ArticleInternational journal of molecular sciences2020
A Screen for PKN3 Substrates Reveals an Activating Phosphorylation of ARHGAP18.
Article in International journal of molecular sciences, 2020. 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, 6 citations in OpenAlex.
- Syntaxin-3 Regulates Tight Junction Assembly in Human Retinal Pigment Epithelium.Cell biochemistry and function · 2026Article
- Selective Inhibitor of Protein Kinase PKN3 Generated by Conjugation of a Structurally Optimized BumpedMolecules (Basel, Switzerland) · 2026Article
- Chemical proteomics reveals the target landscape of 1,000 kinase inhibitors.Nature chemical biology · 2024Article
- Patterning of the cell cortex by Rho GTPases.Nature reviews. Molecular cell biology · 2024Review
- ARHGAP18 is Upregulated by Transcription Factor GATA1 Promotes the Proliferation and Invasion in Hepatocellular Carcinoma.Applied biochemistry and biotechnology · 2024Article
- Protein Kinases: Function, Substrates, and Implication in Diseases.International journal of molecular sciences · 2022Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Protein kinase N3 (PKN3) is a serine/threonine kinase implicated in tumor progression of multiple cancer types, however, its substrates and effector proteins still remain largely understudied. In the present work we aimed to identify novel PKN3 substrates in a phosphoproteomic screen using analog sensitive PKN3. Among the identified putative substrates we selected ARHGAP18, a protein from RhoGAP family, for validation of the screen and further study. We confirmed that PKN3 can phosphorylate ARHGAP18 in vitro and we also characterized the interaction of the two proteins, which is mediated via the
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Registered trials
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