Evidence map›Paper›PMID 28955033›Full record

ArticleNature communications2017

Plasma membrane-derived extracellular microvesicles mediate non-canonical intercellular NOTCH signaling.

Qiyu Wang, Quan Lu

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

97 citing papers in PubMed, 128 citations in OpenAlex.

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37 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Qiyu WangProgram in Molecular and Integrative Physiological Sciences, Department of Environment Health, Harvard T.H. Chan School of Public Health, 665 Huntington Ave., Boston, MA, 02115, USA.
Quan LuProgram in Molecular and Integrative Physiological Sciences, Department of Environment Health, Harvard T.H. Chan School of Public Health, 665 Huntington Ave., Boston, MA, 02115, USA. qlu@hsph.harvard.edu.
Harvard University · US

Funding

Mechanism and Function of Beta-2 Adrenergic Receptor Degradation in the LungR01HL114769 · NHLBI · HARVARD SCHOOL OF PUBLIC HEALTH · PI LU, QUAN · 2013 to 2016
$1.6M
NanoSight System for Particle Tracking Analysis in Biological FluidsS10OD020086 · OD · HARVARD SCHOOL OF PUBLIC HEALTH · PI LU, QUAN · 2015 to 2015
$144k
NHLBI NIH HHS R01 HL114769NIH HHS S10 OD020086
6 · The paper itself

Abstract

ARMMs (arrestin domain-containing protein 1 (ARRDC1)-mediated microvesicles) are extracellular vesicles that bud directly at the plasma membrane; however, little is known about the molecular composition and physiological function of these vesicles. Here we report that ARMMs contain active NOTCH receptors and mediate a non-canonical intercellular NOTCH signaling. We identify over 100 proteins that are significantly enriched in ARMMs, including ARRDC1, TSG101 and multiple ESCRT complex proteins. About a third of ARMMs-enriched proteins are plasma membrane proteins, including the NOTCH2 receptor. The incorporation of NOTCH2 into ARMMs is facilitated by the ITCH E3 ligase and the metalloprotease ADAM10, both of which are also secreted into ARMMs. NOTCH2 in ARMMs can be delivered into recipient cells, and upon activation by γ-secretase cleavage, induces NOTCH-specific gene expression. Together, our findings reveal a role for ARMMs in a novel NOTCH signaling pathway that acts in distance and is independent of direct cell-cell contact.ARMMs are extracellular vesicles that bud directly at the plasma membrane; their function is poorly understood. Here the authors purify and carryout a proteomics analysis of the protein components of ARMMs, and show that NOTCH receptors are recruited into ARMMs and can be transferred to recipient cells to mediate NOTCH signaling.

Indexed as

Amyloid Precursor Protein SecretasesArrestinCell Line, TumorCell MembraneExtracellular VesiclesHEK293 CellsHumansMembrane ProteinsProtein TransportReceptor, Notch2Receptors, NotchSignal TransductionUbiquitin-Protein LigasesAmyloid Precursor Protein SecretasesArrestinMembrane ProteinsReceptor, Notch2Receptors, NotchUbiquitin-Protein Ligases

Identifiers

PMID28955033
PMCPMC5617834
OpenAlexW2758102094

What OpenQuestion holds

Textmetadata
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.