H. Kosako

The Rubicon-WIPI axis regulates exosome biogenesis during aging

This study identifies the Rubicon-WIPI axis as a regulator of exosome biogenesis, showing its role in age-dependent exosome release and microRNA fate in mice.

PDZD8-FKBP8 tethering complex at ER-mitochondria contact sites regulates mitochondrial complexity

This study identifies FKBP8 as the tethering partner of PDZD8 at ER-mitochondria contact sites, showing their interdependence in regulating mitochondrial morphology.

Golgi membrane proteins YIPF3 and YIPF4 regulate turnover of the Golgi apparatus through autophagy

This study identifies YIPF3 and YIPF4 as Golgi-specific autophagy receptors that mediate Golgi turnover via selective autophagy.

Host ZCCHC3 blocks HIV-1 infection and production by a dual mechanism

This study identifies ZCCHC3 as a novel anti-HIV-1 factor that acts through a dual mechanism to block viral infection and production.

Structural basis of Irgb6 inactivation by Toxoplasma gondii through the phosphorylation of switch I.

The paper reveals how Toxoplasma gondii inactivates Irgb6 through ROP18-mediated phosphorylation, preventing its function in host defense.

Optimized Workflow for Enrichment and Identification of Biotinylated Peptides using Tamavidin 2-REV for BioID and Cell Surface Proteomics

The paper optimizes a workflow for enriching and identifying biotinylated peptides using Tamavidin 2-REV, improving detection in cell surface proteomics and BioID applications.

OTUD1 deubiquitylase regulates NF-κB- and KEAP1-mediated inflammatory responses and reactive oxygen species-associated cell death pathways

This study identifies OTUD1 as a deubiquitylase that suppresses NF-κB and KEAP1-mediated inflammatory and oxidative stress responses, while promoting antiviral pathways and ROS-associated cell death.

Peroxisome counteracts oxidative stresses by suppressing catalase import via Pex14 phosphorylation

The paper shows that oxidative stress induces Pex14 phosphorylation, which reduces catalase import into peroxisomes, increasing cytosolic catalase and enhancing cell resistance to H2O2.

Quantitative proteomics indicate a strong correlation of mitotic phospho-/dephosphorylation with non-structured regions of substrates

The paper uses quantitative proteomics to show that mitotic phospho-/dephosphorylation events are strongly correlated with non-structured regions of substrates.