Evidence map›Paper›PMID 32753483›Full record

ArticleThe Journal of biological chemistry2020

Development of Noonan syndrome by deregulation of allosteric SOS autoactivation.

Hope Gloria Umutesi, Hanh My Hoang, Hope Elizabeth Johnson, Kwangho Nam, Jongyun Heo

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.5field-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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Dynamic regulation of RAS and RAS signaling.The Biochemical journal · 2023
    Article
  2. Review
  3. Review
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.

Hope Gloria UmutesiDepartment of Chemistry and Biochemistry, University of Texas, Arlington, Texas, USA.
Hanh My HoangDepartment of Chemistry and Biochemistry, University of Texas, Arlington, Texas, USA.
Hope Elizabeth JohnsonDepartment of Chemistry and Biochemistry, University of Texas, Arlington, Texas, USA.
Kwangho NamDepartment of Chemistry and Biochemistry, University of Texas, Arlington, Texas, USA.
Jongyun HeoDepartment of Chemistry and Biochemistry, University of Texas, Arlington, Texas, USA. Electronic address: jheo@uta.edu.
The University of Texas at Arlington · US

Funding

Determination of the mechanism of the immunosuppressive effects of thiopurinesR15AI096146 · NIAID · UNIVERSITY OF TEXAS ARLINGTON · PI HEO, JONGYUN · 2012 to 2012
$440k
NIAID NIH HHS R15 AI096146
6 · The paper itself

Abstract

Ras family proteins play an essential role in several cellular functions, including growth, differentiation, and survival. The mechanism of action of Ras mutants in Costello syndrome and cancers has been identified, but the contribution of Ras mutants to Noonan syndrome, a genetic disorder that prevents normal development in various parts of the body, is unknown. Son of Sevenless (SOS) is a Ras guanine nucleotide exchange factor. In response to Ras-activating cell signaling, SOS autoinhibition is released and is followed by accelerative allosteric feedback autoactivation. Here, using mutagenesis-based kinetic and pulldown analyses, we show that Noonan syndrome Ras mutants I24N, T50I, V152G, and D153V deregulate the autoactivation of SOS to populate their active form. This previously unknown process has been linked so far only to the development of Noonan syndrome. In contrast, other Noonan syndrome Ras mutants-V14I, T58I, and G60E-populate their active form by deregulation of the previously documented Ras GTPase activities. We propose a novel mechanism responsible for the deregulation of SOS autoactivation, where I24N, T50I, V152G, and D153V Ras mutants evade SOS autoinhibition. Consequently, they are capable of forming a complex with the SOS allosteric site, thus aberrantly promoting SOS autoactivation, resulting in the population of active Ras mutants in cells. The results of this study elucidate the molecular mechanism of the Ras mutant-mediated development of Noonan syndrome.

Indexed as

Allosteric SiteHEK293 CellsHumansKineticsModels, MolecularMutationNoonan SyndromeSon of Sevenless ProteinsSon of Sevenless Proteinsallosteric regulationallosteryautoactivationautoinhibitioncatalysisenzyme kineticsguanine nucleotide exchange factor (GEF)Noonan syndromeRasRas proteinSon of SevenlessSOS

Identifiers

PMID32753483
PMCPMC7521655
OpenAlexW3047262621

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.