vesicles in the presence of GTP (9,42). Finally, the interpretation of the data from Yang et al (34) regarding the inhibitory effect of GTP␥S on COPI budding is in striking contrast to the original observations by Rothman and coworkers, who first demonstrated that COPI-coated vesicles actually accumulate in the presence of nonhydrolyzable analogues of GTP (12,24).…”

Section: Discussioncontrasting

confidence: 54%

Functional reconstitution of COPI coat assembly and disassembly using chemically defined components

Reinhard

Schweikert

Wieland

et al. 2003

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

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Coat protein I (COPI)-coated transport vesicles mediate protein and lipid transport in the early secretory pathway. The basic machinery required for the formation of these transport intermediates has been elucidated based on the reconstitution of COPI-coated vesicle formation from chemically defined liposomes. In this experimental system, the coat components coatomer and GTP-bound ADPribosylation factor (ARF), as well as p23 as a membrane-bound receptor for COPI coat proteins, were shown to be both necessary and sufficient to promote COPI-coated vesicle formation. coatomer ͉ ADP-ribosylation factor ͉ ARF-GAP ͉ p24 protein family

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Section: Discussioncontrasting

confidence: 54%

Functional reconstitution of COPI coat assembly and disassembly using chemically defined components

Reinhard

Schweikert

Wieland

et al. 2003

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

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“…Perhaps the Nmyristoylated ARF1 peptide was more potent in eliciting a phospholipase D activation relevant to TGN-derived secretory vesicle biogenesis than the N-myristoylated ARF4 peptide [33]. A role of phospholipase D in the biogenesis of TGNderived secretory vesicles would be consistent with the growing evidence implicating lipid modifications in the course of vesicle budding and fission [23,[34][35][36][37].…”

Section: Discussionmentioning

confidence: 61%

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

Barr

Huttner

1996

FEBS Letters

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A synthetic N-myristoylated peptide corresponding to the amino-terminal domain of ADP-ribosylation factor 1 (ARF1) markedly increases, in a cell-free system using post-nuclear supernatant from PC12 cells, the biogenesis of constitutive secretory vesicles and immature secretory granules from the trans-Goigi network (TGN). The related N-myristoylated ARF4 peptide only weakly stimulates, and the non-myristoylated ARF1 and ARF4 peptides inhibit, the biogenesis of these secretory vesicles. In a modified cell-free system using TGN membranes, eoatomer-depleted cytosol supports the biogenesis of TGNderived secretory vesicles to the same extent as control cytosol. These results suggest a role for ARF1, but not the COP I coat, in secretory vesicle biogenesis from the TGN, possibly via the activation of phospholipase D. [10,11], the biogenesis of both CSVs and ISGs, collectively referred to as TGN-derived secretory vesicles, is inhibited by brefeldin A. If one extrapolates from the observations on the formation of cis-Golgi-derived vesicles to the biogenesis of TGN-derived secretory vesicles, the inhibition by brefeldin A would be indicative of an involvement of ARF in the latter process [12]. In the present study, we have examined a possible role of ARF in the biogenesis of TGN-derived secretory vesicles. In addition, we have addressed the related question of whether or not coatomer is required for the biogenesis of these vesicles. Materials and methods

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“…The possibility that the acyl groups of membrane proteins are involved in membrane traffic received strong support from the in vitro studies of Rothman and his colleagues. Both membrane fusion [24] and membrane budding [25] require the addition of fatty acyl CoA. This is interpreted to mean that acylation of one or more membrane proteins is required for the fission and fusion events.…”

Section: -mentioning

confidence: 99%