Evidence map›Paper›PMID 22323291›Full record

ArticleMolecular biology of the cell2012

Phosphoinositide lipid phosphatase SHIP1 and PTEN coordinate to regulate cell migration and adhesion.

Subhanjan Mondal, Kulandayan K Subramanian, Jiro Sakai, Besnik Bajrami, Hongbo R Luo

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 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

37 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Article
  3. Neutrophil diversity and function in health and disease.Signal transduction and targeted therapy · 2024
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  7. Expression ofGenes · 2023
    Article
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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

5 authors at 1 institution in 1 country.

Subhanjan MondalDepartment of Pathology, Harvard Medical School, Department of Laboratory Medicine, Children's Hospital Boston, Boston, MA 02115, USA.
Kulandayan K Subramanian
Jiro Sakai
Besnik Bajrami
Hongbo R Luo
Boston Children's Hospital · US

Funding

Enhancing neutrophil function in neutropenia-related pneumoniaR01HL092020 · NHLBI · BOSTON CHILDREN'S HOSPITAL · PI LUO, HONGBO R · 2009 to 2022
$5.2M
Molecular basis of neutrophil spontaneous deathR01HL085100 · NHLBI · BOSTON CHILDREN'S HOSPITAL · PI LUO, HONGBO R · 2007 to 2010
$2.0M
HTS for enhancers of neutrophil function that specifically augment PIP3 signalR01AI076471 · NIAID · BOSTON CHILDREN'S HOSPITAL · PI LUO, HONGBO R · 2009 to 2012
$1.5M
Signal transduction in neutrophil chemotaxisR01GM076084 · NIGMS · BOSTON CHILDREN'S HOSPITAL · PI LUO, HONGBO R · 2006 to 2010
$1.5M
NHLBI NIH HHS HL085100NHLBI NIH HHS HL092020NHLBI NIH HHS R01 HL085100NHLBI NIH HHS R01 HL092020NIAID NIH HHS AI076471NIAID NIH HHS R01 AI076471NIGMS NIH HHS GM076084NIGMS NIH HHS R01 GM076084
6 · The paper itself

Abstract

The second messenger phosphatidylinositol(3,4,5)P(3) (PtdIns(3,4,5)P(3)) is formed by stimulation of various receptors, including G protein-coupled receptors and integrins. The lipid phosphatases PTEN and SHIP1 are critical in regulating the level of PtdIns(3,4,5)P(3) during chemotaxis. Observations that loss of PTEN had minor and loss of SHIP1 resulted in a severe chemotaxis defect in neutrophils led to the belief that SHIP1 rather than PTEN acts as a predominant phospholipid phosphatase in establishing a PtdIns(3,4,5)P(3) compass. In this study, we show that SHIP1 regulates PtdIns(3,4,5)P(3) production in response to cell adhesion and plays a limited role when cells are in suspension. SHIP1((-)/(-)) neutrophils lose their polarity upon cell adhesion and are extremely adherent, which impairs chemotaxis. However, chemo-taxis can be restored by reducing adhesion. Loss of SHIP1 elevates Akt activation following cell adhesion due to increased PtdIns(3,4,5)P(3) production. From our observations, we conclude that SHIP1 prevents formation of top-down PtdIns(3,4,5)P(3) polarity to facilitate proper cell attachment and detachment during chemotaxis.

Indexed as

AnimalsCell AdhesionCell MovementCell PolarityChemotaxis, LeukocyteInositol Polyphosphate 5-PhosphatasesIn Vitro TechniquesMiceMice, KnockoutModels, BiologicalNeutrophilsPhosphatidylinositol-3,4,5-Trisphosphate 5-PhosphatasesPhosphatidylinositol PhosphatesPhosphoric Monoester HydrolasesPhosphorylationProto-Oncogene Proteins c-aktInositol Polyphosphate 5-PhosphatasesInpp5d protein, mousephosphatidylinositol 3,4,5-triphosphatePhosphatidylinositol-3,4,5-Trisphosphate 5-PhosphatasesPhosphatidylinositol PhosphatesPhosphoric Monoester HydrolasesProto-Oncogene Proteins c-aktPTEN PhosphohydrolasePten protein, mouseReactive Oxygen SpeciesTyrosine

Identifiers

PMID22323291
PMCPMC3315799
OpenAlexW2124810927

What Socratic 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 Socratic graph.