Microtubule affinity-regulating kinase 3 (MARK3)

Microtubule affinity-regulating kinase 3 (MARK3) is a serine/threonine-protein kinase that plays a critical role in regulating microtubule dynamics by phosphorylating microtubule-associated proteins, such as tau, MAP2, and MAP4[1][3]. MARK3 is a member of the MARK/Par-1 family and is central to the control of cell polarity, cell cycle progression (notably mitosis), and the structural organization of the cytoskeleton[1][2][3]. Its activities influence transitions between microtubule- and actin-dominated cellular states to support processes like migration, division, and tissue organization[2]. Dysregulation of MARK3 has been implicated in cancer progression and neurodegenerative diseases, including those involving tau pathology, and specific genetic defects are associated with visual impairment and syndromes such as Peutz-Jeghers[1][3][5]. MARK3 acts via phosphorylation, including of ARHGEF2, thereby affecting RHOA signaling, focal adhesion dynamics, and epithelial organization[2].

Other names

MAP/microtubule affinity-regulating kinase 3CTAK1EMK2cTAK1EMK-2Par-1aKP78PAR-1AC-TAK1Cdc25C-associated protein kinase 1ELKL motif kinase 2Protein kinase STK10Ser/Thr protein kinase PAR-1Serine/threonine-protein kinase p78VIPB

Phosphorylation of microtubule-associated proteins leading to microtubule destabilization and regulation of cell polarity; phosphorylation cascade involvement; regulates Hippo pathway and cytoskeletal switching[1][2][3]