Evidence map›Paper›PMID 22981863›Full record

ArticleMolecular cell2012

LAT-independent Erk activation via Bam32-PLC-γ1-Pak1 complexes: GTPase-independent Pak1 activation.

Alexandre K Rouquette-Jazdanian, Connie L Sommers, Robert L Kortum, Deborah K Morrison, Lawrence E Samelson

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

24 citing papers in PubMed, 34 citations in OpenAlex.

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  10. Genome-wide CRISPR screen identifies FAM49B as a key regulator of actin dynamics and T cell activation.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  11. Article
  12. Frontiers in cellular and infection microbiology · 2018
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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.

Alexandre K Rouquette-JazdanianLaboratory of Cellular and Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Connie L Sommers
Robert L Kortum
Deborah K Morrison
Lawrence E Samelson
National Institutes of Health · US

Funding

Biochemical Basis of T Cell ActivationZIABC010304 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI SAMELSON, LAWRENCE · 2009 to 2025
$36.3M
Regulation of Ras-Dependent Signal Transduction PathwaysZIABC010329 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI MORRISON, DEBORAH · 2009 to 2025
$16.1M
Role of Protein Scaffolds in RTKRas-dependent Signal TransductionZIABC011107 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI MORRISON, DEBORAH · 2009 to 2025
$7.3M
Intramural NIH HHS Z99 CA999999NCI NIH HHS Y99 CA999999
6 · The paper itself

Abstract

In T cells, the adaptor Bam32 is coupled to Erk activation downstream of the TCR by an unknown mechanism. We characterized in Jurkat cells and primary T lymphocytes a pathway dependent on Bam32-PLC-γ1-Pak1 complexes, in which Pak1 kinase activates Raf-1 and Mek-1, both upstream of Erk. In the Bam32-PLC-γ1-Pak1 complex, catalytically inactive PLC-γ1 is used as a scaffold linking Bam32 to Pak1. PLC-γ1(C-SH2) directly binds S141 of Bam32, preventing LAT-mediated activation of Ras by PLC-γ1. The Bam32-PLC-γ1 interaction enhances the binding of the SH3 domain of the phospholipase with Pak1. The PLC-γ1(SH3)-Pak1 interaction activates Pak1 independently of the small GTPases Rac1/Cdc42, previously described as being the only activators of Pak1 in T cells. Direct binding of the SH3 domain of PLC-γ1 to Pak1 dissociates inactive Pak1 homodimers, a mechanism required for Pak1 activation. We have thus uncovered a LAT/Ras-independent, Bam32-nucleated pathway that activates Erk signaling in T cells.

Indexed as

Protein Interaction MapsSignal TransductionAdaptor Proteins, Signal TransducingBinding SitesCD4-Positive T-LymphocytesGTP PhosphohydrolasesHumansJurkat CellsMAP Kinase Kinase 1MAP Kinase Signaling SystemMembrane ProteinsMultiprotein Complexesp21-Activated KinasesPhospholipase C gammaProto-Oncogene Proteins c-rafsrc Homology DomainsAdaptor Proteins, Signal TransducingGTP PhosphohydrolasesLAT protein, humanMAP2K1 protein, humanMAP Kinase Kinase 1Membrane ProteinsMultiprotein Complexesp21-Activated KinasesPAK1 protein, humanPhospholipase C gammaProto-Oncogene Proteins c-rafType C Phospholipases

Identifiers

PMID22981863
PMCPMC3483363
OpenAlexW2063950156

What OpenQuestion holds

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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.