The tau of MARK: a polarized view of the cytoskeleton.
Microtubule-affinity regulating kinases (MARKs) were originally discovered by their ability to phosphorylate tau protein and related microtubule-associated proteins (MAPs), and thereby to regulate microtubule dynamics in neurons. Members of the MARK (also known as partition-defective [Par]-1 kinase) family were subsequently found to be highly conserved and to have key roles in cell processes such as determination of polarity, cell-cycle control, intracellular signal transduction, transport and cytoskeleton. This is important for neuronal differentiation, but is also prominent in neurodegenerative 'tauopathies' such as Alzheimer's disease. The identified functions of MARK/Par-1 are diverse and require accurate regulation. Recent discoveries including the x-ray structure of human MARKs contributed to an increased understanding of the mechanisms that control the kinase activity and, thus, the actin and microtubule cytoskeleton.
Matenia
Dorthe
D
Max-Planck-Unit for Structural Molecular Biology, Hamburg, Germany. matenia@mpasmb.desy.de
Mandelkow
Eva-Maria
EM
D000818:Animals; D016764:Cell Polarity / Q000502:physiology; D003599:Cytoskeleton / Q000378:metabolism*; D006801:Humans; D009474:Neurons / Q000378:metabolism / Q000648:ultrastructure; D010766:Phosphorylation / Q000502:physiology; D047428:Protein Kinase Inhibitors; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D024801:Tauopathies / Q000473:pathology; D016875:tau Proteins / Q000378:metabolism*
D047428:Protein Kinase Inhibitors; D016875:tau Proteins; D017346:Protein Serine-Threonine Kinases