Evidence map›Paper›PMID 10704453›Full record

ArticleThe Journal of cell biology2000

Syndapin isoforms participate in receptor-mediated endocytosis and actin organization.

B Qualmann, R B Kelly

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 143 papers.

0numbers the graph read from it
0cells of the map it votes in
143citing papers in PubMed
8.6field-weighted citation impact, top 2% 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

143 citing papers in PubMed, 317 citations in OpenAlex.

  1. Article
  2. Review
  3. Roles in physiology and disease of the inositol phosphatase synaptojanin 1.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2026
    Review
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  15. EHBP1 Is Critically Involved in the Dendritic Arbor Formation and Is Coupled to Factors Promoting Actin Filament Formation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    Article
  16. Article
  17. Article
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  19. Article
  20. Article

83 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

2 authors at 1 institution in 1 country.

B QualmannDepartment of Biochemistry and Biophysics and the Hormone Research Institute, University of California, San Francisco, CA 94143-0534, USA.
R B Kelly
University of California, San Francisco · US

Funding

The Presynaptic Vesicle Cycle for the Slow Acting Neurotransmitter SecretionP01DA010154 · NIDA · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI KREITZER, ANATOL, SULZER, DAVID · 1995 to 2016
$14.7M
ANTIBODIES TO SYNAPTIC VESICLESR01NS015927 · NINDS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI KELLY, REGIS B · 1985 to 2005
$1.5M
BIOCHEMISTRY OF SYNAPTIC TRANSMISSIONR01NS009878 · NINDS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI KELLY, REGIS B · 1985 to 2001
$574k
NIDA NIH HHS DA10154NIDA NIH HHS P01 DA010154NINDS NIH HHS NS09878NINDS NIH HHS NS15927NINDS NIH HHS R01 NS015927
6 · The paper itself

Abstract

Syndapin I (SdpI) interacts with proteins involved in endocytosis and actin dynamics and was therefore proposed to be a molecular link between the machineries for synaptic vesicle recycling and cytoskeletal organization. We here report the identification and characterization of SdpII, a ubiquitously expressed isoform of the brain-specific SdpI. Certain splice variants of rat SdpII in other species were named FAP52 and PACSIN 2. SdpII binds dynamin I, synaptojanin, synapsin I, and the neural Wiskott-Aldrich syndrome protein (N-WASP), a stimulator of Arp2/3 induced actin filament nucleation. In neuroendocrine cells, SdpII colocalizes with dynamin, consistent with a role for syndapin in dynamin-mediated endocytic processes. The src homology 3 (SH3) domain of SdpI and -II inhibited receptor-mediated internalization of transferrin, demonstrating syndapin involvement in endocytosis in vivo. Overexpression of full-length syndapins, but not the NH(2)-terminal part or the SH3 domains alone, had a strong effect on cortical actin organization and induced filopodia. This syndapin overexpression phenotype appears to be mediated by the Arp2/3 complex at the cell periphery because it was completely suppressed by coexpression of a cytosolic COOH-terminal fragment of N-WASP. Consistent with a role in actin dynamics, syndapins localized to sites of high actin turnover, such as filopodia tips and lamellipodia. Our results strongly suggest that syndapins link endocytosis and actin dynamics.

Indexed as

PhosphoproteinsActinsAdaptor Proteins, Signal TransducingAlternative SplicingAnimalsCarrier ProteinsCell Adhesion MoleculesCell DifferentiationCytoskeletal ProteinsCytoskeletonDynamin IDynaminsEndocytosisGTP PhosphohydrolasesHeLa CellsHumansActinsAdaptor Proteins, Signal TransducingCarrier ProteinsCell Adhesion MoleculesCytoskeletal ProteinsDynamin IDynaminsfocal adhesion protein, 52-kDaGTP PhosphohydrolasesNerve Growth FactorNerve Tissue ProteinsPACSIN1 protein, humanPacsin1 protein, ratPACSIN2 protein, humanPacsin2 protein, ratPhosphoproteinsProtein IsoformsProteinsWASL protein, humanWasl protein, ratWiskott-Aldrich Syndrome Protein, Neuronal

Identifiers

PMID10704453
PMCPMC2174535
OpenAlexW2053610637

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.