Evidence map›Paper›PMID 22072788›Full record

ArticleMolecular biology of the cell2012

Recruitment of OCRL and Inpp5B to phagosomes by Rab5 and APPL1 depletes phosphoinositides and attenuates Akt signaling.

Michal Bohdanowicz, Daniel M Balkin, Pietro De Camilli, Sergio Grinstein

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

78 citing papers in PubMed, 153 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Rab21 recruits EEA1 and competes with Rab5 for Rabex-5 activation.Frontiers in cell and developmental biology · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. p97/VCP Promotes the Recycling of Endocytic Cargo.Molecular biology of the cell · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. Poly(ADP-ribose) Polymerase 1 Mediates Rab5 Inactivation after DNA Damage.International journal of molecular sciences · 2022
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

18 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 2 institutions in 2 countries.

Michal BohdanowiczDivision of Cell Biology, Hospital for Sick Children, Toronto, ON, Canada.
Daniel M Balkin
Pietro De Camilli
Sergio Grinstein
Hospital for Sick Children · CAHoward Hughes Medical Institute · US

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007205 · NIGMS · YALE UNIVERSITY · PI KAZMIERCZAK, BARBARA I · 1985 to 2019
$42.9M
OCRL and the pathogenesis of Lowe Syndrome and Dent DiseaseR01DK082700 · NIDDK · YALE UNIVERSITY · PI DE CAMILLI, PIETRO · 2009 to 2016
$2.4M
CIHR MOP7075NIDDK NIH HHS DK082700NIDDK NIH HHS R01 DK082700NIGMS NIH HHS T32 GM007205NIGMS NIH HHS T32GM07205
6 · The paper itself

Abstract

Sealing of phagosomes is accompanied by the disappearance of phosphatidylinositol (4,5)-bisphosphate (PtdIns(4,5)P(2)) from their cytoplasmic leaflet. Elimination of PtdIns(4,5)P(2), which is required for actin remodeling during phagosome formation, has been attributed to hydrolysis by phospholipase C and phosphorylation by phosphatidylinositol 3-kinase. We found that two inositol 5-phosphatases, OCRL and Inpp5B, become associated with nascent phagosomes. Both phosphatases, which are Rab5 effectors, associate with the adaptor protein APPL1, which is recruited to the phagosomes by active Rab5. Knockdown of APPL1 or inhibition of Rab5 impairs association of OCRL and Inpp5B with phagosomes and prolongs the presence of PtdIns(4,5)P(2) and actin on their membranes. Even though APPL1 can serve as an anchor for Akt, its depletion accentuated the activation of the kinase, likely by increasing the amount of PtdIns(4,5)P(2) available to generate phosphatidylinositol (3,4,5)-trisphosphate. Thus, inositol 5-phosphatases are important contributors to the phosphoinositide remodeling and signaling that are pivotal for phagocytosis.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsCell LineEnzyme ActivationGene Knockdown TechniquesGreen Fluorescent ProteinsMacrophagesMiceMicroscopy, ConfocalPhagosomesPhosphatidylinositolsPhosphoinositide 5-PhosphatasesPhosphoric Monoester HydrolasesProtein BindingProtein TransportProto-Oncogene Proteins c-aktAdaptor Proteins, Signal TransducingAkt1 protein, mouseAppl1 protein, mouseGreen Fluorescent ProteinsOcrl protein, mousePhosphatidylinositolsPhosphoinositide 5-PhosphatasesPhosphoric Monoester HydrolasesProto-Oncogene Proteins c-aktrab5 GTP-Binding ProteinsRecombinant Fusion Proteins

Identifiers

PMID22072788
PMCPMC3248896
OpenAlexW2137629224

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.