Evidence map›Paper›PMID 16581786›Full record

ArticleMolecular and cellular biology2006

The ETS protein MEF is regulated by phosphorylation-dependent proteolysis via the protein-ubiquitin ligase SCFSkp2.

Yan Liu, Cyrus V Hedvat, Shifeng Mao, Xin-Hua Zhu, Jinjuan Yao, Hoang Nguyen, Andrew Koff, Stephen D Nimer

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

26 citing papers in PubMed, 37 citations in OpenAlex.

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  16. Cullins and cancer.Genes & cancer · 2010
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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 2 institutions in 2 countries.

Yan LiuDivision of Hematologic Oncology, Department of Medicine, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, Box 575, New York, NY 10021, USA.
Cyrus V Hedvat
Shifeng Mao
Xin-Hua Zhu
Jinjuan Yao
Hoang Nguyen
Andrew Koff
Stephen D Nimer
Laboratory of Molecular Genetics · PLKettering University · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Nicholas D Socci · 1985 to 2026
$347.4M
FUNCTION OF MEF IN HEMATOPOIETIC CELLSR01DK052208 · NIDDK · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI NIMER, STEPHEN D. · 1997 to 2011
$3.1M
REGULATION OF P27 AND ITS ROLE IN G1 PROGRESSIONR01GM052597 · NIGMS · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI KOFF, ANDREW · 1996 to 2003
$1.4M
ROLE OF MYELOID ELF-1 LIKE FACTOR IN HEMATOPOIESISK08HL004478 · NHLBI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI HEDVAT, CYRUS V · 2001 to 2005
$629k
Function of MEF in Hematopoietic CellsR56DK052208 · NIDDK · SLOAN-KETTERING INST CAN RESEARCH · PI NIMER, STEPHEN DAVID · 2007 to 2007
$500k
REGULATION OF P27KIPI AND ITS ROLE IN G1 PROGRESSIONR55GM052597 · NIGMS · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI KOFF, ANDREW · 1995 to 1995
–
NCI NIH HHS P30 CA008748NHLBI NIH HHS K08 HL004478NHLBI NIH HHS K08 HL 04478NIDDK NIH HHS DK 52208NIDDK NIH HHS R01 DK052208NIDDK NIH HHS R56 DK052208NIGMS NIH HHS GM 52597NIGMS NIH HHS R01 GM052597
6 · The paper itself

Abstract

MEF is an ETS-related transcription factor with strong transcriptional activating activity that affects hematopoietic stem cell behavior and is required for normal NK cell and NK T-cell development. The MEF (also known as ELF4) gene is repressed by several leukemia-associated fusion transcription factor proteins (PML-retinoic acid receptor alpha and AML1-ETO), but it is also activated by retroviral insertion in several cancer models. We have previously shown that cyclin A-dependent phosphorylation of MEF largely restricts its activity to the G(1) phase of the cell cycle; we now show that MEF is a short-lived protein whose expression level also peaks during late G(1) phase. Mutagenesis studies show that the rapid turnover of MEF in S phase is dependent on the specific phosphorylation of threonine 643 and serine 648 at the C terminus of MEF by cdk2 and on the Skp1/Cul1/F-box (SCF) E3 ubiquitin ligase complex SCF(Skp2), which targets MEF for ubiquitination and proteolysis. Overexpression of MEF drives cells through the G(1)/S transition, thereby promoting cell proliferation. The tight regulation of MEF levels during the cell cycle contributes to its effects on regulating cell cycle entry and cell proliferation.

Indexed as

Amino Acid SequenceCell LineCell Line, TumorCysteine Proteinase InhibitorsDNA-Binding ProteinsGene Expression RegulationHalf-LifeHumansHydrolysisLeupeptinsLigasesMutagenesis, Site-DirectedPhosphorylationProteinsSerineThreoninebenzyloxycarbonylleucyl-leucyl-leucine aldehydeCysteine Proteinase InhibitorsDNA-Binding ProteinsELF4 protein, humanLeupeptinsLigasesProteinsSerineThreonineTranscription FactorsUbiquitin

Identifiers

PMID16581786
PMCPMC1446966
OpenAlexW2149358418

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.