Evidence map›Paper›PMID 16705171›Full record

ArticleMolecular and cellular biology2006

Focal adhesion kinase controls cellular levels of p27/Kip1 and p21/Cip1 through Skp2-dependent and -independent mechanisms.

Patrick Bryant, Qingxia Zheng, Kevin Pumiglia

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 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.1field-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

42 citing papers in PubMed, 69 citations in OpenAlex.

  1. Zyxin protects against hypertensive nephropathy by restraining FAK/Skp2-CDK8/YAP signaling in tubular epithelial cells.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2026
    Article
  2. Review
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  4. Article
  5. Targeting CDK2 to combat drug resistance in cancer therapy.Future oncology (London, England) · 2024
    Review
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  18. An In Vitro Model of Cellular Quiescence in Primary Human Dermal Fibroblasts.Methods in molecular biology (Clifton, N.J.) · 2018
    Article
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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

3 authors at 1 institution in 1 country.

Patrick BryantCenter for Cell Biology and Cancer Research, Albany Medical College, 47 New Scotland Ave., Albany, NY 12208, USA.
Qingxia Zheng
Kevin Pumiglia
Albany Medical Center Hospital · US

Funding

TISSUE REMODELING AND CARDIOVASCULAR DISEASET32HL007194 · NHLBI · ALBANY MEDICAL COLLEGE · PI MC KEOWN-LONGO, PAULA J · 1985 to 2006
$2.9M
VEGF SIGNAL TRANSDUCTION AND TUMOR ANGIOGENESISR01CA081419 · NCI · ALBANY MEDICAL COLLEGE · PI PUMIGLIA, KEVIN M · 1999 to 2008
$2.0M
NCI NIH HHS CA81419NCI NIH HHS R01 CA081419NHLBI NIH HHS T32 HL007194NHLBI NIH HHS T32-HL-07194
6 · The paper itself

Abstract

Endothelial cell proliferation is a critical step in angiogenesis and requires a coordinated response to soluble growth factors and the extracellular matrix. As focal adhesion kinase (FAK) integrates signals from both adhesion events and growth factor stimulation, we investigated its role in endothelial cell proliferation. Expression of a dominant-negative FAK protein, FAK-related nonkinase (FRNK), impaired phosphorylation of FAK and blocked DNA synthesis in response to multiple angiogenic stimuli. These results coincided with elevated cyclin-dependent kinase inhibitors (CDKIs) p21/Cip and p27/Kip, as a consequence of impaired degradation. FRNK inhibited the expression of Skp2, an F-box protein that targets CDKIs, by inhibiting mitogen-induced mRNA. The FAK-regulated degradation of p27/Kip was Skp2 dependent, while levels of p21/Cip were regulated independent of Skp2. Skp2 is required for endothelial cell proliferation as a consequence of degrading p27. Finally, knockdown of both p21 and p27 in FRNK-expressing cells completely restored mitogen-induced endothelial cell proliferation. These data demonstrate a critical role for FAK in the regulation of CDKIs through two independent mechanisms: Skp2 dependent and Skp2 independent. They also provide important insights into the requirement of focal adhesion kinase for normal vascular development and reveal novel regulatory control points for angiogenesis.

Indexed as

Cell AdhesionCell MovementCell ProliferationCells, CulturedCell SurvivalCyclin-Dependent Kinase Inhibitor p21Cyclin-Dependent Kinase Inhibitor p27Endothelial CellsExtracellular Signal-Regulated MAP KinasesFocal Adhesion Protein-Tyrosine KinasesGene Expression Regulation, EnzymologicHumansPaxillinPhosphorylationProtein Processing, Post-TranslationalProtein-Tyrosine KinasesCyclin-Dependent Kinase Inhibitor p21Cyclin-Dependent Kinase Inhibitor p27Extracellular Signal-Regulated MAP KinasesFAK-related nonkinaseFocal Adhesion Protein-Tyrosine KinasesPaxillinProtein-Tyrosine KinasesRNA, MessengerS-Phase Kinase-Associated ProteinsVascular Endothelial Growth Factor A

Identifiers

PMID16705171
PMCPMC1489078
OpenAlexW2120440477

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.