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This article is part of the supplement: Proceedings of the 8th International Conference on Alzheimer's Disease Drug Discovery

Open Access Review

Structure and regulation of MARK, a kinase involved in abnormal phosphorylation of Tau protein

Thomas Timm, Alexander Marx, Saravanan Panneerselvam, Eckhard Mandelkow and Eva-Maria Mandelkow*

Author affiliations

Max-Planck-Unit for Structural Molecular Biology, c/o DESY, Notkestrasse 85, 22607 Hamburg, Germany

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Citation and License

BMC Neuroscience 2008, 9(Suppl 2):S9  doi:10.1186/1471-2202-9-S2-S9

Published: 3 December 2008

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.