Evidence map›Paper›PMID 19244343›Full record

ArticleMolecular biology of the cell2009

Syndapin promotes formation of a postsynaptic membrane system in Drosophila.

Vimlesh Kumar, Robert Fricke, Debjani Bhar, Suneel Reddy-Alla, K S Krishnan, Sven Bogdan, Mani Ramaswami

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In one paragraph

Article in Molecular biology of the cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

28 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. PACSIN proteins in vivo: Roles in development and physiology.Acta physiologica (Oxford, England) · 2022
    Review
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  6. RNAi Screen inG3 (Bethesda, Md.) · 2019
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  18. Phosphorylation of syndapin I F-BAR domain at two helix-capping motifs regulates membrane tubulation.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
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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

7 authors at 5 institutions in 4 countries.

Vimlesh KumarSmurfit Institute of Genetics and Trinity College Institute of Neuroscience, University of Dublin Trinity College, Ireland. kumarv@tcd.ie
Robert Fricke
Debjani Bhar
Suneel Reddy-Alla
K S Krishnan
Sven Bogdan
Mani Ramaswami
Tata Institute of Fundamental Research · INUniversity of Münster · DENational Centre for Biological Sciences · INTrinity College Dublin · IEUniversity of Arizona · US

Funding

Wellcome Trust
6 · The paper itself

Abstract

Syndapins belong to the F-BAR domain protein family whose predicted functions in membrane tubulation remain poorly studied in vivo. At Drosophila neuromuscular junctions, syndapin is associated predominantly with a tubulolamellar postsynaptic membrane system known as the subsynaptic reticulum (SSR). We show that syndapin overexpression greatly expands this postsynaptic membrane system. Syndapin can expand the SSR in the absence of dPAK and Dlg, two known regulators of SSR development. Syndapin's N-terminal F-BAR domain, required for membrane tubulation in cultured cells, is required for SSR expansion. Consistent with a model in which syndapin acts directly on postsynaptic membrane, SSR expansion requires conserved residues essential for membrane binding in vitro. However, syndapin's Src homology (SH) 3 domain, which negatively regulates membrane tubulation in cultured cells, is required for synaptic targeting and strong SSR induction. Our observations advance knowledge of syndapin protein function by 1) demonstrating the in vivo relevance of membrane remodeling mechanisms suggested by previous in vitro and structural analyses, 2) showing that SH3 domains are necessary for membrane expansion observed in vivo, and 3) confirming that F-BAR proteins control complex membrane structures.

Indexed as

AnimalsBiomarkersCarrier ProteinsDrosophila melanogasterDrosophila ProteinsEndoplasmic ReticulumIntracellular MembranesLarvaModels, BiologicalMutationNeuromuscular JunctionProtein BindingProtein Structure, TertiaryProtein TransportBiomarkersCarrier ProteinsDrosophila ProteinsSynd protein, Drosophila

Identifiers

PMID19244343
PMCPMC2669032
OpenAlexW2147786443

What OpenQuestion holds

Textmetadata
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.