ArticleScientific reports2017
The repeat region of cortactin is intrinsically disordered in solution.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Intrinsic Disorder in Tetratricopeptide Repeat Proteins.International journal of molecular sciences · 2020Article
- Predicting Conformational Properties of Intrinsically Disordered Proteins from Sequence.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Cortactin in Epithelial-Mesenchymal Transition.Frontiers in cell and developmental biology · 2020Review
- Chasing Tails: Cathepsin-L Improves Structural Analysis of Histones by HX-MS.Molecular & cellular proteomics : MCP · 2019Article
- Acetylation of intrinsically disordered regions regulates phase separation.Nature chemical biology · 2019Article
- 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
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Authors and funding
8 authors.
Funding
Abstract
The multi-domain protein, cortactin, contains a 37-residue repeating motif that binds to actin filaments. This cortactin repeat region comprises 6½ similar copies of the motif and binds actin filaments. To better understand this region of cortactin, and its fold, we conducted extensive biophysical analysis. Size exclusion chromatography with multi-angle light scattering (SEC-MALS) reveals that neither constructs of the cortactin repeats alone or together with the adjacent helical region homo-oligomerize. Using circular dichroism (CD) we find that in solution the cortactin repeats resemble a coil-like intrinsically disordered protein. Small-angle X-ray scattering (SAXS) also indicates that the cortactin repeats are intrinsically unfolded, and the experimentally observed radius of gyration (R
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