Evidence map›Paper›PMID 19997509›Full record

ArticlePloS one2009

Structural requirements for PACSIN/Syndapin operation during zebrafish embryonic notochord development.

Melissa A Edeling, Subramaniam Sanker, Takaki Shima, P K Umasankar, Stefan Höning, Hye Y Kim, Lance A Davidson, Simon C Watkins, Michael Tsang, David J Owen and 1 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed, 43 citations in OpenAlex.

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  5. PACSIN proteins in vivo: Roles in development and physiology.Acta physiologica (Oxford, England) · 2022
    Review
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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

11 authors at 3 institutions in 3 countries.

Melissa A EdelingCambridge Institute for Medical Research, University of Cambridge, Cambridge, United Kingdom.
Subramaniam Sanker
Takaki Shima
P K Umasankar
Stefan Höning
Hye Y Kim
Lance A Davidson
Simon C Watkins
Michael Tsang
David J Owen
Linton M Traub
University of Pittsburgh · USUniversity of Cambridge · GBUniversity of Cologne · DE

Funding

Single Nephron and MetabolomicsP30DK079307 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI KLEYMAN, THOMAS R · 2008 to 2022
$13.4M
The Biomechanics of morphogenesis in the frogR01HD044750 · NICHD · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI DAVIDSON, LANCE A. · 2005 to 2020
$3.8M
CLATHRIN COATED VESICLES AND LYSOSOME FUNCTIONR01DK053249 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI TRAUB, LINTON M. · 1998 to 2011
$3.0M
Delineating the Role of FGF Signaling and Vertebrate Heart DevelopmentR01HL088016 · NHLBI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI TSANG, MICHAEL WAIKOK · 2008 to 2012
$2.1M
NHLBI NIH HHS R01 HL088016NICHD NIH HHS R01 HD044750NIDDK NIH HHS P30 DK079307NIDDK NIH HHS P30 DK79307NIDDK NIH HHS R01 DK053249NIDDK NIH HHS R01 DK53249Wellcome Trust
6 · The paper itself

Abstract

PACSIN/Syndapin proteins are membrane-active scaffolds that participate in endocytosis. The structure of the Drosophila Syndapin N-terminal EFC domain reveals a crescent shaped antiparallel dimer with a high affinity for phosphoinositides and a unique membrane-inserting prong upon the concave surface. Combined structural, biochemical and reverse genetic approaches in zebrafish define an important role for Syndapin orthologue, Pacsin3, in the early formation of the notochord during embryonic development. In pacsin3-morphant embryos, midline convergence of notochord precursors is defective as axial mesodermal cells fail to polarize, migrate and differentiate properly. The pacsin3 morphant phenotype of a stunted body axis and contorted trunk is rescued by ectopic expression of Drosophila Syndapin, and depends critically on both the prong that protrudes from the surface of the bowed Syndapin EFC domain and the ability of the antiparallel dimer to bind tightly to phosphoinositides. Our data confirm linkage between directional migration, endocytosis and cell specification during embryonic morphogenesis and highlight a key role for Pacsin3 in this coupling in the notochord.

Indexed as

Embryonic DevelopmentAmino Acid SequenceAnimalsCarrier ProteinsCell MovementEmbryo, NonmammalianHeLa CellsHumansLiposomesMolecular Sequence DataNotochordOligonucleotides, AntisensePhenotypeProtein BindingProtein Structure, TertiaryStructure-Activity RelationshipCarrier ProteinsLiposomesOligonucleotides, Antisensepacsin3 protein, zebrafishZebrafish Proteins

Identifiers

PMID19997509
PMCPMC2780292
OpenAlexW2118920769

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LicenceCC BY
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.