Deciphering the role of TYK2 in tau phosphorylation and pathology

Alexander Fröhlich; Kathryn R. Bowles

doi:10.1016/j.tins.2025.01.004

Deciphering the role of TYK2 in tau phosphorylation and pathology

Alexander Fröhlich
, Kathryn R. Bowles

Research output: Contribution to journal › Short survey › peer-review

2 Scopus citations

Abstract

Tau phosphorylation plays an essential role in regulating tau's microtubule-stabilizing function, but its hyperphosphorylation drives tauopathies such as Alzheimer's disease (AD). In a recent study, Kim and colleagues decipher that tyrosine kinase 2 (TYK2) phosphorylates tau at tyrosine 29, promoting its stabilization and aggregation by interfering with autophagic clearance, providing novel insights into tau pathology and potential therapeutic strategies.

Original language	English
Pages (from-to)	171-173
Number of pages	3
Journal	Trends in Neurosciences
Volume	48
Issue number	3
DOIs	https://doi.org/10.1016/j.tins.2025.01.004
State	Published - Mar 2025
Externally published	Yes

Keywords

Alzheimer's disease
hyperphosphorylation
microtubule
neurodegeneration
post-translational modification
tauopathies

Access to Document

10.1016/j.tins.2025.01.004

Cite this

@article{23c90141cad6448fa95474bc17312fd9,

title = "Deciphering the role of TYK2 in tau phosphorylation and pathology",

abstract = "Tau phosphorylation plays an essential role in regulating tau's microtubule-stabilizing function, but its hyperphosphorylation drives tauopathies such as Alzheimer's disease (AD). In a recent study, Kim and colleagues decipher that tyrosine kinase 2 (TYK2) phosphorylates tau at tyrosine 29, promoting its stabilization and aggregation by interfering with autophagic clearance, providing novel insights into tau pathology and potential therapeutic strategies.",

keywords = "Alzheimer's disease, hyperphosphorylation, microtubule, neurodegeneration, post-translational modification, tauopathies",

author = "Alexander Fr{\"o}hlich and Bowles, \{Kathryn R.\}",

note = "Publisher Copyright: {\textcopyright} 2025 The Author(s)",

year = "2025",

month = mar,

doi = "10.1016/j.tins.2025.01.004",

language = "English",

volume = "48",

pages = "171--173",

journal = "Trends in Neurosciences",

issn = "0166-2236",

publisher = "Elsevier Ltd.",

number = "3",

}

TY - JOUR

T1 - Deciphering the role of TYK2 in tau phosphorylation and pathology

AU - Fröhlich, Alexander

AU - Bowles, Kathryn R.

PY - 2025/3

Y1 - 2025/3

N2 - Tau phosphorylation plays an essential role in regulating tau's microtubule-stabilizing function, but its hyperphosphorylation drives tauopathies such as Alzheimer's disease (AD). In a recent study, Kim and colleagues decipher that tyrosine kinase 2 (TYK2) phosphorylates tau at tyrosine 29, promoting its stabilization and aggregation by interfering with autophagic clearance, providing novel insights into tau pathology and potential therapeutic strategies.

AB - Tau phosphorylation plays an essential role in regulating tau's microtubule-stabilizing function, but its hyperphosphorylation drives tauopathies such as Alzheimer's disease (AD). In a recent study, Kim and colleagues decipher that tyrosine kinase 2 (TYK2) phosphorylates tau at tyrosine 29, promoting its stabilization and aggregation by interfering with autophagic clearance, providing novel insights into tau pathology and potential therapeutic strategies.

KW - Alzheimer's disease

KW - hyperphosphorylation

KW - microtubule

KW - neurodegeneration

KW - post-translational modification

KW - tauopathies

UR - https://www.scopus.com/pages/publications/85217405120

U2 - 10.1016/j.tins.2025.01.004

DO - 10.1016/j.tins.2025.01.004

M3 - Short survey

AN - SCOPUS:85217405120

SN - 0166-2236

VL - 48

SP - 171

EP - 173

JO - Trends in Neurosciences

JF - Trends in Neurosciences

IS - 3

ER -

Deciphering the role of TYK2 in tau phosphorylation and pathology

Abstract

Keywords

Access to Document

Fingerprint

Cite this