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

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 a...

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Autores principales: Timm, Thomas, Marx, Alexander, Panneerselvam, Saravanan, Mandelkow, Eckhard, Mandelkow, Eva-Maria
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2008
Materias:
Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2604893/
https://www.ncbi.nlm.nih.gov/pubmed/19090997
http://dx.doi.org/10.1186/1471-2202-9-S2-S9
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author Timm, Thomas
Marx, Alexander
Panneerselvam, Saravanan
Mandelkow, Eckhard
Mandelkow, Eva-Maria
author_facet Timm, Thomas
Marx, Alexander
Panneerselvam, Saravanan
Mandelkow, Eckhard
Mandelkow, Eva-Maria
author_sort Timm, Thomas
collection PubMed
description 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.
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spelling pubmed-26048932008-12-18 Structure and regulation of MARK, a kinase involved in abnormal phosphorylation of Tau protein Timm, Thomas Marx, Alexander Panneerselvam, Saravanan Mandelkow, Eckhard Mandelkow, Eva-Maria BMC Neurosci Review 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. BioMed Central 2008-12-03 /pmc/articles/PMC2604893/ /pubmed/19090997 http://dx.doi.org/10.1186/1471-2202-9-S2-S9 Text en Copyright © 2008 Timm et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an open access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review
Timm, Thomas
Marx, Alexander
Panneerselvam, Saravanan
Mandelkow, Eckhard
Mandelkow, Eva-Maria
Structure and regulation of MARK, a kinase involved in abnormal phosphorylation of Tau protein
title Structure and regulation of MARK, a kinase involved in abnormal phosphorylation of Tau protein
title_full Structure and regulation of MARK, a kinase involved in abnormal phosphorylation of Tau protein
title_fullStr Structure and regulation of MARK, a kinase involved in abnormal phosphorylation of Tau protein
title_full_unstemmed Structure and regulation of MARK, a kinase involved in abnormal phosphorylation of Tau protein
title_short Structure and regulation of MARK, a kinase involved in abnormal phosphorylation of Tau protein
title_sort structure and regulation of mark, a kinase involved in abnormal phosphorylation of tau protein
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2604893/
https://www.ncbi.nlm.nih.gov/pubmed/19090997
http://dx.doi.org/10.1186/1471-2202-9-S2-S9
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