Evidence map›Paper›PMID 23629860›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2013

Epidermal growth factor-induced cellular invasion requires sphingosine-1-phosphate/sphingosine-1-phosphate 2 receptor-mediated ezrin activation.

K Alexa Orr Gandy, Mohamad Adada, Daniel Canals, Brittany Carroll, Patrick Roddy, Yusuf A Hannun, Lina M Obeid

Open access · greenAbstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

21 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. The doxorubicin-induced cell motility network is under the control of the ceramide-activated protein phosphatase 1 alpha.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Cellular functions of TMEM16/anoctamin.Pflugers Archiv : European journal of physiology · 2016
    Review
  13. Article
  14. Antitumor Activity of a Novel Sphingosine-1-Phosphate 2 Antagonist, AB1, in Neuroblastoma.The Journal of pharmacology and experimental therapeutics · 2015
    Article
  15. Article
  16. A novel role of sphingosine kinase-1 in the invasion and angiogenesis of VHL mutant clear cell renal cell carcinoma.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015
    Article
  17. Review
  18. Article
  19. Article
  20. Article
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

7 authors at 3 institutions in 1 country.

K Alexa Orr GandyDepartment of Molecular and Cellular Biology and Pathobiology, Medical University of South Carolina, Charleston, South Carolina, USA.
Mohamad Adada
Daniel Canals
Brittany Carroll
Patrick Roddy
Yusuf A Hannun
Lina M Obeid
Stony Brook University · USMedical University of South Carolina · USNorthport VA Medical Center · US

Funding

Translational Science Laboratory Shared ResourceP30CA138313 · NCI · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI Jian Ouyang · 2009 to 2026
$42.7M
Sphingolipids in Cancer Therapy and AngiogenesisP01CA097132 · NCI · STATE UNIVERSITY NEW YORK STONY BROOK · PI YUSUF AWNI HANNUN · 2003 to 2026
$30.8M
MEDICAL SCIENTIST TRAINING PROGRAMT32GM008444 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI FROHMAN, MICHAEL A. · 1992 to 2024
$12.6M
TRAINING TO IMPROVE CARDIOVASCULAR THERAPIEST32HL007260 · NHLBI · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI MENICK, DONALD R. · 1985 to 2021
$11.1M
CERAMIDE ACTIVATED PROTEIN PHOSPHATASESR01CA087584 · NCI · STATE UNIVERSITY NEW YORK STONY BROOK · PI HANNUN, YUSUF AWNI · 2000 to 2015
$4.2M
Role and Regulation of Ceramide Synthases in ApoptosisR01GM097741 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI LUBERTO, CHIARA · 2011 to 2019
$3.5M
Sphingosine Phosphate Role in InflammationR01GM062887 · NIGMS · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI OBEID, LINA M · 2001 to 2009
$2.1M
Regulation and Role of Ceramidase in InflammationI01BX000156 · VA · RALPH H JOHNSON VA MEDICAL CENTER · PI OBEID, LINA M · 2009 to 2017
–
BLRD VA I01 BX000156NCI NIH HHS P01 CA097132NCI NIH HHS P01-CA97132NCI NIH HHS P30 CA138313NCI NIH HHS R01 CA087584NCI NIH HHS R01-CA87584NHLBI NIH HHS HL-007260NHLBI NIH HHS T32 HL007260NIGMS NIH HHS R01 GM062887NIGMS NIH HHS R01-GM062887NIGMS NIH HHS R01 GM097741NIGMS NIH HHS T32 GM008444
6 · The paper itself

Abstract

Ezrin, radixin, and moesin (ERM) proteins link cortical actin to the plasma membrane and coordinate cellular events that require cytoskeletal rearrangement, including cell division, migration, and invasion. While ERM proteins are involved in many important cellular events, the mechanisms regulating their function are not completely understood. Our laboratory previously identified reciprocal roles for the sphingolipids ceramide and sphingosine-1-phosphate (S1P) in the regulation of ERM proteins. We recently showed that ceramide-induced activation of PP1α leads to dephosphorylation and inactivation of ERM proteins, while S1P results in phosphorylation and activation of ERM proteins. Following these findings, we aimed to examine known inducers of the SK/S1P pathway and evaluate their ability to regulate ERM proteins. We examined EGF, a known inducer of the SK/S1P pathway, for its ability to regulate the ERM family of proteins. We found that EGF induces ERM c-terminal threonine phosphorylation via activation of the SK/S1P pathway, as this was prevented by siRNA knockdown or pharmacological inhibition of SK. Using pharmacological, as well as genetic, knockdown approaches, we determined that EGF induces ERM phosphorylation via activation of S1PR2. In addition, EGF led to cell polarization in the form of lamellipodia, and this occurred through a mechanism involving S1PR2-mediated phosphorylation of ezrin T567. EGF-induced cellular invasion was also found to be dependent on S1PR2-induced T567 ezrin phosphorylation, such that S1PR2 antagonist, JTE-013, and expression of a dominant-negative ezrin mutant prevented cellular invasion toward EGF. In this work, a novel mechanism of EGF-stimulated invasion is unveiled, whereby S1P-mediated activation of S1PR2 and phosphorylation of ezrin T567 is required.

Indexed as

Cell MovementCytoskeletal ProteinsDose-Response Relationship, DrugEpidermal Growth FactorEzrinHeLa CellsHumansImmunoblottingLysophospholipidsMicroscopy, ConfocalMutationPhosphorylationPhosphotransferases (Alcohol Group Acceptor)PyrazolesPyridinesReceptors, LysosphingolipidCytoskeletal ProteinsEpidermal Growth FactorEzrinJTE 013LysophospholipidsPhosphotransferases (Alcohol Group Acceptor)PyrazolesPyridinesReceptors, LysosphingolipidS1PR2 protein, humanSphingosinesphingosine 1-phosphateSphingosine-1-Phosphate ReceptorsSphingosine Kinaseactin cytoskeletonmoesinpolarizationradixin

Identifiers

PMID23629860
PMCPMC3714586
OpenAlexW2045200199

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.