Evidence map›Paper›PMID 10662777›Full record

ArticleThe Journal of cell biology2000

Actin-dependent propulsion of endosomes and lysosomes by recruitment of N-WASP.

J Taunton, B A Rowning, M L Coughlin, M Wu, R T Moon, T J Mitchison, C A Larabell

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 178 papers.

0numbers the graph read from it
0cells of the map it votes in
178citing papers in PubMed
15.3field-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

178 citing papers in PubMed, 451 citations in OpenAlex.

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  20. WNK1 controls endosomal trafficking through TRIM27-dependent regulation of actin assembly.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article

118 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

7 authors at 4 institutions in 1 country.

J TauntonDepartment of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA. jack_taunton@hms.harvard.edu
B A Rowning
M L Coughlin
M Wu
R T Moon
T J Mitchison
C A Larabell
Harvard University · USLawrence Berkeley National Laboratory · USHoward Hughes Medical Institute · USUniversity of California, Berkeley · US

Funding

STRUCTURE/FUNCTION OF ACTIN DEPOLYMERIZING FACTORR01GM035126 · NIGMS · COLORADO STATE UNIVERSITY-FORT COLLINS · PI BAMBURG, JAMES R · 1985 to 2003
$1.1M
NIGMS NIH HHS GM35126NIGMS NIH HHS R01 GM035126
6 · The paper itself

Abstract

We examined the spatial and temporal control of actin assembly in living Xenopus eggs. Within minutes of egg activation, dynamic actin-rich comet tails appeared on a subset of cytoplasmic vesicles that were enriched in protein kinase C (PKC), causing the vesicles to move through the cytoplasm. Actin comet tail formation in vivo was stimulated by the PKC activator phorbol myristate acetate (PMA), and this process could be reconstituted in a cell-free system. We used this system to define the characteristics that distinguish vesicles associated with actin comet tails from other vesicles in the extract. We found that the protein, N-WASP, was recruited to the surface of every vesicle associated with an actin comet tail, suggesting that vesicle movement results from actin assembly nucleated by the Arp2/3 complex, the immediate downstream target of N-WASP. The motile vesicles accumulated the dye acridine orange, a marker for endosomes and lysosomes. Furthermore, vesicles associated with actin comet tails had the morphological features of multivesicular endosomes as revealed by electron microscopy. Endosomes and lysosomes from mammalian cells preferentially nucleated actin assembly and moved in the Xenopus egg extract system. These results define endosomes and lysosomes as recruitment sites for the actin nucleation machinery and demonstrate that actin assembly contributes to organelle movement. Conversely, by nucleating actin assembly, intracellular membranes may contribute to the dynamic organization of the actin cytoskeleton.

Indexed as

ActinsAnimalsCell-Free SystemEndosomesFemaleHeLa CellsHumansIntracellular MembranesIsoenzymesLysosomesMaleNerve Tissue ProteinsOvumProtein Kinase CProtein Kinase C-alphaRecombinant Fusion ProteinsActinsIsoenzymesNerve Tissue ProteinsPRKCA protein, humanProtein Kinase CProtein Kinase C-alphaRecombinant Fusion ProteinsTetradecanoylphorbol AcetateWASL protein, humanWiskott-Aldrich Syndrome Protein, Neuronal

Identifiers

PMID10662777
PMCPMC2174808
OpenAlexW2099573412

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.