(Q27934415)

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Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle

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1 December 2016

Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle (English)

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1 December 2016

Arf family GTPase SAR1 YPL218W

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stated in

GOA release 2020-03-11

author

Randy Schekman

series ordinal

6

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author name string

Marcus C S Lee

series ordinal

1

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Lelio Orci

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2

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Susan Hamamoto

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3

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Eugene Futai

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4

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Mariella Ravazzola

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5

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language of work or name

English

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publication date

26 August 2005

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1 December 2016

122

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page(s)

605-17

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issue

4

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cites work

Sec24p and Iss1p function interchangeably in transport vesicle formation from the endoplasmic reticulum in Saccharomyces cerevisiae

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Bi-directional protein transport between the ER and Golgi

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SNARE selectivity of the COPII coat

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Generation of high curvature membranes mediated by direct endophilin bilayer interactions

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N-terminal hydrophobic residues of the G-protein ADP-ribosylation factor-1 insert into membrane phospholipids upon GDP to GTP exchange

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Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles

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Activation of phospholipase D by the small GTPase Sar1p is required to support COPII assembly and ER export

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Biological membranes as bilayer couples. A molecular mechanism of drug-erythrocyte interactions

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The use of liposomes to study COPII- and COPI-coated vesicle formation and membrane protein sorting

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Cargo selection by the COPII budding machinery during export from the ER

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COPII-cargo interactions direct protein sorting into ER-derived transport vesicles

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Dynamics of the COPII coat with GTP and stable analogues

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COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes

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COP and clathrin-coated vesicle budding: different pathways, common approaches

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GTP/GDP exchange by Sec12p enables COPII vesicle bud formation on synthetic liposomes

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Cargo selection into COPII vesicles is driven by the Sec24p subunit

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The organization of endoplasmic reticulum export complexes

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Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae

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Crystal structure of Sar1-GDP at 1.7 Å resolution and the role of the NH 2 terminus in ER export

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Structure of the Sec23p/24p and Sec13p/31p complexes of COPII

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Evolutionary biology. Pelvic problems for mammals.

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COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum

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ER-to-Golgi transport visualized in living cells

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Adaptors for clathrin coats: structure and function.

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BAR domains as sensors of membrane curvature: the amphiphysin BAR structure

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Protein-Lipid Interplay in Fusion and Fission of Biological Membranes

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Visualization of a Ran-GTP gradient in interphase and mitotic Xenopus egg extracts

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Two-dimensional crystallization of histidine-tagged, HIV-1 reverse transcriptase promoted by a novel nickel-chelating lipid

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Requirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum

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Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat

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Mechanisms of membrane deformation

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Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis

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Vesicle budding from endoplasmic reticulum

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Structural Basis for Activation of ARF GTPase

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The Sar1 GTPase coordinates biosynthetic cargo selection with endoplasmic reticulum export site assembly

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Surface structure of the COPII-coated vesicle

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12 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.CELL.2005.07.025

(Q27934415)

Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle

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