The effect of tau K677 lactylation on ferritinophagy and ferroptosis in Alzheimer's disease

Alzheimer's disease (AD) is characterized by cognitive decline and the accumulation of amyloid-beta plaques and hyperphosphorylated tau protein. The role of tau lactylation at the K677 site in AD progression is not well understood. This study explores how tau K677 lactylation affects ferritinophagy, ferroptosis, and their functions in an AD mouse model. Results show that mutating the K677 site to R reduces tau lactylation and inhibits ferroptosis by regulating iron metabolism factors like NCOA4 and FTH1.Tau-mutant mice showed improved memory and learning skills compared to wild-type mice. The mutation also reduced neuronal damage and was associated with decreased tau lactylation at the K677 site, regardless of phosphorylated tau levels. Gene set enrichment analysis showed that lactylation at this site was linked to the MAPK pathway, which was important for ferritinophagy in AD mice. In summary, our research indicates that the K677 mutation in tau protein may protect against AD by influencing ferritinophagy and ferroptosis through MAPK signaling pathways. Understanding these modifications in tau could lead to new treatments for AD.

Authors

Institutions

Publication Details

Journal
Free Radical Biology and Medicine
Published
2024-09-21
DOI
https://doi.org/10.1016/j.freeradbiomed.2024.09.021
Citations
42
Primary Topic
Ferroptosis and cancer prognosis
Type
article
Field-Weighted Citation Impact
17.60
Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

The effect of tau K677 lactylation on ferritinophagy and ferroptosis in Alzheimer's disease

Peng Xie, Wenfeng Yu, Bin Bi, Cheng‐Peng Li et al.
42 citations
Free Radical Biology and Medicine
Ferroptosis and cancer prognosis
17.60
article

The effect of tau K677 lactylation on ferritinophagy and ferroptosis in Alzheimer's disease

Peng Xie, Wenfeng Yu, Bin Bi, Cheng‐Peng Li, Mingyan Xia, Zhenkui Ren, Dongfen Guo, Jianwei Xu, Gang Wu, Xiaoqiong An, Jun He
article en
42 citations

Abstract

Alzheimer's disease (AD) is characterized by cognitive decline and the accumulation of amyloid-beta plaques and hyperphosphorylated tau protein. The role of tau lactylation at the K677 site in AD progression is not well understood. This study explores how tau K677 lactylation affects ferritinophagy, ferroptosis, and their functions in an AD mouse model. Results show that mutating the K677 site to R reduces tau lactylation and inhibits ferroptosis by regulating iron metabolism factors like NCOA4 and FTH1.Tau-mutant mice showed improved memory and learning skills compared to wild-type mice. The mutation also reduced neuronal damage and was associated with decreased tau lactylation at the K677 site, regardless of phosphorylated tau levels. Gene set enrichment analysis showed that lactylation at this site was linked to the MAPK pathway, which was important for ferritinophagy in AD mice. In summary, our research indicates that the K677 mutation in tau protein may protect against AD by influencing ferritinophagy and ferroptosis through MAPK signaling pathways. Understanding these modifications in tau could lead to new treatments for AD.

Free Radical Biology and MedicineVol. 224
Guiyang Medical University (CN), Guizhou University (CN), Affiliated Hospital of Guizhou Medical University (CN), Guizhou Provincial People's Hospital (CN)
Zero hunger
Openalex Percentile: Top 0%
Ferroptosis and cancer prognosis
17.60
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.