A5057457862- Autophagy in Disease and Therapy
- Endoplasmic Reticulum Stress and Disease
- Cellular transport and secretion
- Calcium signaling and nucleotide metabolism
- RNA modifications and cancer
- Toxoplasma gondii Research Studies
- RNA Interference and Gene Delivery
- RNA and protein synthesis mechanisms
- Lysosomal Storage Disorders Research
- Studies on Chitinases and Chitosanases
- Ubiquitin and proteasome pathways
- Bacterial Genetics and Biotechnology
- Nuclear Structure and Function
- Mosquito-borne diseases and control
- Adenosine and Purinergic Signaling
- Polyamine Metabolism and Applications
- Lipid metabolism and biosynthesis
- CRISPR and Genetic Engineering
- Fungal and yeast genetics research
- RNA Research and Splicing
- Bacteriophages and microbial interactions
- Microbial Natural Products and Biosynthesis
- Plant responses to water stress
- Plant Gene Expression Analysis
- Signaling Pathways in Disease
Tokyo Institute of Technology
2015-2024
Institute of Science Tokyo
2024
Japan Science and Technology Agency
2004-2015
Research Institute for Bioscience and Biotechnology
2015
Centre de Recherche en Économie et Statistique
2015
Centre for Research in Engineering Surface Technology
2015
Center for Responsible Travel
2015
Frontier Hospital
2012-2014
The Graduate University for Advanced Studies, SOKENDAI
2008
National Institute for Basic Biology
2007-2008
Autophagy is a non‐selective bulk degradation process in which isolation membranes enclose portion of cytoplasm to form double‐membrane vesicles, called autophagosomes, and deliver their inner constituents the lytic compartments. Recent studies have also shed light on another mode autophagy that selectively degrades various targets. Yeast Atg8 its mammalian homologue LC3 are ubiquitin‐like modifiers localized play crucial roles formation autophagosomes. These proteins involved selective...
Although ubiquitin is thought to be important for the autophagic sequestration of invading bacteria (also called xenophagy), its precise role remains largely enigmatic. Here we determined how involved in this process. After invasion, conjugated host cellular proteins endosomes that contain Salmonella or transfection reagent–coated latex (polystyrene) beads, which mimic bacteria. Ubiquitin recognized by machinery independently LC3–ubiquitin interaction through adaptor proteins, including a...
The biogenesis of double-membrane vesicles called autophagosomes, which sequester and transport intracellular material for degradation in lysosomes or vacuoles, is a central event autophagy. This process requires unique set factors autophagy-related (Atg) proteins. Atg proteins assemble to organize the preautophagosomal structure (PAS), at cup-shaped membrane, isolation membrane (or phagophore), forms expands become autophagosome. molecular mechanism autophagosome remains poorly understood....
Atg8 is a ubiquitin-like protein required for autophagy in the budding yeast Saccharomyces cerevisiae. A system mediates conjugation of C terminus to lipid phosphatidylethanolamine (PE), and this conjugate (Atg8–PE) plays crucial role autophagosome formation at phagophore assembly site/pre-autophagosomal structure (PAS). The cysteine protease Atg4 processes newly synthesized also delipidates release from membranes. While former prerequisite lipidation Atg8, significance latter has remained...
The Atg8 family of ubiquitin-like proteins play pivotal roles in autophagy and other processes involving vesicle fusion transport where the lysosome/vacuole is end station. Nuclear are also emerging. Here, we review structural functional features their protein-protein interaction modes model organisms such as yeast, Arabidopsis, C. elegans Drosophila to humans. Although varying number homologs, from one yeast seven humans, more than ten some plants, there a strong evolutionary conservation...
Atg16 interacts with the Atg12-Atg5 protein conjugate through its N-terminal domain and self-assembles coiled-coil (CCD). Formation of Atg12-Atg5·Atg16 complex is essential for autophagy, bulk degradation process conserved among most eukaryotes. Here, we report crystal structures full-length Saccharomyces cerevisiae at 2.8 Å resolution CCD 2.5 resolution. The each exhibit an extended α-helix, 90 130 Å, respectively, form a parallel dimer in crystals. Although apparent molecular weight...
In selective autophagy, degradation targets are specifically recognized, sequestered by the autophagosome, and transported into lysosome or vacuole. Previous studies delineated molecular basis which autophagy machinery recognizes those targets, but regulation of this process is still poorly understood. paper, we find that highly conserved multifunctional kinase Hrr25 regulates two distinct autophagy–related pathways in Saccharomyces cerevisiae. responsible for phosphorylation receptor...
A hallmark of autophagy is the de novo formation double-membrane vesicles called autophagosomes, which sequester various cellular constituents for degradation in lysosomes or vacuoles. The membrane dynamics underlying biogenesis including origin autophagosomal membrane, are still elusive. Although previous studies suggested that COPII closely associated with autophagosome biogenesis, it remains unclear whether these serve as a source membrane. Using recently developed vesicle-labeling system...
In selective autophagy of the nucleus (hereafter nucleophagy), nucleus-derived double-membrane vesicles (NDVs) are formed, sequestered within autophagosomes, and delivered to lysosomes or vacuoles for degradation. Saccharomyces cerevisiae, nuclear envelope (NE) protein Atg39 acts as a nucleophagy receptor, which interacts with Atg8 target NDVs forming autophagosomal membranes. this study, we revealed that is anchored outer membrane via its transmembrane domain also associated inner...