Tau protein modifications and interactions: their role in function and dysfunction

Tau protein modifications and interactions: their role in function and dysfunction

Tau protein is abundant in the central nervous system and involved in microtubule assembly and stabilization. It is predominantly associated with axonal microtubules and present at lower level in dendrites where it is engaged in signaling functions. Post-translational modifications of tau and its in...

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Bibliographic Details
Published in:International journal of molecular sciences Vol. 15; no. 3; pp. 4671 - 4713
Main Authors: Mietelska-Porowska, Anna, Wasik, Urszula, Goras, Marcelina, Filipek, Anna, Niewiadomska, Grazyna
Format: Journal Article
Language:English
Published: Switzerland MDPI AG 18-03-2014
Molecular Diversity Preservation International (MDPI)
Subjects:
Cytoskeleton
Cytoskeleton - metabolism
Dementia - metabolism
Humans
Kinases
microtubule
Microtubules - metabolism
Models, Biological
Nervous system
Neurodegeneration
neurodegenerative disorders
Neurons - metabolism
Neurons - pathology
neurotrophic support
Protein Binding
Protein expression
Protein Processing, Post-Translational
Proteins
Review
Signal transduction
tau interacting proteins
tau kinases and phosphatases
tau protein
tau Proteins - metabolism
Tauopathies - metabolism
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Summary:Tau protein is abundant in the central nervous system and involved in microtubule assembly and stabilization. It is predominantly associated with axonal microtubules and present at lower level in dendrites where it is engaged in signaling functions. Post-translational modifications of tau and its interaction with several proteins play an important regulatory role in the physiology of tau. As a consequence of abnormal modifications and expression, tau is redistributed from neuronal processes to the soma and forms toxic oligomers or aggregated deposits. The accumulation of tau protein is increasingly recognized as the neuropathological hallmark of a number of dementia disorders known as tauopathies. Dysfunction of tau protein may contribute to collapse of cytoskeleton, thereby causing improper anterograde and retrograde movement of motor proteins and their cargos on microtubules. These disturbances in intraneuronal signaling may compromise synaptic transmission as well as trophic support mechanisms in neurons.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms15034671