Evidence map›Paper›PMID 11782545›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2002

Dynamin at actin tails.

Eunkyung Lee, Pietro De Camilli

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 109 papers.

0numbers the graph read from it
0cells of the map it votes in
109citing papers in PubMed
9.8field-weighted citation impact, top 1% 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

109 citing papers in PubMed, 236 citations in OpenAlex.

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  11. PathogenicThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
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  15. Taming the Triskelion: Bacterial Manipulation of Clathrin.Microbiology and molecular biology reviews : MMBR · 2019
    Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

49 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.

Eunkyung LeeDepartment of Cell Biology and Howard Hughes Medical Institute, Yale University School of Medicine, P.O. Box 9812, New Haven, CT 06536-0812, USA.
Pietro De Camilli
Howard Hughes Medical Institute · US

Funding

ROLE OF YPT5 INTERACTING COMPONENTS IN ENDOCYTOSISP01CA046128 · NCI · YALE UNIVERSITY · PI NOVICK, PETER JAY · 1988 to 2007
$9.5M
MOLECULAR MECHANISMS IN SYNAPTIC VESICLE RECYCLINGR01NS036251 · NINDS · YALE UNIVERSITY · PI DE CAMILLI, PIETRO · 1997 to 2021
$4.7M
Molecular Mechanisms in Synaptic Vesicle RecyclingR37NS036251 · NINDS · YALE UNIVERSITY · PI DE CAMILLI, PIETRO · 2010 to 2016
$2.7M
NCI NIH HHS CA46128NCI NIH HHS P01 CA046128NINDS NIH HHS NS36251NINDS NIH HHS R01 NS036251NINDS NIH HHS R37 NS036251
6 · The paper itself

Abstract

Dynamin, the product of the shibire gene of Drosophila, is a GTPase critically required for endocytosis. Some studies have suggested a functional link between dynamin and the actin cytoskeleton. This link is of special interest, because there is evidence implicating actin dynamics in endocytosis. Here we show that endogenous dynamin 2, as well as green fluorescence protein fusion proteins of both dynamin 1 and 2, is present in actin comets generated by Listeria or by type I PIP kinase (PIPK) overexpression. In PIPK-induced tails, dynamin is further enriched at the interface between the tails and the moving organelles. Dynamin mutants harboring mutations in the GTPase domain inhibited nucleation of actin tails induced by PIPK and moderately reduced their speed. Although dynamin localization to the tails required its proline-rich domain, expression of a dynamin mutant lacking this domain also diminished tail formation. In addition, this mutant disrupted a membrane-associated actin scaffold (podosome rosette) previously shown to include dynamin. These findings suggest that dynamin is part of a protein network that controls nucleation of actin from membranes. At endocytic sites, dynamin may couple the fission reaction to the polymerization of an actin pool that functions in the separation of the endocytic vesicles from the plasma membrane.

Indexed as

Drosophila ProteinsActinsAnimalsCell LineCell MembraneCell MovementCricetinaeCytoskeletonDynamin IDynaminsEndocytosisGreen Fluorescent ProteinsGTP PhosphohydrolasesHeLa CellsHumansListeria monocytogenes1-phosphatidylinositol-4-phosphate 5-kinaseActinsDrosophila ProteinsDynamin IDynaminsGreen Fluorescent ProteinsGTP PhosphohydrolasesLuminescent ProteinsPhosphotransferases (Alcohol Group Acceptor)ProlineRecombinant Fusion Proteinsshi protein, Drosophila

Identifiers

PMID11782545
PMCPMC117532
OpenAlexW2075457034

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.