Evidence map›Paper›PMID 19690049›Full record

ArticleJournal of cell science2009

Sequential signaling in plasma-membrane domains during macropinosome formation in macrophages.

Sei Yoshida, Adam D Hoppe, Nobukazu Araki, Joel A Swanson

Abstract read
In one paragraph

Article in Journal of cell science, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.

0numbers the graph read from it
0cells of the map it votes in
98citing 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

98 citing papers in PubMed, 173 citations in OpenAlex.

  1. Article
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  7. RNA activation ofMolecular therapy. Nucleic acids · 2025
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  13. Destruction of the brush border byFrontiers in microbiology · 2024
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  19. Review
  20. Review

38 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

4 authors at 3 institutions in 2 countries.

Sei YoshidaDepartment of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, MI 48109, USA.
Adam D Hoppe
Nobukazu Araki
Joel A Swanson
University of Michigan–Ann Arbor · USKagawa University · JPSouth Dakota State University · US

Funding

Cellular Biotechnology Training Program (CBTP) - Years 31-35T32GM145304 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Guizhi Zhu · 2022 to 2026
$2.6M
MANIPULATION OF PHAGOCYTOSIS IN MACROPHAGESR01AI035950 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SWANSON, JOEL A · 1994 to 2008
$2.2M
Coordination of signaling during phagocytosisR01AI064668 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SWANSON, JOEL A · 2005 to 2010
$1.6M
Mechanisms and regulation of macropinosome closureR21AI079414 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SWANSON, JOEL A · 2009 to 2010
$411k
MANIPULATION OF PHAGOCYTOSIS IN MACROPHAGESR21AI035950 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SWANSON, JOEL A · 1999 to 1999
–
NIAID NIH HHS AI35950NIAID NIH HHS AI64668NIAID NIH HHS R01 AI035950NIAID NIH HHS R01 AI064668NIAID NIH HHS R21 AI079414NIGMS NIH HHS T32 GM145304
6 · The paper itself

Abstract

Macropinosomes are large endocytic vesicles that form in ruffling regions of plasma membrane. To analyze signal organization relative to ruffle closure into circular ruffles and cup closure into macropinosomes, this study used quantitative microscopy to measure 3' phosphoinositides and small-GTPase activities in a representative subset of forming macropinosomes. Macropinocytosis was stimulated by the addition of macrophage colony-stimulating factor (M-CSF) to macrophages expressing fluorescent reporter proteins. Ratiometric and fluorescence resonance energy transfer (FRET) microscopy determined that Rac1 activity and phosphatidylinositol (3,4,5)-trisphosphate [PtdIns(3,4,5)P(3)] levels increased transiently, peaking 26-30 seconds after ruffle closure. Three-dimensional reconstruction of cells labeled with the fluorescent dye FM4-64 showed that PtdIns(3,4,5)P(3) was restricted to open, circular cups in the plasma membrane. Quantitative fluorescence microscopic methods determined the timing of cup closure, which followed 40-100 seconds after Rac1 and PtdIns(3,4,5)P(3) deactivation and coincided with accumulation of phosphatidylinositol 3-phosphate and Rab5a. Thus, ruffle closure creates a circular domain of plasma membrane that localizes the activation and deactivation of Rac1 and phosphoinositide 3-kinase (PI3K), followed by recruitment of Rab5a and the contractile activities of cup closure.

Indexed as

PinocytosisSignal TransductionAnimalscdc42 GTP-Binding ProteinCell MembraneFemaleMacrophagesMiceMice, Inbred C57BLModels, BiologicalPhosphatidylinositol 3-KinasesPhosphatidylinositol Phosphatesrab5 GTP-Binding Proteinsrac GTP-Binding ProteinsTime Factorscdc42 GTP-Binding Proteinphosphatidylinositol 3,4,5-triphosphatePhosphatidylinositol 3-KinasesPhosphatidylinositol Phosphatesrab5 GTP-Binding Proteinsrac GTP-Binding Proteins

Identifiers

PMID19690049
PMCPMC2736863
OpenAlexW2123778917

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.