ArticleNeuroscience2012
Identification and functional characterization of polo-like kinase 2 autoregulatory sites.
Article in Neuroscience, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- DYRK1A and Parkinson's disease, facts and hypotheses.Neurobiology of disease · 2026Review
- Polo-like kinase 2 targeting as novel strategy to sensitize mutant p53-expressing tumor cells to anticancer treatments.Journal of molecular medicine (Berlin, Germany) · 2024Article
- DYRK1A-mediated PLK2 phosphorylation regulates the proliferation and invasion of glioblastoma cells.International journal of oncology · 2023Article
- Polo-Like Kinase 2: From Principle to Practice.Frontiers in oncology · 2022Review
- Dissecting the Molecular Pathway Involved in PLK2 Kinase-mediated α-Synuclein-selective Autophagic Degradation.The Journal of biological chemistry · 2017Article
- Polo Kinase Phosphorylates Miro to Control ER-Mitochondria Contact Sites and Mitochondrial Ca(2+) Homeostasis in Neural Stem Cell Development.Developmental cell · 2016Article
- Polo-like kinases: structural variations lead to multiple functions.Nature reviews. Molecular cell biology · 2014Review
- Parkinson's disease-implicated kinases in the brain; insights into disease pathogenesis.Frontiers in molecular neuroscience · 2014Review
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Polo family kinases play important roles in cellular proliferation as well as neuronal synaptic plasticity. However, the posttranslational regulation of these kinases is not fully understood. Here, we identified several novel Plk2 phosphorylation sites stimulated by Plk2 itself. By site-directed mutagenesis, we uncovered three additional hyperactivating Plk2 mutations as well as a series of residues regulating Plk2 steady-state expression level. Because of the established role of Plk2 in homeostatic negative control of excitatory synaptic strength, these phosphorylation sites could play an important role in the rapid activation, expansion, and prolongation of Plk2 signaling in this process.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.