The interaction of α-synuclein and Tau: A molecular conspiracy in neurodegeneration?

Tutkimustuotos: ArtikkelijulkaisuArtikkeliTieteellinenvertaisarvioitu

Kuvaus

α-synuclein and Tau are proteins prone to pathological misfolding and aggregation that are normally found in the presynaptic and axonal compartments of neurons. Misfolding initiates a homo-oligomerization and aggregation cascade culminating in cerebral accumulation of aggregated α-synuclein and Tau in insoluble protein inclusions in multiple neurodegenerative diseases. Traditionally, α-synuclein-containing Lewy bodies have been associated with Parkinson’s disease and Tau-containing neurofibrillary tangles with Alzheimer’s disease and various frontotemporal dementia syndromes. However, there is significant overlap and co-occurrence of α-synuclein and Tau pathologies in a spectrum of neurodegenerative diseases. Importantly, α-synuclein and Tau can interact in cells, and their pathological conformations are capable of templating further misfolding and aggregation of each other. They also share a number of protein interactors indicating that network perturbations may contribute to chronic proteotoxic stress and neuronal dysfunction in synucleinopathies and tauopathies, some of which share similarities in both neuropathological and clinical manifestations. In this review, we focus on the protein interactions of these two pathologically important proteins and consider a network biology perspective towards neurodegenerative diseases.
Alkuperäiskielienglanti
LehtiSeminars in Cell and Developmental Biology
ISSN1084-9521
DOI - pysyväislinkit
TilaE-pub ahead of print - 10 toukokuuta 2018
OKM-julkaisutyyppiA1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä, vertaisarvioitu

Tieteenalat

  • 3112 Neurotieteet

Lainaa tätä

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title = "The interaction of α-synuclein and Tau: A molecular conspiracy in neurodegeneration?",
abstract = "α-synuclein and Tau are proteins prone to pathological misfolding and aggregation that are normally found in the presynaptic and axonal compartments of neurons. Misfolding initiates a homo-oligomerization and aggregation cascade culminating in cerebral accumulation of aggregated α-synuclein and Tau in insoluble protein inclusions in multiple neurodegenerative diseases. Traditionally, α-synuclein-containing Lewy bodies have been associated with Parkinson’s disease and Tau-containing neurofibrillary tangles with Alzheimer’s disease and various frontotemporal dementia syndromes. However, there is significant overlap and co-occurrence of α-synuclein and Tau pathologies in a spectrum of neurodegenerative diseases. Importantly, α-synuclein and Tau can interact in cells, and their pathological conformations are capable of templating further misfolding and aggregation of each other. They also share a number of protein interactors indicating that network perturbations may contribute to chronic proteotoxic stress and neuronal dysfunction in synucleinopathies and tauopathies, some of which share similarities in both neuropathological and clinical manifestations. In this review, we focus on the protein interactions of these two pathologically important proteins and consider a network biology perspective towards neurodegenerative diseases.",
keywords = "Neurodegeneration, Network biology, Protein-protein interaction, Pathobiology, Interactome, 3112 Neurosciences",
author = "Xu Yan and Riikka-Liisa Uronen and Huttunen, {Henri J.}",
year = "2018",
month = "5",
day = "10",
doi = "10.1016/j.semcdb.2018.05.005",
language = "English",
journal = "Seminars in Cell and Developmental Biology",
issn = "1084-9521",
publisher = "ACADEMIC PRESS INC ELSEVIER SCIENCE",

}

The interaction of α-synuclein and Tau: A molecular conspiracy in neurodegeneration? / Yan, Xu; Uronen, Riikka-Liisa; Huttunen, Henri J.

julkaisussa: Seminars in Cell and Developmental Biology, 10.05.2018.

Tutkimustuotos: ArtikkelijulkaisuArtikkeliTieteellinenvertaisarvioitu

TY - JOUR

T1 - The interaction of α-synuclein and Tau: A molecular conspiracy in neurodegeneration?

AU - Yan, Xu

AU - Uronen, Riikka-Liisa

AU - Huttunen, Henri J.

PY - 2018/5/10

Y1 - 2018/5/10

N2 - α-synuclein and Tau are proteins prone to pathological misfolding and aggregation that are normally found in the presynaptic and axonal compartments of neurons. Misfolding initiates a homo-oligomerization and aggregation cascade culminating in cerebral accumulation of aggregated α-synuclein and Tau in insoluble protein inclusions in multiple neurodegenerative diseases. Traditionally, α-synuclein-containing Lewy bodies have been associated with Parkinson’s disease and Tau-containing neurofibrillary tangles with Alzheimer’s disease and various frontotemporal dementia syndromes. However, there is significant overlap and co-occurrence of α-synuclein and Tau pathologies in a spectrum of neurodegenerative diseases. Importantly, α-synuclein and Tau can interact in cells, and their pathological conformations are capable of templating further misfolding and aggregation of each other. They also share a number of protein interactors indicating that network perturbations may contribute to chronic proteotoxic stress and neuronal dysfunction in synucleinopathies and tauopathies, some of which share similarities in both neuropathological and clinical manifestations. In this review, we focus on the protein interactions of these two pathologically important proteins and consider a network biology perspective towards neurodegenerative diseases.

AB - α-synuclein and Tau are proteins prone to pathological misfolding and aggregation that are normally found in the presynaptic and axonal compartments of neurons. Misfolding initiates a homo-oligomerization and aggregation cascade culminating in cerebral accumulation of aggregated α-synuclein and Tau in insoluble protein inclusions in multiple neurodegenerative diseases. Traditionally, α-synuclein-containing Lewy bodies have been associated with Parkinson’s disease and Tau-containing neurofibrillary tangles with Alzheimer’s disease and various frontotemporal dementia syndromes. However, there is significant overlap and co-occurrence of α-synuclein and Tau pathologies in a spectrum of neurodegenerative diseases. Importantly, α-synuclein and Tau can interact in cells, and their pathological conformations are capable of templating further misfolding and aggregation of each other. They also share a number of protein interactors indicating that network perturbations may contribute to chronic proteotoxic stress and neuronal dysfunction in synucleinopathies and tauopathies, some of which share similarities in both neuropathological and clinical manifestations. In this review, we focus on the protein interactions of these two pathologically important proteins and consider a network biology perspective towards neurodegenerative diseases.

KW - Neurodegeneration

KW - Network biology

KW - Protein-protein interaction

KW - Pathobiology

KW - Interactome

KW - 3112 Neurosciences

U2 - 10.1016/j.semcdb.2018.05.005

DO - 10.1016/j.semcdb.2018.05.005

M3 - Article

JO - Seminars in Cell and Developmental Biology

JF - Seminars in Cell and Developmental Biology

SN - 1084-9521

ER -