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TMEM59 regulates microglial Aβ phagocytosis in a TREM2-dependent manner and acts as a potential therapeutic target for Aβ amyloidosis.

Created on 25 Sep 2026

Authors

Jian Meng, Yong Wang, Jinghui Wang, Yiqing Chen, Zihao Zhao, Ziqian Tang, Jing Cao, Xian Zhang, Hong Luo, Huihui Li, Yili Wu, Yingjun Zhao, Weihong Song, Yun-Wu Zhang

Published in

Alzheimer's & dementia : the journal of the Alzheimer's Association. Volume 22. Issue 9. Pages e71873.

Abstract

Microglia-mediated clearance of amyloid beta (Aβ) is crucial for mitigating Alzheimer's disease (AD) progression, yet the molecular regulators of microglial phagocytosis remain incompletely understood.
We assessed AD-related phenotypes in 5xFAD mice with microglia-specific deletion of transmembrane protein 59 (TMEM59). Microglial transcriptomic profiling was performed using single-cell RNA sequencing (scRNA-seq). A chaperone-mediated autophagy-targeting chimera (CMATAC) peptide was developed to degrade TMEM59, and its therapeutic efficacy was evaluated.
Microglia-specific TMEM59 ablation attenuated cognitive deficits, Aβ plaque burden, and synapse loss in 5xFAD mice. TMEM59 deficiency reprogrammed disease-associated microglia toward a highly phagocytic state. Mechanistically, TMEM59 deficiency enhanced microglial Aβ phagocytosis in a triggering receptor expressed on myeloid cells 2 (TREM2)-dependent manner, as it stabilized TREM2 protein, whereas loss of TREM2 abolished these protective effects. Treatment with the TMEM59-degrading CMATAC peptide alleviated behavioral deficits and enhanced microglial Aβ phagocytosis in 5xFAD mice.
TMEM59 is a key regulator of microglial phagocytosis in AD and a novel target for amyloidosis intervention.

PMID:
42786742
Bibliographic data and abstract were imported from PubMed on 25 Sep 2026.

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