ArticleScientific reports2017
Structural characterization of CAS SH3 domain selectivity and regulation reveals new CAS interaction partners.
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 9 papers.
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Who cites it
9 citing papers in PubMed.
- Dissecting the propensity of RIM1 subdomains to form phase condensates.Scientific reports · 2026Article
- Use of phosphotyrosine-containing peptides to target SH2 domains: Antagonist peptides of the Crk/CrkL-p130Cas axis.Methods in enzymology · 2024Article
- Phosphorylation of tyrosine 90 in SH3 domain is a new regulatory switch controlling Src kinase.eLife · 2023Article
- The TFIIS N-terminal domain (TND): a transcription assembly module at the interface of order and disorder.Biochemical Society transactions · 2023Review
- A germline SNP in BRMS1 predisposes patients with lung adenocarcinoma to metastasis and can be ameliorated by targeting c-fos.Science translational medicine · 2022Article
- Structural determinants for subnanomolar inhibition of the secreted aspartic protease Sapp1p fromJournal of enzyme inhibition and medicinal chemistry · 2021Article
- A Screen for PKN3 Substrates Reveals an Activating Phosphorylation of ARHGAP18.International journal of molecular sciences · 2020Article
- The interaction of p130Cas with PKN3 promotes malignant growth.Molecular oncology · 2019Article
- PTPN12/PTP-PEST Regulates Phosphorylation-Dependent Ubiquitination and Stability of Focal Adhesion Substrates in Invasive Glioblastoma Cells.Cancer research · 2018Article
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Authors and funding
9 authors.
Funding
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Abstract
CAS is a docking protein downstream of the proto-oncogene Src with a role in invasion and metastasis of cancer cells. The CAS SH3 domain is indispensable for CAS-mediated signaling, but structural aspects of CAS SH3 ligand binding and regulation are not well understood. Here, we identified the consensus CAS SH3 binding motif and structurally characterized the CAS SH3 domain in complex with ligand. We revealed the requirement for an uncommon centrally localized lysine residue at position +2 of CAS SH3 ligands and two rather dissimilar optional anchoring residues, leucine and arginine, at position +5. We further expanded the knowledge of CAS SH3 ligand binding regulation by manipulating tyrosine 12 phosphorylation and confirmed the negative role of this phosphorylation on CAS SH3 ligand binding. Finally, by exploiting the newly identified binding requirements of the CAS SH3 domain, we predicted and experimentally verified two novel CAS SH3 binding partners, DOK7 and GLIS2.
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