Evidence map›Paper›PMID 31888228›Full record

ArticleCells2019

Phosphatidylinositol Monophosphates Regulate Optimal Vav1 Signaling Output.

Sonia Rodríguez-Fdez, Carmen Citterio, L Francisco Lorenzo-Martín, Jesús Baltanás-Copado, Clara Llorente-González, Senena Corbalán-García, Miguel Vicente-Manzanares, Xosé R Bustelo

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cells, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.4field-weighted citation impact, top 37% 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

5 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Vav2 lacks CaJournal of cell science · 2020
    Article
  5. Article
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

8 authors at 2 institutions in 1 country.

Sonia Rodríguez-FdezCentro de Investigación del Cáncer, CSIC-University of Salamanca, 37007 Salamanca, Spain.ORCID 0000-0001-5369-2969
Carmen CitterioCentro de Investigación del Cáncer, CSIC-University of Salamanca, 37007 Salamanca, Spain.
L Francisco Lorenzo-MartínCentro de Investigación del Cáncer, CSIC-University of Salamanca, 37007 Salamanca, Spain.ORCID 0000-0003-4717-9338
Jesús Baltanás-CopadoDepartment of Biochemistry and Molecular Biology, University of Murcia, 30100 Murcia, Spain.
Clara Llorente-GonzálezCentro de Investigación del Cáncer, CSIC-University of Salamanca, 37007 Salamanca, Spain.
Senena Corbalán-GarcíaDepartment of Biochemistry and Molecular Biology, University of Murcia, 30100 Murcia, Spain.ORCID 0000-0003-1840-5578
Miguel Vicente-ManzanaresCentro de Investigación del Cáncer, CSIC-University of Salamanca, 37007 Salamanca, Spain.ORCID 0000-0001-5943-3220
Xosé R BusteloCentro de Investigación del Cáncer, CSIC-University of Salamanca, 37007 Salamanca, Spain.ORCID 0000-0001-9398-6072
Universidad de Salamanca · ESUniversidad de Murcia · ES

Funding

GENETIC REGULATION OF APOPTOTIC CELL DEATHR01CA064556 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI NUNEZ, GABRIEL · 1994 to 2003
$980k
PRE TARGETED THERAPY USING THE NOVEL TACHYKININ (NK) RECR21CA087408 · NCI · CTR FOR MOLECULAR MEDICINE/IMMUNOLOGY · PI BLUMENTHAL, ROSALYN D · 2000 to 2001
$285k
SXR--A TARGET FOR BREAST CANCER PREVENTION AND TREATMENTR21CA087222 · NCI · UNIVERSITY OF CALIFORNIA IRVINE · PI BLUMBERG, BRUCE · 2000 to 2001
$219k
6 · The paper itself

Abstract

Phosphatidylinositol-5 phosphate (PI5P) and other mono-phosphoinositides (mono-PIs) play second messenger roles in both physiological and pathological conditions. Despite this, their intracellular targets and mechanisms of action remain poorly characterized. Here, we show that Vav1, a protein that exhibits both Rac1 GDP/GTP exchange and adaptor activities, is positively modulated by PI5P and, possibly, other mono-PIs. Unlike other phospholipid-protein complexes, the affinity and specificity of the Vav1-lipid interaction entail a new structural solution that involves the synergistic action of the Vav1 C1 domain and an adjacent polybasic tail. This new regulatory layer, which is not conserved in the Vav family paralogs, favors the engagement of optimal Vav1 signaling outputs in lymphocytes.

Indexed as

AnimalsHumansJurkat CellsMicePhosphatidylinositol PhosphatesPhosphatidylinositolsPhosphorylationProtein BindingProto-Oncogene Proteins c-vavrac1 GTP-Binding ProteinSignal TransductionT-Lymphocytesphosphatidylinositol 4-phosphatephosphatidylinositol 5-phosphatePhosphatidylinositol PhosphatesPhosphatidylinositolsProto-Oncogene Proteins c-vavrac1 GTP-Binding ProteinVAV1 protein, humanVav1 protein, mouseJNKNFATphospholipidsPI4PPI5PRac1Rho GEFsT cell receptorT lymphocytesVav

Identifiers

PMID31888228
PMCPMC6952945
OpenAlexW2995295933

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.