Evidence map›Paper›PMID 20214752›Full record

ArticleTraffic (Copenhagen, Denmark)2010

Cell-free reconstitution of multivesicular body formation and receptor sorting.

Wei Sun, Thomas A Vida, Natalie Sirisaengtaksin, Samuel A Merrill, Phyllis I Hanson, Andrew J Bean

Open access · bronzeAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.1field-weighted citation impact, top 26% 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

12 citing papers in PubMed, 18 citations in OpenAlex.

  1. O-GlcNAcylation regulates epidermal growth factor receptor intracellular trafficking and signaling.Proceedings of the National Academy of Sciences of the United States of America · 2022
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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

6 authors at 2 institutions in 1 country.

Wei SunDepartment of Neurobiology and Anatomy, University of Texas Health Science Center, Houston, TX, USA.
Thomas A Vida
Natalie Sirisaengtaksin
Samuel A Merrill
Phyllis I Hanson
Andrew J Bean
The University of Texas Health Science Center at Houston · USWashington University in St. Louis · US

Funding

Tumor Evolution and Metastasis ProgramP30CA016672 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI Scott Kopetz · 1985 to 2026
$290.8M
MOLECULAR MECHANISMS OF NEUROTRANSMITTER SECRETIONR01MH058920 · NIMH · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI BEAN, ANDREW J · 1998 to 2010
$2.9M
NCI NIH HHS CA16672NCI NIH HHS P30 CA016672NIMH NIH HHS MH-58920NIMH NIH HHS R01 MH058920
6 · The paper itself

Abstract

The number of surface membrane proteins and their residence time on the plasma membrane are critical determinants of cellular responses to cues that can control plasticity, growth and differentiation. After internalization, the ultimate fate of many plasma membrane proteins is dependent on whether they are sorted for internalization into the lumenal vesicles of multivesicular bodies (MVBs), an obligate step prior to lysosomal degradation. To help to elucidate the mechanisms underlying MVB sorting, we have developed a novel cell-free assay that reconstitutes the sorting of a prototypical membrane protein, the epidermal growth factor receptor, with which we have probed some of its molecular requirements. The sorting event measured is dependent on cytosol, ATP, time, temperature and an intact proton gradient. Depletion of Hrs inhibited biochemical and morphological measures of sorting that were rescued by inclusion of recombinant Hrs in the assay. Moreover, depletion of signal-transducing adaptor molecule (STAM), or addition of mutated ATPase-deficient Vps4, also inhibited sorting. This assay reconstitutes the maturation of late endosomes, including the formation of internal vesicles and the sorting of a membrane protein, and allows biochemical investigation of this process.

Indexed as

Cell-Free SystemAdaptor Proteins, Signal TransducingAdenosine TriphosphatasesAnimalsATPases Associated with Diverse Cellular ActivitiesBrainCell MembraneEndocytosisEndosomal Sorting Complexes Required for TransportEndosomesHeLa CellsHumansLysosomesMicroscopy, ElectronModels, BiologicalPhosphoproteinsAdaptor Proteins, Signal TransducingAdenosine TriphosphatasesATPases Associated with Diverse Cellular ActivitiesEndosomal Sorting Complexes Required for TransportPhosphoproteinsSTAM protein, humanVacuolar Proton-Translocating ATPasesVPS4A protein, human

Identifiers

PMID20214752
PMCPMC3375900
OpenAlexW2012564813

What OpenQuestion holds

Textmetadata
LicenceTDM
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.