Recombinant Mouse Serine/threonine-protein kinase PLK2 (Plk2) Protein

Function

Tumor suppressor serine/threonine-protein kinase involved in synaptic plasticity, centriole duplication and G1/S phase transition. Polo-like kinases act by binding and phosphorylating proteins that are already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates CPAP, NPM1, RAPGEF2, RASGRF1, SNCA, SIPA1L1 and SYNGAP1. Plays a key role in synaptic plasticity and memory by regulating the Ras and Rap protein signaling: required for overactivity-dependent spine remodeling by phosphorylating the Ras activator RASGRF1 and the Rap inhibitor SIPA1L1 leading to their degradation by the proteasome. Conversely, phosphorylates the Rap activator RAPGEF2 and the Ras inhibitor SYNGAP1, promoting their activity. Also regulates synaptic plasticity independently of kinase activity, via its interaction with NSF that disrupts the interaction between NSF and the GRIA2 subunit of AMPARs, leading to a rapid rundown of AMPAR-mediated current that occludes long term depression. Required for procentriole formation and centriole duplication by phosphorylating CPAP and NPM1, respectively. Its induction by p53/TP53 suggests that it may participate in the mitotic checkpoint following stress

Subcellular Location

Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole; Cell projection, dendrite

Tissue Specificity

Brain, lung and heart

Subunit

Interacts with NSF; causing NSF dissociation from GRIA2 (By similarity). Interacts with CIB1

• Simmons D.L. et al. Identification of an early-growth-response gene encoding a novel putative protein kinase. — Mol. Cell. Biol. (1992)
• Ma S. et al. The serum-inducible protein kinase Snk is a G1 phase polo-like kinase that is inhibited by the calcium- and integrin-binding protein CIB. — Mol. Cancer Res. (2003)
• Burns T.F. et al. Silencing of the novel p53 target gene Snk/Plk2 leads to mitotic catastrophe in paclitaxel (taxol)-exposed cells. — Mol. Cell. Biol. (2003)
• Ma S. et al. Role of Plk2 (Snk) in mouse development and cell proliferation. — Mol. Cell. Biol. (2003)
• Inglis K.J. et al. Polo-like kinase 2 (PLK2) phosphorylates alpha-synuclein at serine 129 in central nervous system. — J. Biol. Chem. (2009)
• Lee K.J. et al. Requirement for Plk2 in orchestrated ras and rap signaling, homeostatic structural plasticity, and memory. — Neuron (2011)