ArticleCell motility and the cytoskeleton2009
The actin-binding domain of cortactin is dynamic and unstructured and affects lateral and longitudinal contacts in F-actin.
Article in Cell motility and the cytoskeleton, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 27 citations in OpenAlex.
- Loss of p190A RhoGAP induces aneuploidy and enhances bladder cancer cell migration and invasion by modulating actin dynamics.Scientific reports · 2025Article
- Desmoglein-driven dynamic signaling in pemphigus vulgaris: a systematic review of pathogenic pathways.NPJ Regenerative medicine · 2025Article
- Cortactin stabilization of actin requires actin-binding repeats and linker, is disrupted by specific substitutions, and is independent of nucleotide state.The Journal of biological chemistry · 2018Article
- Cortical Actin Dynamics in Endothelial Permeability.Current topics in membranes · 2018Article
- The repeat region of cortactin is intrinsically disordered in solution.Scientific reports · 2017Article
- Cortactin in cancer cell migration and invasion.Oncotarget · 2017Review
- Pathogenicity-associated protein domains: The fiercely-conserved evolutionary signatures.Gene reports · 2017Review
- p27eLife · 2017Article
- Interactions with actin monomers, actin filaments, and Arp2/3 complex define the roles of WASP family proteins and cortactin in coordinately regulating branched actin networks.The Journal of biological chemistry · 2014Article
- Article
- Src binds cortactin through an SH2 domain cystine-mediated linkage.Journal of cell science · 2012Article
- Cortactin in cell migration and cancer at a glance.Journal of cell science · 2012Review
- Juxtanodin is an intrinsically disordered F-actin-binding protein.Scientific reports · 2012Article
- Arabidopsis Actin-Depolymerizing Factor-4 links pathogen perception, defense activation and transcription to cytoskeletal dynamics.PLoS pathogens · 2012Article
- Cortactin: a multifunctional regulator of cellular invasiveness.Cell adhesion & migrationReview
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Cortactin is an F-actin- and Arp2/3 complex-binding protein, implicated in the regulation of cytoskeleton dynamics and cortical actin-assembly. The actin-binding domain of cortactin consists of a 6.5 tandem repeat of a 37-amino acid sequence known as the cortactin repeat (residues 80-325). Using a combination of structure prediction, circular dichroism, and cysteine crosslinking, we tested a recently published three-dimensional model of the cortactin molecule in which the cortactin repeat is folded as a globular helical domain [Zhang et al., 2007, Mol Cell 27:197-213]. We show that the cortactin repeat is unstructured in solution. Thus, wild type and mutant constructs of the cortactin repeat, containing pairs of cysteines at positions 112 and 246, 83 and 112, 83 and 246, and 83 and 306, could be readily crosslinked with reagents of varying lengths (0-9.6 A). Using yeast actin cysteine mutants, we also show that cortactin inhibits disulfide and dibromobimane crosslinking across the lateral and longitudinal interfaces of actin subunits in the filament, suggesting a weakening of intersubunits contacts. Our results are in disagreement with the proposed model of the cortactin molecule and have important implications for our understanding of cortactin regulation of cytoskeleton dynamics.
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