The Importance of Tau Phosphorylation for Neurodegenerative Diseases

Fibrillar deposits of highly phosphorylated tau are a key pathological feature of several neurodegenerative tauopathies including Alzheimer’s disease (AD) and some frontotemporal dementias. Increasing evidence suggests that the presence of these end-stage neurofibrillary lesions do not cause neurona...

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Main Authors:	Noble, Wendy, Hanger, Diane P., Miller, Christopher C. J., Lovestone, Simon
Format:	Online
Language:	English
Published:	Frontiers Media S.A. 2013
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3696910/

id	pubmed-3696910
recordtype	oai_dc
spelling	pubmed-36969102013-07-11 The Importance of Tau Phosphorylation for Neurodegenerative Diseases Noble, Wendy Hanger, Diane P. Miller, Christopher C. J. Lovestone, Simon Neuroscience Fibrillar deposits of highly phosphorylated tau are a key pathological feature of several neurodegenerative tauopathies including Alzheimer’s disease (AD) and some frontotemporal dementias. Increasing evidence suggests that the presence of these end-stage neurofibrillary lesions do not cause neuronal loss, but rather that alterations to soluble tau proteins induce neurodegeneration. In particular, aberrant tau phosphorylation is acknowledged to be a key disease process, influencing tau structure, distribution, and function in neurons. Although typically described as a cytosolic protein that associates with microtubules and regulates axonal transport, several additional functions of tau have recently been demonstrated, including roles in DNA stabilization, and synaptic function. Most recently, studies examining the trans-synaptic spread of tau pathology in disease models have suggested a potential role for extracellular tau in cell signaling pathways intrinsic to neurodegeneration. Here we review the evidence showing that tau phosphorylation plays a key role in neurodegenerative tauopathies. We also comment on the tractability of altering phosphorylation-dependent tau functions for therapeutic intervention in AD and related disorders. Frontiers Media S.A. 2013-07-01 /pmc/articles/PMC3696910/ /pubmed/23847585 http://dx.doi.org/10.3389/fneur.2013.00083 Text en Copyright © 2013 Noble, Hanger, Miller and Lovestone. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in other forums, provided the original authors and source are credited and subject to any copyright notices concerning any third-party graphics etc.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Noble, Wendy Hanger, Diane P. Miller, Christopher C. J. Lovestone, Simon
spellingShingle	Noble, Wendy Hanger, Diane P. Miller, Christopher C. J. Lovestone, Simon The Importance of Tau Phosphorylation for Neurodegenerative Diseases
author_facet	Noble, Wendy Hanger, Diane P. Miller, Christopher C. J. Lovestone, Simon
author_sort	Noble, Wendy
title	The Importance of Tau Phosphorylation for Neurodegenerative Diseases
title_short	The Importance of Tau Phosphorylation for Neurodegenerative Diseases
title_full	The Importance of Tau Phosphorylation for Neurodegenerative Diseases
title_fullStr	The Importance of Tau Phosphorylation for Neurodegenerative Diseases
title_full_unstemmed	The Importance of Tau Phosphorylation for Neurodegenerative Diseases
title_sort	importance of tau phosphorylation for neurodegenerative diseases
description	Fibrillar deposits of highly phosphorylated tau are a key pathological feature of several neurodegenerative tauopathies including Alzheimer’s disease (AD) and some frontotemporal dementias. Increasing evidence suggests that the presence of these end-stage neurofibrillary lesions do not cause neuronal loss, but rather that alterations to soluble tau proteins induce neurodegeneration. In particular, aberrant tau phosphorylation is acknowledged to be a key disease process, influencing tau structure, distribution, and function in neurons. Although typically described as a cytosolic protein that associates with microtubules and regulates axonal transport, several additional functions of tau have recently been demonstrated, including roles in DNA stabilization, and synaptic function. Most recently, studies examining the trans-synaptic spread of tau pathology in disease models have suggested a potential role for extracellular tau in cell signaling pathways intrinsic to neurodegeneration. Here we review the evidence showing that tau phosphorylation plays a key role in neurodegenerative tauopathies. We also comment on the tractability of altering phosphorylation-dependent tau functions for therapeutic intervention in AD and related disorders.
publisher	Frontiers Media S.A.
publishDate	2013
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3696910/
_version_	1611990636168216576

The Importance of Tau Phosphorylation for Neurodegenerative Diseases

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