ArticleCell cycle (Georgetown, Tex.)2013
CUL3 and protein kinases: insights from PLK1/KLHL22 interaction.
Article in Cell cycle (Georgetown, Tex.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 21 citations in OpenAlex.
- EHMT2-mediated R-loop formation promotes the malignant progression of prostate cancer via activating Aurora B.Clinical and translational medicine · 2025Article
- Non-proteolytic ubiquitylation in cellular signaling and human disease.Communications biology · 2022Review
- The roles of KLHL family members in human cancers.American journal of cancer research · 2022Review
- Genome-wide association study reveals novel loci for adult type 1 diabetes in a 5-year nested case-control study.World journal of diabetes · 2021Article
- KLHL5 Is a Prognostic-Related Biomarker and Correlated With Immune Infiltrates in Gastric Cancer.Frontiers in molecular biosciences · 2020Article
- In the line-up: deleted genes associated with DiGeorge/22q11.2 deletion syndrome: are they all suspects?Journal of neurodevelopmental disorders · 2019Review
- Chlorogenic acid effectively treats cancers through induction of cancer cell differentiation.Theranostics · 2019Article
- KLHL5 knockdown increases cellular sensitivity to anticancer drugs.Oncotarget · 2018Article
- Cotargeting HSP90 and Its Client Proteins for Treatment of Prostate Cancer.Molecular cancer therapeutics · 2016Article
- Cullin3-KLHL15 ubiquitin ligase mediates CtIP protein turnover to fine-tune DNA-end resection.Nature communications · 2016Article
- Novel mutations in WWOX, RARS2, and C10orf2 genes in consanguineous Arab families with intellectual disability.Metabolic brain disease · 2016Article
- Tumour suppressor TRIM33 targets nuclear β-catenin degradation.Nature communications · 2015Article
- Kelch proteins: emerging roles in skeletal muscle development and diseases.Skeletal muscle · 2014Review
- Molecular dynamics of PLK1 during mitosis.Molecular & cellular oncologyReview
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Posttranslational mechanisms drive fidelity of cellular processes. Phosphorylation and ubiquitination of substrates represent very common, covalent, posttranslational modifications and are often co-regulated. Phosphorylation may play a critical role both by directly regulating E3-ubiquitin ligases and/or by ensuring specificity of the ubiquitination substrate. Importantly, many kinases are not only critical regulatory components of these pathways but also represent themselves the direct ubiquitination substrates. Recent data suggest the role of CUL3-based ligases in both proteolytic and non-proteolytic regulation of protein kinases. Our own recent study identified the mitotic kinase PLK1 as a direct target of the CUL3 E3-ligase complex containing BTB-KELCH adaptor protein KLHL22. (1) In this study, we aim at gaining mechanistic insights into CUL3-mediated regulation of the substrates, in particular protein kinases, by analyzing mechanisms of interaction between KLHL22 and PLK1. We find that kinase activity of PLK1 is redundant for its targeting for CUL3-ubiquitination. Moreover, CUL3/KLHL22 may contact 2 distinct motifs within PLK1 protein, consistent with the bivalent mode of substrate targeting found in other CUL3-based complexes. We discuss these findings in the context of the existing knowledge on other protein kinases and substrates targeted by CUL3-based E3-ligases.
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