PLK2
PLK2 (polo like kinase 2, also known as SNK) is a serine/threonine-protein kinase of the polo-like kinase family. It acts as a tumour suppressor and is involved in synaptic plasticity, centriole duplication and the G1/S phase transition. Browse Assay Genie's current range of PLK2 research reagents below, or read on for the biology behind the target.
PLK2 is a tumour suppressor serine/threonine-protein kinase. Polo-like kinases act by binding and phosphorylating proteins that are already phosphorylated on a specific motif recognised by the POLO box domains. In cell division, PLK2 is required for procentriole formation and centriole duplication, phosphorylating CPAP and NPM1 respectively. Its induction by p53/TP53 suggests that it may participate in the mitotic checkpoint following stress.
In neurons, PLK2 plays a key role in synaptic plasticity and memory by regulating Ras and Rap protein signalling. It is required for overactivity-dependent spine remodelling: phosphorylation of the Ras activator RASGRF1 and the Rap inhibitor SIPA1L1 leads to their degradation by the proteasome. Conversely, it phosphorylates the Rap activator RAPGEF2 and the Ras inhibitor SYNGAP1, promoting their activity. Further reported substrates include SNCA. PLK2 also regulates synaptic plasticity independently of kinase activity, through an interaction with NSF that disrupts the NSF interaction with the GRIA2 subunit of AMPA receptors. This causes a rapid rundown of AMPAR-mediated current that occludes long term depression.
The PLK2 gene encodes a member of the polo family of kinases, which belongs to the CDC5/Polo subfamily of the protein kinase superfamily. It is most abundantly expressed in testis, spleen and foetal tissues, and its expression is inducible by serum, suggesting a role in cells undergoing rapid division. Alternatively spliced transcript variants encoding different isoforms have been described. Earlier names include polo-like kinase 2 (Drosophila) and the alias SNK. Mouse and rat orthologues are both designated Plk2; PLK1 is another member of the family.
PLK2 phosphorylates CPAP and NPM1 to support procentriole formation and centriole duplication, and contributes to the G1/S phase transition.
PLK2 regulates Ras and Rap signalling and spine remodelling, and modulates AMPAR-mediated current through NSF, linking it to plasticity and memory.
Induction of PLK2 by p53/TP53 suggests participation in the mitotic checkpoint following stress, making it relevant to tumour suppression studies.
PLK2 phosphorylates substrates including CPAP, NPM1, RAPGEF2, RASGRF1, SNCA, SIPA1L1 and SYNGAP1, providing a model for POLO box-directed phosphorylation.
PLK2 is a tumour suppressor serine/threonine kinase involved in centriole duplication, the G1/S transition and synaptic plasticity. It phosphorylates CPAP and NPM1 during centriole duplication, and substrates such as RASGRF1, SIPA1L1, RAPGEF2 and SYNGAP1 to regulate Ras and Rap signalling in neurons.
Yes. The HGNC-approved name is polo like kinase 2, and the alias SNK is also used. Previous names include polo-like kinase 2 (Drosophila). UniProt lists the protein as serine/threonine-protein kinase PLK2. Alternatively spliced transcript variants encoding different isoforms have been reported for the gene.
Mouse and rat both have a Plk2 orthologue; check the datasheet of any product for its validated reactivity. PLK2 expression is induced by p53/TP53, which suggests it may take part in the mitotic checkpoint after stress, consistent with its tumour suppressor annotation.
Other polo-like kinase family members with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q9NYY3; product specifications from Assay Genie datasheets.