Evidence map›Paper›PMID 22315426›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Formation and release of arrestin domain-containing protein 1-mediated microvesicles (ARMMs) at plasma membrane by recruitment of TSG101 protein.

Joseph F Nabhan, Ruoxi Hu, Raymond S Oh, Stanley N Cohen, Quan Lu

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 441 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
441citing papers in PubMed, 1 pooled it
11.1field-weighted citation impact, top 1% 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

441 citing papers in PubMed, 1 synthesis or guideline pooled it, 683 citations in OpenAlex.

  1. Pooled it
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  15. Membrane interaction of cyanobacterial and chloroplast ESCRT-III proteins.The Plant journal : for cell and molecular biology · 2026
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381 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Joseph F NabhanProgram in Molecular and Integrative Physiological Sciences, Department of Environmental Health, Harvard School of Public Health, Boston, MA 02115, USA.
Ruoxi Hu
Raymond S Oh
Stanley N Cohen
Quan Lu
Harvard University · USStanford University · US

Funding

Superfund Metal Mixtures, Biomarkers and NeurodevelopmentP42ES016454 · NIEHS · HARVARD SCHOOL OF PUBLIC HEALTH · PI BELLINGER, DAVID C · 2010 to 2015
$10.1M
CIHRNIEHS NIH HHS P42 ES016454NIEHS NIH HHS P42ES016454
6 · The paper itself

Abstract

Mammalian cells are capable of delivering multiple types of membrane capsules extracellularly. The limiting membrane of late endosomes can fuse with the plasma membrane, leading to the extracellular release of multivesicular bodies (MVBs), initially contained within the endosomes, as exosomes. Budding viruses exploit the TSG101 protein and endosomal sorting complex required for transport (ESCRT) machinery used for MVB formation to mediate the egress of viral particles from host cells. Here we report the discovery of a virus-independent cellular process that generates microvesicles that are distinct from exosomes and which, like budding viruses, are produced by direct plasma membrane budding. Such budding is driven by a specific interaction of TSG101 with a tetrapeptide PSAP motif of an accessory protein, arrestin domain-containing protein 1 (ARRDC1), which we show is localized to the plasma membrane through its arrestin domain. This interaction results in relocation of TSG101 from endosomes to the plasma membrane and mediates the release of microvesicles that contain TSG101, ARRDC1, and other cellular proteins. Unlike exosomes, which are derived from MVBs, ARRDC1-mediated microvesicles (ARMMs) lack known late endosomal markers. ARMMs formation requires VPS4 ATPase and is enhanced by the E3 ligase WWP2, which interacts with and ubiquitinates ARRDC1. ARRDC1 protein discharged into ARMMs was observed in co-cultured cells, suggesting a role for ARMMs in intercellular communication. Our findings reveal an intrinsic cellular mechanism that results in direct budding of microvesicles from the plasma membrane, providing a formal paradigm for the evolutionary recruitment of ESCRT proteins in the release of budding viruses.

Indexed as

Adenosine TriphosphatasesAmino Acid MotifsAmino Acid SequenceArrestinBiomarkersCell MembraneDNA-Binding ProteinsEndosomal Sorting Complexes Required for TransportExosomesExtracellular SpaceHEK293 CellsHumansMembrane FusionModels, BiologicalMolecular Sequence DataProtein BindingAdenosine TriphosphatasesArrestinBiomarkersDNA-Binding ProteinsEndosomal Sorting Complexes Required for TransportTranscription FactorsTsg101 ProteinUbiquitin-Protein Ligases

Identifiers

PMID22315426
PMCPMC3306724
OpenAlexW1998307755

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.