TATA-box binding protein-associated factor 15 (TAF15) is an RNA-binding member of the FET family recently identified as the primary fibrillar constituent in a subset of frontotemporal lobar degenerati...

Targeting replication-associated DNA repair mechanisms, including the control of ADP-ribosylation by PARP1/2 and PARG, is a powerful therapeutic approach for cancer. However, the mechanisms by which PARG inhibition impacts DNA replication remain unclear. Here, we combine isolation of proteins on nascent DNA (iPOND) with quantitative proteomics and functional assays to investigate replication fork dynamics upon acute PARG inhibition. We find that FET family proteins (FUS, EWS, and TAF15) are recruited to replication forks in a PAR-dependent manner, forming condensates that slow fork progression and promote fork reversal. FET proteins control fork dynamics in response to some, but not all, replication stresses. FUS inactivation leads to unrestrained fork progression via RECQ1 and PRIMPOL, increased single-stranded DNA gaps, genome instability, and synthetic lethality with BRCA1 deficiency. These findings reveal that FET protein assemblies modulate replication stress responses, influencin

Yi et al. uncover a TAF15-oxidative stress axis in neurodegeneration. They demonstrate that the neuronal TAF15 overexpression triggers oxidative stress and neurotoxicity, leading to gliosis and behavioral abnormalities. Notably, the antioxidant N-acetylcysteine amide (NACA) rescues these phenotypes, highlighting TAF15 as a potential therapeutic target.

2026.10.05 新潟大学 プレスリリース 【本研究成果のポイント】ALS の進行には個人差がありますが、その理由はまだ十分に解明されていません。137 例の孤発性...

Nature - Cryogenic electron microscopy structures of amyloid filaments extracted from patient brains reveal that the protein TAF15 forms filaments that characterize certain cases of frontotemporal...

FUS, EWSR1 and TAF15 function in a variety of cellular processes by forming biomolecular condensates. Here the authors reveal that these proteins respond to replication stress to promote fork reversal...

Droplet simulations were undertaken of six human TF IDRs from three different TF families: the FET family (FUS residues 2–214, EWS residues 47–266, TAF15 residues 2–205), the SP/KLF family (SP1 residues 2–507, and SP2 residues 1–524), and the HNF family...

The FET family proteins, which includes FUS, EWS, and TAF15, are RNA chaperones instrumental in proc

Read the full paper: TAF15-mediated m5C modification of MTHFD2 RNA reveals a novel therapeutic target for IDH mutant gliomas

Yi et al. uncover a TAF15-oxidative stress axis in neurodegeneration. They demonstrate that the neuronal TAF15 overexpression triggers oxidative stress and neurotoxicity, leading to gliosis and behavi...

Acute leukemias with chimeric fusion genes involving FET (FUS, EWSR1, and TAF15) family proteins and ETS (E26 transformation-specific)-like transcription factors often present with unique clinical and pathological characteristics. This mini-review aims to summarize the clinical and pathological features of acute leukemia cases harboring rearrangements involving the fused in sarcoma (FUS) or Ewing sarcoma breakpoint region 1 (EWSR1) genes.

Read the full paper: Elevated neuronal TAF15 expression induces oxidative stress and anxiety-related behavioral deficits

Acute leukemias with chimeric fusion genes involving FET (FUS, EWSR1, and TAF15) family proteins and ETS (E26 transformation-specific)-like transcription factors often present with unique clinical and pathological characteristics. This mini-review aims to summarize the clinical and pathological features of acute leukemia cases harboring rearrangements involving the fused in sarcoma (FUS) or Ewing sarcoma breakpoint region 1 (EWSR1) genes.

Read the full paper: Aggregation and propagation of TAF15 trigger neurodegeneration

Meng et al. report that TAF15 forms amyloid fibrils capable of propagation both in vitro and in vivo. The spread of TAF15 pathology triggers progressive neurodegeneration, cognitive impairment, and anxiety- and depression-like behaviors. These findings establish TAF15 aggregation as a key pathogenic driver of neurodegenerative disease.