Journal Article (Review Article)

DZNE-2023-01136

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Regulation of tau by peptidyl-prolyl isomerases

Zhuang, S. (First author)DZNE* ; Chakraborty, P.Extern* ; Zweckstetter, M. (Last author)DZNE*

2024
Elsevier Amsterdam [u.a.]

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Please use a persistent id in citations: doi:10.1016/j.sbi.2023.102739

Abstract: Tau is an intrinsically disordered protein found abundantly in axons, where it binds to microtubules. Since tau is a central player in the dynamic microtubule network, it is highly regulated by post-translational modifications. Abnormal hyperphosphorylation and aggregation of tau characterize a group of diseases called tauopathies. A specific protein family of cis/trans peptidyl-prolyl isomerases (PPIases) can interact with tau to regulate its aggregation and neuronal resilience. Structural interactions between tau and specific PPIases have been determined, establishing possible mechanisms for tau regulation and modification. While there have been numerous in vivo studies evaluating the impact of PPIase expression on tau biology/pathology, the direct roles of PPIases have yet to be fully characterized. Different PPIases correlate to either increased or decreased levels of tau-associated degeneration. Therefore, the ability of PPIases to structurally modify and regulate tau should be further investigated due to its potential therapeutic implications for Alzheimer's disease and other tauopathies.

Keyword(s): Humans (MeSH) ; Peptidylprolyl Isomerase: chemistry (MeSH) ; Alzheimer Disease: metabolism (MeSH) ; Tauopathies: drug therapy (MeSH) ; Tauopathies: metabolism (MeSH) ; Protein Processing, Post-Translational (MeSH) ; Peptidylprolyl Isomerase

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Contributing Institute(s):

1. Translational Structural Biology (AG Zweckstetter)

Research Program(s):

1. 352 - Disease Mechanisms (POF4-352) (POF4-352)

Appears in the scientific report 2024

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