Evidence map›Paper›PMID 25945738›Full record

ArticleNature2015

Coordinated regulation of bidirectional COPI transport at the Golgi by CDC42.

Seung-Yeol Park, Jia-Shu Yang, Angela B Schmider, Roy J Soberman, Victor W Hsu

Open access · greenAbstract read
In one paragraph

Article in Nature, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
5.5field-weighted citation impact, top 4% 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

58 citing papers in PubMed, 82 citations in OpenAlex.

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  8. Studying the Role of Lipid Geometry in COPI Vesicle Formation.Methods in molecular biology (Clifton, N.J.) · 2023
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Seung-Yeol Park1] Division of Rheumatology, Immunology and Allergy, Brigham and Women's Hospital, Boston, Massachusetts 02115, USA [2] Department of Medicine, Harvard Medical School, Boston, Massachusetts 02115, USA.
Jia-Shu Yang1] Division of Rheumatology, Immunology and Allergy, Brigham and Women's Hospital, Boston, Massachusetts 02115, USA [2] Department of Medicine, Harvard Medical School, Boston, Massachusetts 02115, USA.
Angela B Schmider1] Department of Medicine, Harvard Medical School, Boston, Massachusetts 02115, USA [2] Nephrology Division and Department of Medicine, Massachusetts General Hospital, Charlestown, Massachusetts 02129, USA.
Roy J Soberman1] Department of Medicine, Harvard Medical School, Boston, Massachusetts 02115, USA [2] Nephrology Division and Department of Medicine, Massachusetts General Hospital, Charlestown, Massachusetts 02129, USA [3] Molecular Imaging Core, Massachusetts General Hospital, Charlestown, Massachusetts 02129, USA.
Victor W Hsu1] Division of Rheumatology, Immunology and Allergy, Brigham and Women's Hospital, Boston, Massachusetts 02115, USA [2] Department of Medicine, Harvard Medical School, Boston, Massachusetts 02115, USA.
Harvard University · USBrigham and Women's Hospital · US

Funding

COPI TransportR01GM058615 · NIGMS · BRIGHAM AND WOMEN'S HOSPITAL · PI HSU, VICTOR W · 2001 to 2015
$5.7M
Ly6 family members in neutrophil biologyR01AR065538 · NIAMS · BRIGHAM AND WOMEN'S HOSPITAL · PI NIGROVIC, PETER A · 2014 to 2024
$4.0M
Leukotrienes and Lung InflammationR01AI068871 · NIAID · MASSACHUSETTS GENERAL HOSPITAL · PI SOBERMAN, ROY · 2007 to 2011
$2.5M
The Macromolecular Organization of Leukotriene Synthesis and Renal InflammationK01DK089145 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI SCHMIDER, ANGELA BAIR · 2011 to 2015
$798k
A System for FLIM MicroscopyS10RR027931 · NCRR · MASSACHUSETTS GENERAL HOSPITAL · PI SOBERMAN, ROY · 2010 to 2010
$321k
NCRR NIH HHS 1S10RR027931-01NIAID NIH HHS R01 AI068871NIAID NIH HHS R01AI068871NIAMS NIH HHS R01 AR065538NIAMS NIH HHS R01AR065538NIDDK NIH HHS K01 DK089145NIDDK NIH HHS K01DK089145NIGMS NIH HHS R01 GM058615NIGMS NIH HHS R01GM058615
6 · The paper itself

Abstract

The Golgi complex has a central role in the intracellular sorting of secretory proteins. Anterograde transport through the Golgi has been explained by the movement of Golgi cisternae, known as cisternal maturation. Because this explanation is now appreciated to be incomplete, interest has developed in understanding tubules that connect the Golgi cisternae. Here we show that the coat protein I (COPI) complex sorts anterograde cargoes into these tubules in human cells. Moreover, the small GTPase CDC42 regulates bidirectional Golgi transport by targeting the dual functions of COPI in cargo sorting and carrier formation. CDC42 also directly imparts membrane curvature to promote COPI tubule formation. Our findings further reveal that COPI tubular transport complements cisternal maturation in explaining how anterograde Golgi transport is achieved, and that bidirectional COPI transport is modulated by environmental cues through CDC42.

Indexed as

cdc42 GTP-Binding ProteinCell MembraneCoatomer ProteinCoat Protein Complex IGolgi ApparatusHeLa CellsHumansMembrane GlycoproteinsProtein TransportReceptors, LDLViral Envelope Proteinscdc42 GTP-Binding ProteinCoatomer ProteinCoat Protein Complex IG protein, vesicular stomatitis virusMembrane GlycoproteinsReceptors, LDLViral Envelope Proteins

Identifiers

PMID25945738
PMCPMC4449304
OpenAlexW1603763773

What OpenQuestion holds

Textmetadata
LicenceTDM
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.