Evidence map›Paper›PMID 11739406›Full record

ArticleThe Journal of cell biology2001

Crystal structure of Sar1-GDP at 1.7 A resolution and the role of the NH2 terminus in ER export.

M Huang, J T Weissman, S Beraud-Dufour, P Luan, C Wang, W Chen, M Aridor, I A Wilson, W E Balch

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
2.4field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

61 citing papers in PubMed, 158 citations in OpenAlex.

  1. Review
  2. Article
  3. A molten globule ensemble primes Arf1-GDP for the nucleotide switch.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Article
  6. Molecular mechanism of GTP binding- and dimerization-induced enhancement of Sar1-mediated membrane remodeling.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. COPII-mediated trafficking at the ER/ERGIC interface.Traffic (Copenhagen, Denmark) · 2019
    Review
  18. Chloroplast vesicle transport.Photosynthesis research · 2018
    Review
  19. Article
  20. Article

1 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 1 institution in 1 country.

M HuangDepartment of Cell Biology, The Scripps Research Institute, La Jolla, CA 92130, USA.
J T Weissman
S Beraud-Dufour
P Luan
C Wang
W Chen
M Aridor
I A Wilson
W E Balch
Scripps Research Institute · US

Funding

ROLE OF RAB PROTEINS AND CA2+ IN VESICULAR TRANSPORTR01GM042336 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI BALCH, WILLIAM EDWARD · 1990 to 2011
$4.8M
X-RAY STUDIES OF MHR FABS AND IL-2 RECEPTOR COMPLEXESR01GM049497 · NIGMS · SCRIPPS RESEARCH INSTITUTE · PI WILSON, IAN A · 1993 to 2001
$429k
NIGMS NIH HHS GM42336NIGMS NIH HHS GM49497NIGMS NIH HHS R01 GM042336
6 · The paper itself

Abstract

The Sar1 GTPase is an essential component of COPII vesicle coats involved in export of cargo from the ER. We report the 1.7-A structure of Sar1 and find that consistent with the sequence divergence of Sar1 from Arf family GTPases, Sar1 is structurally distinct. In particular, we show that the Sar1 NH2 terminus contains two regions: an NH2-terminal extension containing an evolutionary conserved hydrophobic motif that facilitates membrane recruitment and activation by the mammalian Sec12 guanine nucleotide exchange factor, and an alpha1' amphipathic helix that contributes to interaction with the Sec23/24 complex that is responsible for cargo selection during ER export. We propose that the hydrophobic Sar1 NH2-terminal activation/recruitment motif, in conjunction with the alpha1' helix, mediates the initial steps in COPII coat assembly for export from the ER.

Indexed as

Saccharomyces cerevisiae ProteinsAnimalsCOP-Coated VesiclesCrystallographyDNA-Binding ProteinsEndoplasmic ReticulumGuanine Nucleotide Exchange FactorsGuanosine DiphosphateGuanosine TriphosphateHydrolysisHydrophobic and Hydrophilic InteractionsMammalsMembrane ProteinsMonomeric GTP-Binding ProteinsProteinsProtein Structure, SecondaryDNA-Binding ProteinsGuanine Nucleotide Exchange FactorsGuanosine DiphosphateGuanosine TriphosphateMembrane ProteinsMonomeric GTP-Binding ProteinsPreb protein, mouseProteinsSaccharomyces cerevisiae ProteinsSAR1 protein, S cerevisiaeSEC24 protein, S cerevisiaeTranscription FactorsVesicular Transport Proteins

Identifiers

PMID11739406
PMCPMC2150902
OpenAlexW2137516675

What OpenQuestion holds

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LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.