Truncated tau disrupts autophagy and endolysosomal systems

Maria Jimenez Sanchez; Wendy Noble; Diane Hanger; Saskia Pollack

doi:10.1080/27694127.2024.2409563

Truncated tau disrupts autophagy and endolysosomal systems

Maria Jimenez Sanchez^*, Wendy Noble^*, Diane Hanger, Saskia Pollack

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

Abstract

Tauopathies are a group of neurodegenerative diseases characterised by cognitive and motor dysfunction, attributed to the accumulation of abnormal tau protein in the brain. Truncated forms of tau contribute to disease pathogenesis, including a C-terminal fragment of tau (Tau35) that we previously identified in the brain of individuals affected by tauopathy. Tau35 expression under the control of the human tau promoter in mice results in the deposition of highly phosphorylated aggregates of human Tau35 and endogenous mouse tau, progressive cognitive and motor deficits and impaired synaptic plasticity. However, the pathological mechanisms driven by tau fragments remain unclear. In our latest study, we linked disease-associated Tau35 with alterations in the autophagy and endolysosomal pathway, which have already been widely implicated in the pathogenesis of Alzheimer’s disease (AD) and other tauopathies.

Original language	English
Journal	Autophagy Reports
DOIs	https://doi.org/10.1080/27694127.2024.2409563
Publication status	Published - 8 Oct 2024

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10.1080/27694127.2024.2409563

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title = "Truncated tau disrupts autophagy and endolysosomal systems",

abstract = "Tauopathies are a group of neurodegenerative diseases characterised by cognitive and motor dysfunction, attributed to the accumulation of abnormal tau protein in the brain. Truncated forms of tau contribute to disease pathogenesis, including a C-terminal fragment of tau (Tau35) that we previously identified in the brain of individuals affected by tauopathy. Tau35 expression under the control of the human tau promoter in mice results in the deposition of highly phosphorylated aggregates of human Tau35 and endogenous mouse tau, progressive cognitive and motor deficits and impaired synaptic plasticity. However, the pathological mechanisms driven by tau fragments remain unclear. In our latest study, we linked disease-associated Tau35 with alterations in the autophagy and endolysosomal pathway, which have already been widely implicated in the pathogenesis of Alzheimer{\textquoteright}s disease (AD) and other tauopathies.",

author = "{Jimenez Sanchez}, Maria and Wendy Noble and Diane Hanger and Saskia Pollack",

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T1 - Truncated tau disrupts autophagy and endolysosomal systems

AU - Jimenez Sanchez, Maria

AU - Noble, Wendy

AU - Hanger, Diane

AU - Pollack, Saskia

PY - 2024/10/8

Y1 - 2024/10/8

N2 - Tauopathies are a group of neurodegenerative diseases characterised by cognitive and motor dysfunction, attributed to the accumulation of abnormal tau protein in the brain. Truncated forms of tau contribute to disease pathogenesis, including a C-terminal fragment of tau (Tau35) that we previously identified in the brain of individuals affected by tauopathy. Tau35 expression under the control of the human tau promoter in mice results in the deposition of highly phosphorylated aggregates of human Tau35 and endogenous mouse tau, progressive cognitive and motor deficits and impaired synaptic plasticity. However, the pathological mechanisms driven by tau fragments remain unclear. In our latest study, we linked disease-associated Tau35 with alterations in the autophagy and endolysosomal pathway, which have already been widely implicated in the pathogenesis of Alzheimer’s disease (AD) and other tauopathies.

AB - Tauopathies are a group of neurodegenerative diseases characterised by cognitive and motor dysfunction, attributed to the accumulation of abnormal tau protein in the brain. Truncated forms of tau contribute to disease pathogenesis, including a C-terminal fragment of tau (Tau35) that we previously identified in the brain of individuals affected by tauopathy. Tau35 expression under the control of the human tau promoter in mice results in the deposition of highly phosphorylated aggregates of human Tau35 and endogenous mouse tau, progressive cognitive and motor deficits and impaired synaptic plasticity. However, the pathological mechanisms driven by tau fragments remain unclear. In our latest study, we linked disease-associated Tau35 with alterations in the autophagy and endolysosomal pathway, which have already been widely implicated in the pathogenesis of Alzheimer’s disease (AD) and other tauopathies.

U2 - 10.1080/27694127.2024.2409563

DO - 10.1080/27694127.2024.2409563

M3 - Article

JO - Autophagy Reports

JF - Autophagy Reports

ER -

Truncated tau disrupts autophagy and endolysosomal systems

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