Evidence map›Paper›PMID 11553719›Full record

ArticleMolecular biology of the cell2001

Sequential activities of phosphoinositide 3-kinase, PKB/Aakt, and Rab7 during macropinosome formation in Dictyostelium.

A Rupper, K Lee, D Knecht, J Cardelli

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

33 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. The Amoebal Model for Macropinocytosis.Sub-cellular biochemistry · 2022
    Article
  5. Review
  6. Review
  7. Frontiers in cellular and infection microbiology · 2020
    Article
  8. The origins and evolution of macropinocytosis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2019
    Review
  9. Article
  10. GQDs-MSNs nanocomposite nanoparticles for simultaneous intracellular drug delivery and fluorescent imaging.Journal of nanoparticle research : an interdisciplinary forum for nanoscale science and technology · 2018
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review
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 2 institutions in 1 country.

A RupperDepartment of Microbiology and Immunology, Louisiana State University Health Sciences Center, Shreveport, LA 71130, USA.
K Lee
D Knecht
J Cardelli
University of Connecticut · USLouisiana State University Health Sciences Center Shreveport · US

Funding

TARGETING OF LYSOSOMAL ENZYMES IN DICTYOSTELIUMR01DK039232 · NIDDK · LOUISIANA STATE UNIV HSC SHREVEPORT · PI CARDELLI, JAMES · 1992 to 2001
$365k
TARGETING O LYSOSOMAL ENZYMES IN DICTYOSTELIUM DISCOIDEUR29DK039232 · NIDDK · LOUISIANA STATE UNIV HSC SHREVEPORT · PI CARDELLI, JAMES · 1988 to 1990
–
NIDDK NIH HHS DK 39232
6 · The paper itself

Abstract

Macropinocytosis plays an important role in the internalization of antigens by dendritic cells and is the route of entry for many bacterial pathogens; however, little is known about the molecular mechanisms that regulate the formation or maturation of macropinosomes. Like dendritic cells, Dictyostelium amoebae are active in macropinocytosis, and various proteins have been identified that contribute to this process. As described here, microscopic analysis of null mutants have revealed that the class I phosphoinositide 3-kinases, PIK1 and PIK2, and the downstream effector protein kinase B (PKB/Akt) are important in regulating completion of macropinocytosis. Although actin-rich membrane protrusions form in these cell lines, they recede without forming macropinosomes. Imaging of cells expressing green fluorescent protein (GFP) fused to the pleckstrin homology domain (PH) of PKB (GFP-PHPKB) indicates that D3 phosphoinositides are enriched in the forming macropinocytic cup and remain associated with newly formed macropinosomes for <1 minute. A fusion protein, consisting of GFP fused to an F-actin binding domain, overlaps with GFP-PHPKB in the timing of association with forming macropinosomes. Although macropinocytosis is reduced in cells expressing dominant negative Rab7, microscopic imaging studies reveal that GFP-Rab7 associates only with formed macropinosomes at approximately the time that F-actin and D3 phosphoinositide levels decrease. These results support a model in which F-actin modulating proteins and vesicle trafficking proteins coordinately regulate the formation and maturation of macropinosomes.

Indexed as

PinocytosisProtein Serine-Threonine KinasesSaccharomyces cerevisiae Proteins1-Phosphatidylinositol 4-KinaseActinsAnimalsDictyosteliumGreen Fluorescent ProteinsLuminescent ProteinsLysosomesMicroscopy, ConfocalModels, BiologicalPhosphatidylinositol 3-KinasesPhosphatidylinositolsPhosphoinositide-3 Kinase InhibitorsProtein Binding1-Phosphatidylinositol 4-KinaseActinsGreen Fluorescent ProteinsLuminescent ProteinsPhosphatidylinositol 3-KinasesPhosphatidylinositolsPhosphoinositide-3 Kinase InhibitorsPIK1 protein, S cerevisiaeProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktrab7 GTP-Binding Proteinsrab GTP-Binding ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID11553719
PMCPMC59715
OpenAlexW2116082644

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.