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Title: Glycogen synthase kinase-3 beta, or a link between amyloid and tau pathology?
Authors: Muyllaert, David ×
Kremer, Anna Magdalena
Jaworski, Tomasz
Borghgraef, P
Devijver, H
Croes, S
Dewachter, Ilse
Van Leuven, Freddy #
Issue Date: Feb-2008
Publisher: Blackwell publishing
Series Title: Genes brain and behavior vol:7 pages:57-66
Abstract: Phosphorylation is the most common post-translational modification of cellular proteins, essential for most physiological functions. Deregulation of phosphorylation has been invoked in disease mechanisms, and the case of Alzheimer's disease (AD) is no exception: both in the amyloid pathology and in the tauopathy are kinases deeply implicated. The glycogen synthase kinase-3 (GSK-3) isozymes participate in diverse cellular processes and important signalling pathways and have been implicitly linked to diverse medical problems, i. e. from diabetes and cancer to mood disorders and schizophrenia, and in the neurodegeneration of AD. Here, we review specific aspects of GSK-3 isozymes in the framework of recent data that we obtained in novel transgenic mouse models that robustly recapitulate the pathology and mechanistical problems of AD. Phosphorylation is the most common post-translational modification of cellular proteins, essential for most physiological functions. Deregulation of phosphorylation has been invoked in disease mechanisms, and the case of Alzheimer's disease (AD) is no exception: both in the amyloid pathology and in the tauopathy are kinases deeply implicated. The glycogen synthase kinase-3 (GSK-3) isozymes participate in diverse cellular processes and important signalling pathways and have been implicitly linked to diverse medical problems, i.e. from diabetes and cancer to mood disorders and schizophrenia, and in the neurodegeneration of AD. Here, we review specific aspects of GSK-3 isozymes in the framework of recent data that we obtained in novel transgenic mouse models that robustly recapitulate the pathology and mechanistical problems of AD.
ISSN: 1601-1848
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Laboratory of Experimental Genetics and Transgenesis (-)
Associated Laboratories - miscellaneous (-)
Department of Human Genetics - miscellaneous
× corresponding author
# (joint) last author

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