ArticleOncogene2001
The intrinsic ability of AFAP-110 to alter actin filament integrity is linked with its ability to also activate cellular tyrosine kinases.
Article in Oncogene, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Actin-Binding Proteins as Potential Biomarkers for Chronic Inflammation-Induced Cancer Diagnosis and Therapy.Analytical cellular pathology (Amsterdam) · 2021Review
- Long non-coding RNA AFAP1-AS1 plays an oncogenic role in promoting cell migration in non-small cell lung cancer.Cellular and molecular life sciences : CMLS · 2018Article
- Actin Filament-Associated Protein 1-Like 1 Mediates Proliferation and Survival in Non-Small Cell Lung Cancer Cells.Medical science monitor : international medical journal of experimental and clinical research · 2018Article
- Upregulation of the long non-coding RNA AFAP1-AS1 affects the proliferation, invasion and survival of tongue squamous cell carcinoma via the Wnt/β-catenin signaling pathway.Molecular cancer · 2018Article
- Long Noncoding RNA AFAP1-AS1 Promotes Cell Proliferation and Apoptosis of Gastric Cancer Cells via PTEN/p-AKT Pathway.Digestive diseases and sciences · 2017Article
- Long Noncoding RNAs in the Pathogenesis of Barrett's Esophagus and Esophageal Carcinoma.Gastroenterology · 2017Review
- Preparation and Characterization of a Polyclonal Antibody against Human Actin Filament-Associated Protein-120 kD.International journal of molecular sciences · 2016Article
- AFAP1-AS1, a long noncoding RNA upregulated in lung cancer and promotes invasion and metastasis.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016Article
- Long noncoding RNA AFAP1-AS1, a potential novel biomarker to predict the clinical outcome of cancer patients: a meta-analysis.OncoTargets and therapy · 2016Article
- Upregulated long non-coding RNA AFAP1-AS1 expression is associated with progression and poor prognosis of nasopharyngeal carcinoma.Oncotarget · 2015Article
- Actin filament-associated protein 1 is required for cSrc activity and secretory activation in the lactating mammary gland.Oncogene · 2015Article
- AFAP1L1, a novel associating partner with vinculin, modulates cellular morphology and motility, and promotes the progression of colorectal cancers.Cancer medicine · 2014Article
- Junctional adhesion molecules 2 and 3 may potentially be involved in progression of gastric adenocarcinoma tumors.Medical oncology (Northwood, London, England) · 2013Article
- The actin-binding domain of actin filament-associated protein (AFAP) is involved in the regulation of cytoskeletal structure.Cellular and molecular life sciences : CMLS · 2012Article
- Article
- AFAP1L1 is a novel adaptor protein of the AFAP family that interacts with cortactin and localizes to invadosomes.European journal of cell biology · 2011Article
- A Polymorphic Variant of AFAP-110 Enhances cSrc Activity.Translational oncology · 2010Article
- Tiam1 and Rac1 are required for platelet-activating factor-induced endothelial junctional disassembly and increase in vascular permeability.The Journal of biological chemistry · 2009Article
- AFAP120 regulates actin organization during neuronal differentiation.Differentiation; research in biological diversity · 2009Article
- The actin cross-linking protein AFAP120 regulates axon elongation in a tyrosine phosphorylation-dependent manner.Neuroscience letters · 2008Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The actin filament-associated protein of 110 kDa (AFAP-110) is a Src binding partner that represents a potential modulator of actin filament integrity in response to cellular signals. Previous reports have demonstrated that AFAP-110 is capable of directly binding and altering actin filaments. Deletion of the leucine zipper motif of AFAP-110 (AFAP-110(Deltalzip)) has been shown to induce a phenotype which resembles Src-transformed cells, by repositioning actin filaments into rosettes. This deletion also mimics a conformational change in AFAP-110 that is detected in Src-transformed cells. The results presented here indicate that unlike AFAP-110, AFAP-110(Deltalzip) is capable of activating cellular tyrosine kinases, including Src family members, and that AFAP-110(Deltalzip) itself is hyperphosphorylated. The newly tyrosine phosphorylated proteins and activated Src-family members appear to be associated with actin-rich lamellipodia. A point mutation that alters the SH3-binding motif of AFAP-110(Deltalzip) prevents it from activating tyrosine kinases and altering actin filament integrity. In addition, a deletion within a pleckstrin homology (PH) domain of AFAP-110(Deltalzip) will also revert its effects upon actin filaments. Lastly, dominant-positive RhoA(V14) will block the ability of AFAP-110(Deltalzip) from inducing actin filament rosettes, but does not inhibit Src activation. Thus, conformational changes in AFAP-110 enable it to activate cellular kinases in a mechanism requiring SH3 and/or PH domain interactions. We hypothesize that cellular signals which alter AFAP-110 conformation, enable it to activate cellular kinases such as cSrc, which then direct changes in actin filament integrity in a Rho-dependent fashion.
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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.