ArticleMolecular biology of the cell2002
PC phosphorylation increases the ability of AFAP-110 to cross-link actin filaments.
Article in Molecular biology of the cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 43 citations in OpenAlex.
- Cross-Tissue Transcriptome-Wide Association Study and TWAS-FOCUS Fine-Mapping Reveal Novel Susceptibility Genes for Primary Open-Angle Glaucoma.Translational vision science & technology · 2026Article
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- Spatial proximity of proteins surrounding zyxin under force-bearing conditions.Molecular biology of the cell · 2021Article
- AFAP1-AS1: A novel oncogenic long non-coding RNA in human cancers.Cell proliferation · 2018Review
- Preparation and Characterization of a Polyclonal Antibody against Human Actin Filament-Associated Protein-120 kD.International journal of molecular sciences · 2016Article
- Phosphatidylinositol 3-Kinase-Associated Protein (PI3KAP)/XB130 Crosslinks Actin Filaments through Its Actin Binding and Multimerization Properties In Vitro and Enhances Endocytosis in HEK293 Cells.Frontiers in endocrinology · 2016Article
- Actin filament-associated protein 1 is required for cSrc activity and secretory activation in the lactating mammary gland.Oncogene · 2015Article
- Article
- Cell fate inclination within 2-cell and 4-cell mouse embryos revealed by single-cell RNA sequencing.Genome research · 2014Article
- Common variants near ABCA1, AFAP1 and GMDS confer risk of primary open-angle glaucoma.Nature genetics · 2014Article
- Junctional adhesion molecules 2 and 3 may potentially be involved in progression of gastric adenocarcinoma tumors.Medical oncology (Northwood, London, England) · 2013Article
- There is more than one way to model an elephant. Experiment-driven modeling of the actin cytoskeleton.Biophysical journal · 2013Review
- 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
- 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
- Perfluorooctane sulfonate (PFOS) induces reactive oxygen species (ROS) production in human microvascular endothelial cells: role in endothelial permeability.Journal of toxicology and environmental health. Part A · 2010Article
- Amplification of transducer gain by angiotensin II-mediated enhancement of cortical actin density in osmosensory neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2008Article
- AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts.The Journal of clinical investigation · 2007Article
- Myosin heavy-chain kinase A from Dictyostelium possesses a novel actin-binding domain that cross-links actin filaments.The Biochemical journal · 2006Article
- Protein kinase Calpha activates c-Src and induces podosome formation via AFAP-110.Molecular and cellular biology · 2004Article
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 1 country.
Funding
Abstract
The actin filament-associated protein and Src-binding partner, AFAP-110, is an adaptor protein that links signaling molecules to actin filaments. AFAP-110 binds actin filaments directly and multimerizes through a leucine zipper motif. Cellular signals downstream of Src(527F) can regulate multimerization. Here, we determined recombinant AFAP-110 (rAFAP-110)-bound actin filaments cooperatively, through a lateral association. We demonstrate rAFAP-110 has the capability to cross-link actin filaments, and this ability is dependent on the integrity of the carboxy terminal actin binding domain. Deletion of the leucine zipper motif or PKC phosphorylation affected AFAP-110's conformation, which correlated with changes in multimerization and increased the capability of rAFAP-110 to cross-link actin filaments. AFAP-110 is both a substrate and binding partner of PKC. On PKC activation, stress filament organization is lost, motility structures form, and AFAP-110 colocalizes strongly with motility structures. Expression of a deletion mutant of AFAP-110 that is unable to bind PKC blocked the effect of PMA on actin filaments. We hypothesize that upon PKC activation, AFAP-110 can be cooperatively recruited to newly forming actin filaments, like those that exist in cell motility structures, and that PKC phosphorylation effects a conformational change that may enable AFAP-110 to promote actin filament cross-linking at the cell membrane.
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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 Socratic graph.