Evidence map›Paper›PMID 19139278›Full record

ArticleMolecular and cellular biology2009

The mitogen-activated protein kinase scaffold KSR1 is required for recruitment of extracellular signal-regulated kinase to the immunological synapse.

Emanuele Giurisato, Joseph Lin, Angus Harding, Elisa Cerutti, Marina Cella, Robert E Lewis, Marco Colonna, Andrey S Shaw

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

15 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
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  5. Regulation of RAF protein kinases in ERK signalling.Nature reviews. Molecular cell biology · 2015
    Review
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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

8 authors at 4 institutions in 2 countries.

Emanuele GiurisatoDepartment of Pathology & Immunology, Washington University School of Medicine, St. Louis, MO 63110, USA.
Joseph Lin
Angus Harding
Elisa Cerutti
Marina Cella
Robert E Lewis
Marco Colonna
Andrey S Shaw
Washington University in St. Louis · USHoward Hughes Medical Institute · USUniversity of Nebraska Medical Center · USUniversity of Queensland · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

KSR1 is a mitogen-activated protein (MAP) kinase scaffold that enhances the activation of the MAP kinase extracellular signal-regulated kinase (ERK). The function of KSR1 in NK cell function is not known. Here we show that KSR1 is required for efficient NK-mediated cytolysis and polarization of cytolytic granules. Single-cell analysis showed that ERK is activated in an all-or-none fashion in both wild-type and KSR1-deficient cells. In the absence of KSR1, however, the efficiency of ERK activation is attenuated. Imaging studies showed that KSR1 is recruited to the immunological synapse during T-cell activation and that membrane recruitment of KSR1 is required for recruitment of active ERK to the synapse.

Indexed as

Immunological SynapsesAnimalsCell LineCytoplasmic GranulesCytotoxicity, ImmunologicExtracellular Signal-Regulated MAP KinasesHumansKiller Cells, NaturalLymphocyte ActivationMAP Kinase Signaling SystemMiceMice, KnockoutProtein KinasesExtracellular Signal-Regulated MAP KinasesKSR-1 protein kinaseProtein Kinases

Identifiers

PMID19139278
PMCPMC2648244
OpenAlexW2145957054

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.