Evidence map›Paper›PMID 20331534›Full record

ArticleTraffic (Copenhagen, Denmark)2010

The membrane-associated protein, supervillin, accelerates F-actin-dependent rapid integrin recycling and cell motility.

Zhiyou Fang, Norio Takizawa, Korey A Wilson, Tara C Smith, Anna Delprato, Michael W Davidson, David G Lambright, Elizabeth J Luna

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 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed, 76 citations in OpenAlex.

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  17. Circular RNAFrontiers in genetics · 2018
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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 3 institutions in 2 countries.

Zhiyou FangDepartment of Cell Biology, University of Massachusetts Medical School, Biotech 4, Suite 306, 377 Plantation Street, Worcester, MA 01605, USA.
Norio Takizawa
Korey A Wilson
Tara C Smith
Anna Delprato
Michael W Davidson
David G Lambright
Elizabeth J Luna
University of Massachusetts Chan Medical School · USFlorida State University · USInserm · FR

Funding

STRUCTURAL BASIS OF G PROTEIN MEDIATED SIGNALINGR01GM056324 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI LAMBRIGHT, DAVID G · 1998 to 2018
$6.2M
CYTOSKELTON-MEMBRANE INTERACTIONSR01GM033048 · NIGMS · WORCESTER FOUNDATION FOR BIOMEDICAL RES · PI LUNA, ELIZABETH J. · 1985 to 2009
$3.3M
SHARED HIGH RESOLUTION MULTIMODE MICROSCOPE SYSTEMS10RR015775 · NCRR · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI SLUDER, GREENFIELD · 2001 to 2001
$185k
NCRR NIH HHS 1S10RR015775NIGMS NIH HHS GM033048NIGMS NIH HHS GM056324NIGMS NIH HHS R01 GM033048NIGMS NIH HHS R01 GM056324
6 · The paper itself

Abstract

In migrating cells, the cytoskeleton coordinates signal transduction and redistribution of transmembrane proteins, including integrins and growth factor receptors. Supervillin is an F-actin- and myosin II-binding protein that tightly associates with signaling proteins in cholesterol-rich, 'lipid raft' membrane microdomains. We show here that supervillin also can localize with markers for early and sorting endosomes (EE/SE) and with overexpressed components of the Arf6 recycling pathway in the cell periphery. Supervillin tagged with the photoswitchable fluorescent protein, tdEos, moves both into and away from dynamic structures resembling podosomes at the basal cell surface. Rapid integrin recycling from EE/SE is inhibited in supervillin-knockdown cells, but the rates of integrin endocytosis and recycling from the perinuclear recycling center (PNRC) are unchanged. A lack of synergy between supervillin knockdown and the actin filament barbed-end inhibitor, cytochalasin D, suggests that both treatments affect actin-dependent rapid recycling. Supervillin also enhances signaling from the epidermal growth factor receptor (EGFR) to extracellular signal-regulated kinases (ERKs) 1 and 2 and increases the velocity of cell translocation. These results suggest that supervillin, F-actin and associated proteins coordinate a rapid, basolateral membrane recycling pathway that contributes to ERK signaling and actin-based cell motility.

Indexed as

Cell MovementActinsAnimalsChlorocebus aethiopsCOS CellsCytochalasin DEndocytosisEndosomesErbB ReceptorsExtracellular Signal-Regulated MAP KinasesHeLa CellsHumansIntegrinsMembrane ProteinsMicrofilament ProteinsSignal TransductionActinsCytochalasin DErbB ReceptorsExtracellular Signal-Regulated MAP KinasesIntegrinsMembrane ProteinsMicrofilament ProteinsSVIL protein, human

Identifiers

PMID20331534
PMCPMC2888608
OpenAlexW2062706926

What OpenQuestion holds

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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.