ArticleMolecular and cellular biology2003
Regulation of focal adhesion kinase by its amino-terminal domain through an autoinhibitory interaction.
Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
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.
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.
Who cites it
73 citing papers in PubMed, 167 citations in OpenAlex.
- miR-373 promotes invasion and metastasis of colorectal cancer cells via activating ERK/MAPK pathway.Scientific reports · 2024Article
- PLEKHH2 binds β-arrestin1 through its FERM domain, activates FAK/PI3K/AKT phosphorylation, and promotes the malignant phenotype of non-small cell lung cancer.Cell death & disease · 2022Article
- FAK in Cancer: From Mechanisms to Therapeutic Strategies.International journal of molecular sciences · 2022Review
- ZINC40099027 activates human focal adhesion kinase by accelerating the enzymatic activity of the FAK kinase domain.Pharmacology research & perspectives · 2021Article
- Manipulation of Focal Adhesion Signaling by Pathogenic Microbes.International journal of molecular sciences · 2021Review
- Roles of Integrins in Gastrointestinal Cancer Metastasis.Frontiers in molecular biosciences · 2021Review
- Loss of CDCP1 triggers FAK activation in detached prostate cancer cells.American journal of clinical and experimental urology · 2021Article
- Beta-arrestins operate an on/off control switch for focal adhesion kinase activity.Cellular and molecular life sciences : CMLS · 2020Article
- FAK Signaling in Rhabdomyosarcoma.International journal of molecular sciences · 2020Review
- Structural basis of Focal Adhesion Kinase activation on lipid membranes.The EMBO journal · 2020Article
- A FAK conundrum is solved: activation and organization of focal adhesion kinase at the plasma membrane.The EMBO journal · 2020Article
- FAK Family Kinases in Vascular Diseases.International journal of molecular sciences · 2020Review
- Integrin alpha11 is an Osteolectin receptor and is required for the maintenance of adult skeletal bone mass.eLife · 2019Article
- Adhesions Assemble!-Autoinhibition as a Major Regulatory Mechanism of Integrin-Mediated Adhesion.Frontiers in molecular biosciences · 2019Review
- Review
- Cx26 drives self-renewal in triple-negative breast cancer via interaction with NANOG and focal adhesion kinase.Nature communications · 2018Article
- Revisiting Netrin-1: One Who Guides (Axons).Frontiers in cellular neuroscience · 2018Review
- Cell matrix adhesions in cancer: The proteins that form the glue.Oncotarget · 2017Review
- Kindlin-1 contributes to EGF-induced re-epithelialization in skin wound healing.International journal of molecular medicine · 2017Article
- Addressing the Functional Determinants of FAK during Ciliogenesis in Multiciliated Cells.The Journal of biological chemistry · 2017Article
13 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
We have investigated a role for the amino-terminal FERM-like domain of the focal adhesion kinase (FAK) as a negative regulator of its own activity and phosphorylation state. Deletion of the first 375 amino acids from the amino terminus of FAK increases its catalytic activity in vitro, its phosphorylation when expressed in mammalian cells, and the phosphorylation of a FAK substrate, paxillin. Deletion mutants are phosphorylated in suspension, suggesting that they are no longer regulated by adhesion. The amino terminus of FAK can interact with the kinase domain of FAK in vitro and in vivo, suggesting that it might act as an autoinhibitor of FAK activity. The amino terminus of FAK can act in trans to inhibit FAK phosphorylation when expressed in mammalian cells or to directly inhibit FAK activity in vitro. Expression of the amino terminus of FAK inhibits cell cycle progression in CHO cells, consistent with its inhibition of FAK phosphorylation and function in trans. A glutathione S-transferase fusion protein containing the cytoplasmic tail of the beta1 integrin stimulates FAK activity in vitro, suggesting that FAK could be regulated by molecular interactions with the amino terminus. Based on these and previous data, we propose a working model for activation of FAK in cell adhesion.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.