Evidence map›Paper›PMID 24196439›Full record

ArticleCell cycle (Georgetown, Tex.)2014

CDK6 binds and promotes the degradation of the EYA2 protein.

Dawn Kohrt, Jennifer Crary, Marc Zimmer, Aaron N Patrick, Heide L Ford, Philip W Hinds, Martha J Grossel

Open access · hybridAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.9field-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

8 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
  2. microRNA-155-5p initiates childhood acute lymphoblastic leukemia by regulating the IRF4/CDK6/CBL axis.Laboratory investigation; a journal of technical methods and pathology · 2022
    Article
  3. The multi-functional eyes absent proteins.Critical reviews in biochemistry and molecular biology · 2020
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
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 5 institutions in 2 countries.

Dawn KohrtDepartment of Biology; Connecticut College; New London, CT USA.
Jennifer CraryDepartment of Biology; Connecticut College; New London, CT USA; Department of Developmental, Molecular, and Chemical Biology; Tufts University School of Medicine, and Molecular Oncology Research Institute; Tufts Medical Center; Boston, MA USA.
Marc ZimmerDepartment of Chemistry; Connecticut College; New London, CT USA.
Aaron N PatrickDepartment of Pharmacology; University of Colorado School of Medicine; Aurora, CO USA.
Heide L FordDepartment of Pharmacology; University of Colorado School of Medicine; Aurora, CO USA.
Philip W HindsDepartment of Developmental, Molecular, and Chemical Biology; Tufts University School of Medicine, and Molecular Oncology Research Institute; Tufts Medical Center; Boston, MA USA.
Martha J GrosselDepartment of Biology; Connecticut College; New London, CT USA.
Connecticut College · USMolecular Oncology (United States) · USThe Medical Center of Aurora · USTufts Medical Center · USUniversity of Colorado Denver · US

Funding

Role of Six1 in EMT and Tumor ProgressionR01CA095277 · NCI · UNIVERSITY OF COLORADO DENVER · PI FORD, HEIDE L. · 2002 to 2017
$4.3M
POSTGRADUATE TRAINING IN PEDIATRIC ONCOLOGYT32CA082086 · NCI · UNIVERSITY OF COLORADO DENVER · PI GORE, LIA · 2000 to 2015
$4.1M
Mechanism of Differentiation Functions of Cyclin Dependent Kinase 6 (Cdk6)R15CA125731 · NCI · CONNECTICUT COLLEGE · PI GROSSEL, MARTHA J. · 2007 to 2015
$1.0M
Understanding and finding new fluorescent proteinsR15GM059108 · NIGMS · CONNECTICUT COLLEGE · PI ZIMMER, MARC · 1999 to 2009
$478k
NCI NIH HHS R012R01-CA095277NCI NIH HHS R01 CA095277NCI NIH HHS R15 CA125731NCI NIH HHS R15CA125731-02A1NCI NIH HHS T32 CA082086NIGMS NIH HHS R15 GM059108NIGMS NIH HHS R15GM059108-04
6 · The paper itself

Abstract

Cyclin-dependent kinase 6 (Cdk6) is a D-Cyclin-activated kinase that is directly involved in driving the cell cycle through inactivation of pRB in G₁ phase. Increasingly, evidence suggests that CDK6, while directly driving the cell cycle, may only be essential for proliferation of specialized cell types, agreeing with the notion that CDK6 also plays an important role in differentiation. Here, evidence is presented that CDK6 binds to and promotes degradation of the EYA2 protein. The EYA proteins are a family of proteins that activate genes essential for the development of multiple organs, regulate cell proliferation, and are misregulated in several types of cancer. This interaction suggests that CDK6 regulates EYA2 activity, a mechanism that could be important in development and in cancer.

Indexed as

ProteolysisCell CycleCell DifferentiationCell ProliferationCyclin-Dependent Kinase 6G1 PhaseHEK293 CellsHumansIntracellular Signaling Peptides and ProteinsNeoplasmsNuclear ProteinsProtein Tyrosine PhosphatasesCDK6 protein, humanCyclin-Dependent Kinase 6EYA2 protein, humanIntracellular Signaling Peptides and ProteinsNuclear ProteinsProtein Tyrosine PhosphatasescancerCdk6cell cycledegradationEYA2progenitor cellproliferation

Identifiers

PMID24196439
PMCPMC3925736
OpenAlexW2057447480

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.