A Primer on Vesicle Budding

Springer, Sebastian; Spang, Anne; Schekman, Randy

doi:10.1016/s0092-8674(00)80722-9

Cited by 265 publications

(215 citation statements)

References 18 publications

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“…The cargo molecules are recruited into a newly forming carrier vesicle by cytoplasmic coat molecules (Matsuoka et al, 1998;Bremser et al, 1999). The recruitment of two of the known coats, COPI and COPII, is regulated by small ARF-like GTPases and appears to be a relatively simple process (Lowe and Kreis, 1998;Springer et al, 1999). COPII coat recruitment also is regulated by phosphorylation, since serines of the sec31p component of the COPII coat need to be phosphorylated for full coating activity (Salama et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

The AP-3 Complex Required for Endosomal Synaptic Vesicle Biogenesis is Associated with a Casein Kinase Ια-Like Isoform

Faúndez

Kelly

2000

MBoC

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The formation of small vesicles is mediated by cytoplasmic coats the assembly of which is regulated by the activity of GTPases, kinases, and phosphatases. A heterotetrameric AP-3 adaptor complex has been implicated in the formation of synaptic vesicles from PC12 endosomes . When the small GTPase ARF1 is prevented from hydrolyzing GTP, we can reconstitute AP-3 recruitment to synaptic vesicle membranes in an assembly reaction that requires temperatures above 15°C and the presence of ATP suggesting that an enzymatic step is involved in the coat assembly. We have now found an enzymatic reaction, the phosphorylation of the AP-3 adaptor complex, that is linked with synaptic vesicle coating. Phosphorylation occurs in the ␤3 subunit of the complex by a kinase similar to casein kinase 1␣. The kinase copurifies with neuronal-specific AP-3. In vitro, purified casein kinase I selectively phosphorylates the ␤3A and ␤3B subunit at its hinge domain. Inhibiting the kinase hinders the recruitment of AP-3 to synaptic vesicles. The same inhibitors that prevent coat assembly in vitro also inhibit the formation of synaptic vesicles in PC12 cells. The data suggest, therefore, that the mechanism of AP-3-mediated vesiculation from neuroendocrine endosomes requires the phosphorylation of the adaptor complex at a step during or after AP-3 recruitment to membranes. INTRODUCTIONMembrane proteins are carried from donor membranes to acceptor membranes by two steps, the vesiculation of a carrier vesicle from the donor and the fusion of the carrier vesicle with the acceptor. Vesiculation of the donor membrane can itself be divided into five steps: recognition of cargo proteins; recruitment of coating molecules; the imposition of curvature on the forming vesicle membrane; fission of the carrier vesicle from the donor membrane; and, finally, the loss of the vesicle coat (Springer et al., 1999). To discover the molecular events that take place at each step, several laboratories have reconstituted either the entire process of vesiculation or individual steps in vitro.The first two steps of vesiculation, cargo recognition and coating, can be regulated by phosphorylation. Membrane proteins are recognized as cargo because they contain sorting domains. Adaptors interact with a tyrosine or a dileucine motif (Schmid, 1997;Kirchhausen et al., 1997;Bonifacino and Dell'Angelica, 1999). The recognition of cargo molecules can be regulated by the phosphorylation of sites close to the sorting domains; for example, in the trafficking of furin (Wan et al., 1998;Teuchert et al., 1999;Molloy et al., 1999), CD4 (Pitcher et al., 1999), CTLA-4 (Shiratori et al., 1997), MHC-II-Ii complex (Anderson and Roche, 1998), and pIgAR (Casanova et al., 1990;Okamoto et al., 1994;Luton et al., 1998). The cargo molecules are recruited into a newly forming carrier vesicle by cytoplasmic coat molecules (Matsuoka et al., 1998;Bremser et al., 1999). The recruitment of two of the known coats, COPI and COPII, is regulated by small ARF-like GTPases and appears to be a relatively simple p...

