Evidence map›Paper›PMID 20624903›Full record

ArticleThe Journal of cell biology2010

Sar1 assembly regulates membrane constriction and ER export.

Kimberly R Long, Yasunori Yamamoto, Adam L Baker, Simon C Watkins, Carolyn B Coyne, James F Conway, Meir Aridor

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

48 citing papers in PubMed, 88 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. ER exit in physiology and disease.Frontiers in molecular biosciences · 2024
    Review
  9. Article
  10. Article
  11. Article
  12. 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
  13. Article
  14. Article
  15. COPII-mediated trafficking at the ER/ERGIC interface.Traffic (Copenhagen, Denmark) · 2019
    Review
  16. Article
  17. Small GTPases SAR1A and SAR1B regulate the trafficking of the cardiac sodium channel NaBiochimica et biophysica acta. Molecular basis of disease · 2018
    Article
  18. Article
  19. Article
  20. Review
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

7 authors at 1 institution in 1 country.

Kimberly R LongDepartment of Cell Biology and Physiology, School of Medicine, University of Pittsburgh, Pittsburgh, PA 15261, USA.
Yasunori Yamamoto
Adam L Baker
Simon C Watkins
Carolyn B Coyne
James F Conway
Meir Aridor
University of Pittsburgh · US

Funding

Renal and Epithelial Biology Training ProgramT32DK061296 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI KLEYMAN, THOMAS R · 2002 to 2022
$3.1M
The Regulation of COPII Coat Mediated ER ExportR01DK062318 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ARIDOR, MEIR · 2004 to 2008
$1.5M
The Regulation of COPII Coat Mediated ER ExportR56DK062318 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ARIDOR, MEIR · 2009 to 2009
$189k
NIDDK NIH HHS DK062318NIDDK NIH HHS R01 DK062318NIDDK NIH HHS R56 DK062318NIDDK NIH HHS T32 DK061296NIDDK NIH HHS T32-DK061296
6 · The paper itself

Abstract

The guanosine triphosphatase Sar1 controls the assembly and fission of COPII vesicles. Sar1 utilizes an amphipathic N-terminal helix as a wedge that inserts into outer membrane leaflets to induce vesicle neck constriction and control fission. We hypothesize that Sar1 organizes on membranes to control constriction as observed with fission proteins like dynamin. Sar1 activation led to membrane-dependent oligomerization that transformed giant unilamellar vesicles into small vesicles connected through highly constricted necks. In contrast, membrane tension provided through membrane attachment led to organization of Sar1 in ordered scaffolds that formed rigid, uniformly nonconstricted lipid tubules to suggest that Sar1 organization regulates membrane constriction. Sar1 organization required conserved residues located on a unique C-terminal loop. Mutations in this loop did not affect Sar1 activation or COPII recruitment and enhanced membrane constriction, yet inhibited Sar1 organization and procollagen transport from the endoplasmic reticulum (ER). Sar1 activity was directed to liquid-disordered lipid phases. Thus, lipid-directed and tether-assisted Sar1 organization controls membrane constriction to regulate ER export.

Indexed as

AnimalsBiological TransportCaco-2 CellsCell MembraneCOP-Coated VesiclesDogsEndoplasmic ReticulumEnzyme ActivationHumansMonomeric GTP-Binding ProteinsMutationProtein MultimerizationProtein Structure, SecondaryMonomeric GTP-Binding ProteinsSAR1A protein, human

Identifiers

PMID20624903
PMCPMC2911667
OpenAlexW1982390145

What OpenQuestion holds

Textmetadata
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.