title: Structure and regulation of MARK, a kinase involved in abnormal phosphorylation of Tau protein.
abstract: Protein kinases of the MARK family phosphorylate tau protein in its repeat domain and thereby regulate its affinity for microtubules and affect the aggregation of tau into Alzheimer paired helical filaments. We are searching for low molecular weight compounds to interfere with the activity of MARK and its pathways. Here we summarize structural features of MARK and cellular pathways of regulation.
authors.affiliation: Max-Planck-Unit for Structural Molecular Biology, c/o DESY, Notkestrasse 85, Hamburg, Germany. timm@mpasmb.desy.de
authors.forename: Thomas
authors.initials: T
authors.lastname: Timm
authors.forename: Alexander
authors.initials: A
authors.lastname: Marx
authors.forename: Saravanan
authors.initials: S
authors.lastname: Panneerselvam
authors.forename: Eckhard
authors.initials: E
authors.lastname: Mandelkow
authors.forename: Eva-Maria
authors.initials: EM
authors.lastname: Mandelkow
mesh_terms: D000544:Alzheimer Disease / Q000201:enzymology* / Q000378:metabolism; D000818:Animals; D020134:Catalytic Domain; D006801:Humans; D008958:Models, Molecular; D010766:Phosphorylation; D011487:Protein Conformation; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry / Q000378:metabolism*; D015398:Signal Transduction; D016875:tau Proteins / Q000378:metabolism*
chemical_list: D016875:tau Proteins; C105547:MARK1 protein, human; D017346:Protein Serine-Threonine Kinases