DCLK2
DCLK2 (doublecortin like kinase 2, also known as DCAMKL2, DCK2, DCDC3 and DCDC3B) is a serine/threonine protein kinase of the doublecortin superfamily. It combines microtubule-binding doublecortin domains with a CaMK-related kinase domain and is found in the cytoskeleton. Browse Assay Genie's current range of DCLK2 research reagents below, or read on for the biology behind the target.
DCLK2 is a protein kinase with a significantly reduced Ca2+/calmodulin affinity and dependence compared with other members of the CaMK family. It may help down-regulate CRE-dependent gene activation, probably by phosphorylating the CREB coactivator CRTC2 (also called TORC2). This phosphorylation is thought to retain TORC2 in the cytoplasm.
The DCLK2 gene encodes a member of the protein kinase superfamily and the doublecortin family. The protein has two N-terminal doublecortin domains, which bind microtubules and regulate microtubule polymerisation. Its C-terminal serine/threonine kinase domain is substantially homologous to Ca2+/calmodulin-dependent protein kinase. Between them lies a serine/proline-rich domain that mediates multiple protein-protein interactions. The microtubule-polymerising activity of the DCLK2 protein is independent of its kinase activity. UniProt places it in the CAMK Ser/Thr protein kinase family, CaMK subfamily, and its subcellular location is the cytoplasm and cytoskeleton. Multiple alternatively spliced transcript variants have been identified.
HGNC classifies DCLK2 in the doublecortin superfamily and the doublecortin like kinase family, alongside DCLK1. Earlier names include doublecortin and CaM kinase-like 2 and doublecortin-like kinase 2. Mouse studies show that the DCX gene, another family member, and this gene share a function in establishing hippocampal organisation. Their absence causes a severe epileptic phenotype and lethality, as described in human patients with lissencephaly. Orthologues are named Dclk2 in both mouse and rat.
The doublecortin domains of DCLK2 bind microtubules and regulate their polymerisation, independently of kinase activity, making it a subject for cytoskeletal studies.
DCLK2 may down-regulate CRE-dependent gene activation, probably by phosphorylating CRTC2/TORC2 and retaining it in the cytoplasm.
In mice, DCLK2 and DCX share a role in establishing hippocampal organisation, so DCLK2 is relevant to neurodevelopmental research.
Loss of Dclk2 together with Dcx in mice causes severe epilepsy and lethality, resembling human lissencephaly.
DCLK2 is a serine/threonine kinase with two doublecortin domains that bind microtubules and regulate their polymerisation. This activity is independent of its kinase function. It may also down-regulate CRE-dependent gene activation, probably by phosphorylating CRTC2/TORC2 and retaining it in the cytoplasm.
DCLK2 is also known as DCAMKL2, DCK2, DCDC3, DCDC3B and MGC45428. Previous names are doublecortin and CaM kinase-like 2 and doublecortin-like kinase 2. UniProt lists the protein as serine/threonine-protein kinase DCLK2. Multiple alternatively spliced transcript variants have been reported.
Mouse and rat both carry a Dclk2 orthologue; check the datasheet of any product for its validated reactivity. In mice, loss of Dclk2 together with Dcx disrupts hippocampal organisation and causes severe epilepsy and lethality, as seen in human lissencephaly.
Other members of the doublecortin like kinase family with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q8N568; product specifications from Assay Genie datasheets.