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Section: Introductionmentioning

confidence: 99%

The AP-3 Complex Required for Endosomal Synaptic Vesicle Biogenesis is Associated with a Casein Kinase Ια-Like Isoform

Faúndez

Kelly

2000

MBoC

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“…We have previously demonstrated that the transient interaction Glo3p with the v-SNAREs Sec22p and Bet1p renders the SNAREs more protease resistant (Rein et al, 2002). This conformational change may promote the inclusion of SNAREs into vesicles, and they might even serve as primers for vesicle formation (Springer et al, 1999;Spang, 2002).…”

Section: Discussionmentioning

confidence: 99%

“…Arf1p is activated through interaction with an ARF guanine nucleotide exchange factor (ArfGEF) at the membrane (Donaldson and Jackson, 2000). Subsequently, coatomer is recruited and forms a complex with Arf1p, cargo, or soluble N-ethylmaleimidesensitive factor attachment protein receptor (SNARE) and an ARF-GTPase activating protein (ArfGAP), a so-called primer (Springer et al, 1999;Spang, 2002). This interaction does not require the deactivation of Arf1p by a GAP.…”

Section: Introductionmentioning

confidence: 99%

Interaction of SNAREs with ArfGAPs Precedes Recruitment of Sec18p/NSF

Schindler

Spang

2007

MBoC

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Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins are key components of the fusion machinery in vesicular transport and in homotypic membrane fusion. We previously found that ADP-ribosylation factor GTPase activating proteins (ArfGAPs) promoted a conformational change on SNAREs that allowed recruitment of the small GTPase Arf1p in stoichiometric amounts. Here, we show that the ArfGAP Gcs1p accelerates vesicle (v)-target membrane (t)-SNARE complex formation in vitro, indicating that ArfGAPs may act as folding chaperones. These SNARE complexes were resolved in the presence of ATP by the yeast homologues of ␣-soluble N-ethylmaleimide-sensitive factor attachment protein and N-ethylmaleimide-sensitive factor, Sec17p and Sec18p, respectively. In addition, Sec18p and Sec17p also recognized the "activated" SNAREs even when they were not engaged in v-t-SNARE complexes. Here again, the induction of a conformational change by ArfGAPs was essential. Surprisingly, recruitment of Sec18p to SNAREs did not require Sec17p or ATP hydrolysis. Moreover, Sec18p displaced prebound Arf1p from SNAREs, indicating that Sec18p may have more than one function: first, to ensure that all vesicle coat proteins are removed from the SNAREs before the engagement in a trans-SNARE complex; and second, to resolve cis-SNARE complexes after fusion has occurred.

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“…Tom Yeung, unétudiant du labo, a montré, par le test d'incorporation d'une protéine SNARE, que les membranes isoléesà partir de cellules traitéesà la cycloheximide, par conséquent purgées des protéines nouvellement synthétisées,étaient parfaitement actives pour bourgeonner en vésiculesà COPII (Yeung et al, 1995). Bien que le cargo biosynthétique ne soit pas forcément essentiel au bourgeonnement vésiculaire, nous avons suggéré que les protéines qui cyclent entre le RE et le Golgi pourraient constituer unélément essentiel de la contribution membranaireà la formation d'un bourgeon COPII (Springer et al, 1999).…”

Section: Copii Est Responsable Du Bourgeonnement Vésiculaireà Partir unclassified

Les gènes et les protéines qui contrôlent la voie de sécrétion

Schekman

2015

Biologie Aujourd'hui

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A Primer on Vesicle Budding

Cited by 265 publications

References 18 publications

The AP-3 Complex Required for Endosomal Synaptic Vesicle Biogenesis is Associated with a Casein Kinase Ια-Like Isoform

The AP-3 Complex Required for Endosomal Synaptic Vesicle Biogenesis is Associated with a Casein Kinase Ια-Like Isoform

Interaction of SNAREs with ArfGAPs Precedes Recruitment of Sec18p/NSF

Les gènes et les protéines qui contrôlent la voie de sécrétion

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