Anti-MARK1

MAP/microtubule affinity-regulating kinase 1 (MARK1) is a 795 amino acid protein belonging to the CAMK Ser/Thr protein kinase family. MARK1 is thought to play a role in the stability of the microtubule matrix of the cytoskeleton. MARK1 is activated by phosphorylation of Thr215 by LKB1 in complex with STRAD and MO25. Localized to the cytoskeleton, MARK1 contains one kinase-associated (KA1) domain, one protein kinase domain and one UBA domain. Expressed as three isoforms produced by alternative splicing, MARK1 is found with highest levels in brain, skeletal muscle and heart. Protein function: Serine/threonine-protein kinase involved in cell polarity and microtubule dynamics regulation. Phosphorylates DCX, MAP2, MAP4 and MAPT/TAU. Involved in cell polarity by phosphorylating the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules, and their disassembly. Involved in the regulation of neuronal migration through its dual activities in regulating cellular polarity and microtubule dynamics, possibly by phosphorylating and regulating DCX. Also acts as a positive regulator of the Wnt signaling pathway, probably by mediating phosphorylation of dishevelled proteins (DVL1, DVL2 and/or DVL3). [The UniProt Consortium]