Evidence map›Paper›PMID 24297905›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Regulation of Son of sevenless by the membrane-actin linker protein ezrin.

Katja J Geissler, M Juliane Jung, Lars Björn Riecken, Tobias Sperka, Yan Cui, Stephan Schacke, Ulrike Merkel, Robby Markwart, Ignacio Rubio, Manuel E Than and 6 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

14 citing papers in PubMed, 26 citations in OpenAlex.

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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

16 authors at 5 institutions in 3 countries.

Katja J GeisslerH.M. Laboratory, P.H. Laboratory, and M.E.T. Laboratory, Leibniz Institute for Age Research - Fritz Lipmann Institute, 07745 Jena, Germany.
M Juliane Jung
Lars Björn Riecken
Tobias Sperka
Yan Cui
Stephan Schacke
Ulrike Merkel
Robby Markwart
Ignacio Rubio
Manuel E Than
Constanze Breithaupt
Sebastian Peuker
Reinhard Seifert
Ulrich Benjamin Kaupp
Peter Herrlich
Helen Morrison
Center of Advanced European Studies and Research · DEBP (United Kingdom) · GBSchiller International University · FRLeibniz Institute on Aging - Fritz Lipmann Institute (FLI) · DEMartin Luther University Halle-Wittenberg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Receptor tyrosine kinases participate in several signaling pathways through small G proteins such as Ras (rat sarcoma). An important component in the activation of these G proteins is Son of sevenless (SOS), which catalyzes the nucleotide exchange on Ras. For optimal activity, a second Ras molecule acts as an allosteric activator by binding to a second Ras-binding site within SOS. This allosteric Ras-binding site is blocked by autoinhibitory domains of SOS. We have reported recently that Ras activation also requires the actin-binding proteins ezrin, radixin, and moesin. Here we report the mechanism by which ezrin modulates SOS activity and thereby Ras activation. Active ezrin enhances Ras/MAPK signaling and interacts with both SOS and Ras in vivo and in vitro. Moreover, in vitro kinetic assays with recombinant proteins show that ezrin also is important for the activity of SOS itself. Ezrin interacts with GDP-Ras and with the Dbl homology (DH)/pleckstrin homology (PH) domains of SOS, bringing GDP-Ras to the proximity of the allosteric site of SOS. These actions of ezrin are antagonized by the neurofibromatosis type 2 tumor-suppressor protein merlin. We propose an additional essential step in SOS/Ras control that is relevant for human cancer as well as all physiological processes involving Ras.

Indexed as

MAP Kinase Signaling SystemAnimalsCytoskeletal ProteinsEzrinGuanosine DiphosphateHumansMiceNeoplasmsNeurofibromin 2NIH 3T3 CellsOncogene Protein p21(ras)Son of Sevenless ProteinsCytoskeletal ProteinsEzrinGuanosine DiphosphateNeurofibromin 2Oncogene Protein p21(ras)Son of Sevenless ProteinsautoinhibitionERM proteinsGEF regulation

Identifiers

PMID24297905
PMCPMC3870676
OpenAlexW2013295723

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.