Evidence map›Paper›PMID 29626191›Full record

ArticleNature communications2018

Lipid binding promotes the open conformation and tumor-suppressive activity of neurofibromin 2.

Krishna Chinthalapudi, Vinay Mandati, Jie Zheng, Andrew J Sharff, Gerard Bricogne, Patrick R Griffin, Joseph Kissil, Tina Izard

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

32 citing papers in PubMed, 52 citations in OpenAlex.

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  11. FERM domains recruit ample PI(4,5)PBiophysical journal · 2023
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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 2 institutions in 2 countries.

Krishna ChinthalapudiDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, Jupiter, FL, 33458, USA.
Vinay MandatiDepartment of Molecular Medicine, The Scripps Research Institute, Jupiter, FL, 33458, USA.
Jie ZhengDepartment of Molecular Medicine, The Scripps Research Institute, Jupiter, FL, 33458, USA.
Andrew J SharffGlobal Phasing Ltd., Sheraton House, Castle Park, Cambridge, CB3 0AX, United Kingdom.
Gerard BricogneGlobal Phasing Ltd., Sheraton House, Castle Park, Cambridge, CB3 0AX, United Kingdom.
Patrick R GriffinDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, Jupiter, FL, 33458, USA.
Joseph KissilDepartment of Molecular Medicine, The Scripps Research Institute, Jupiter, FL, 33458, USA.
Tina IzardDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, Jupiter, FL, 33458, USA. cmorrow@scripps.edu.
Scripps Research Institute · USGlobal Phasing (United Kingdom) · GB

Funding

Mechanisms of cell contact inhibition and their dysregulation in cancer.R01NS077952 · NINDS · SCRIPPS FLORIDA · PI KISSIL, JOSEPH · 2013 to 2017
$2.1M
NINDS NIH HHS R01 NS077952
6 · The paper itself

Abstract

Neurofibromatosis type 2 (NF2) is a tumor-forming disease of the nervous system caused by deletion or by loss-of-function mutations in NF2, encoding the tumor suppressing protein neurofibromin 2 (also known as schwannomin or merlin). Neurofibromin 2 is a member of the ezrin, radixin, moesin (ERM) family of proteins regulating the cytoskeleton and cell signaling. The correlation of the tumor-suppressive function and conformation (open or closed) of neurofibromin 2 has been subject to much speculation, often based on extrapolation from other ERM proteins, and controversy. Here we show that lipid binding results in the open conformation of neurofibromin 2 and that lipid binding is necessary for inhibiting cell proliferation. Collectively, our results provide a mechanism in which the open conformation is unambiguously correlated with lipid binding and localization to the membrane, which are critical for the tumor-suppressive function of neurofibromin 2, thus finally reconciling the long-standing conformation and function debate.

Indexed as

Lipid MetabolismCell LineCell ProliferationCrystallography, X-RayHEK293 CellsHumansNeurofibromin 2Phosphatidylinositol 4,5-DiphosphateProtein BindingProtein ConformationProtein Interaction Domains and MotifsSignal TransductionNeurofibromin 2Phosphatidylinositol 4,5-Diphosphate

Identifiers

PMID29626191
PMCPMC5889391
OpenAlexW2795560340

What OpenQuestion holds

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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.