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

Reinhard, Constanze; Schweikert, Michael; Wieland, Felix; Nickel, Walter

doi:10.1073/pnas.1432391100

Cited by 75 publications

(75 citation statements)

References 45 publications

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“…While our results contrast with previously reported results 18,28,29,34,35,39,58 in which it was reported that Arf1 and coatomer were sufficient for vesicle formation, they do not necessarily contradict these studies. The population of LUVs generated by the extrusion method, which is a frequently used method that we used in this work, contains many vesicles with diameters between 30 and 150 nm.…”

Section: Discussioncontrasting

confidence: 99%

ArfGAP1 promotes COPI vesicle formation by facilitating coatomer polymerization

et al. 2011

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Section: Discussioncontrasting

confidence: 99%

ArfGAP1 promotes COPI vesicle formation by facilitating coatomer polymerization

et al. 2011

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“…Cryo electron microscopy and tomography of liposomes incubated with Arf wt, GTP and coatomer revealed production of regular free COPI vesicles, as expected from earlier work (Reinhard et al 2003). With the nondimerizing mutant of Arf, however, hardly any free vesicles are formed.…”

Section: Budding and Scissionsupporting

confidence: 83%

COPI Budding within the Golgi Stack

Popoff

Adolf²,

Brügger³

et al. 2011

Cold Spring Harbor Perspectives in Biology

151

169

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The Golgi serves as a hub for intracellular membrane traffic in the eukaryotic cell. Transport within the early secretory pathway, that is within the Golgi and from the Golgi to the endoplasmic reticulum, is mediated by COPI-coated vesicles. The COPI coat shares structural features with the clathrin coat, but differs in the mechanisms of cargo sorting and vesicle formation. The small GTPase Arf1 initiates coating on activation and recruits en bloc the stable heptameric protein complex coatomer that resembles the inner and the outer shells of clathrin-coated vesicles. Different binding sites exist in coatomer for membrane machinery and for the sorting of various classes of cargo proteins. During the budding of a COPI vesicle, lipids are sorted to give a liquid-disordered phase composition. For the release of a COPI-coated vesicle, coatomer and Arf cooperate to mediate membrane separation.

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“…This connection may guarantee incorporation of a v-SNARE into nascent vesicles in order to make them fusion-competent at the appropriate acceptor compartment. The classical view for Arf-GAP function has been that GAP-mediated hydrolysis of GTP on Arf1 leads to vesicle uncoating to allow for subsequent fusion (Tanigawa et al, 1993;Bigay et al, 2003;Reinhard et al, 2003). Yet, other studies support the idea that Arf-GAP activity is required for the packaging of cargo into COPI vesicles (Nickel et al, 1998;Pepperkok et al, 2000;Lanoix et al, 2001;Rein et al, 2002;Lee et al, 2004) and for COPI vesicle biogenesis (Yang et al, 2002;Lee et al, 2004).…”

Section: Gcs1 and Endosome-golgi Recyclingmentioning

confidence: 99%

The Gcs1 Arf-GAP Mediates Snc1,2 v-SNARE Retrieval to the Golgi in Yeast

Robinson

Poon

Schindler

et al. 2006

MBoC

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Gcs1 is an Arf GTPase-activating protein (Arf-GAP) that mediates Golgi-ER and post-Golgi vesicle transport in yeast.Here we show that the Snc1,2 v-SNAREs, which mediate endocytosis and exocytosis, interact physically and genetically with Gcs1. Moreover, Gcs1 and the Snc v-SNAREs colocalize to subcellular structures that correspond to the trans-Golgi and endosomal compartments. Studies performed in vitro demonstrate that the Snc-Gcs1 interaction results in the efficient binding of recombinant Arf1⌬17N-Q71L to the v-SNARE and the recruitment of purified coatomer. In contrast, the presence of Snc had no effect on Gcs1 Arf-GAP activity in vitro, suggesting that v-SNARE binding does not attenuate Arf1 function. Disruption of both the SNC and GCS1 genes results in synthetic lethality, whereas overexpression of either SNC gene inhibits the growth of a distinct subset of COPI mutants. We show that GFP-Snc1 recycling to the trans-Golgi is impaired in gcs1⌬ cells and these COPI mutants. Together, these results suggest that Gcs1 facilitates the incorporation of the Snc v-SNAREs into COPI recycling vesicles and subsequent endosome-Golgi sorting in yeast.

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

Cited by 75 publications

References 45 publications

ArfGAP1 promotes COPI vesicle formation by facilitating coatomer polymerization

ArfGAP1 promotes COPI vesicle formation by facilitating coatomer polymerization

COPI Budding within the Golgi Stack

The Gcs1 Arf-GAP Mediates Snc1,2 v-SNARE Retrieval to the Golgi in Yeast

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