Kuninori Suzuki

ORCID: 0000-0003-1239-1179
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About
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Research Areas
  • Autophagy in Disease and Therapy
  • Endoplasmic Reticulum Stress and Disease
  • Studies on Chitinases and Chitosanases
  • Cellular transport and secretion
  • Fungal and yeast genetics research
  • Mitochondrial Function and Pathology
  • Biofuel production and bioconversion
  • Photosynthetic Processes and Mechanisms
  • Microbial Community Ecology and Physiology
  • Algal biology and biofuel production
  • Marine and coastal plant biology
  • Polyamine Metabolism and Applications
  • Geological and Geochemical Analysis
  • Peptidase Inhibition and Analysis
  • CRISPR and Genetic Engineering
  • Mosquito-borne diseases and control
  • Toxoplasma gondii Research Studies
  • Plant pathogens and resistance mechanisms
  • Ubiquitin and proteasome pathways
  • Protist diversity and phylogeny
  • RNA Interference and Gene Delivery
  • Calcium signaling and nucleotide metabolism
  • Genomics and Phylogenetic Studies
  • RNA Research and Splicing
  • Neurological diseases and metabolism

The University of Tokyo
2014-2024

Tokyo Institute of Technology
2009-2012

Bank of Japan
2010

National Institute of Genetics
2010

Hitachi (Japan)
2010

National Institute for Basic Biology
2001-2009

The Graduate University for Advanced Studies, SOKENDAI
2001-2008

Nagoya University
2006

Japan International Research Center for Agricultural Sciences
2001

Tokyo University of Science
1992-1995

In macroautophagy, cytoplasmic components are delivered to lysosomes for degradation via autophagosomes that formed by closure of cup-shaped isolation membranes. However, how the membranes is poorly understood. We recently found in yeast a novel ubiquitin-like system, Apg12-Apg5 conjugation essential autophagy. Here we show mouse conjugate localizes embryonic stem cells. Using green fluorescent protein–tagged Apg5, revealed membrane developed from small crescent-shaped compartment. Apg5 on...

10.1083/jcb.152.4.657 article EN The Journal of Cell Biology 2001-02-12

Autophagy is a bulk degradation process that conserved in eukaryotic cells and functions the turnover of cytoplasmic materials organelles. When face nutrient starvation, autophagosome, double-membraned organelle, generated from pre-autophagosomal structure (PAS). In yeast Saccharomyces cerevisiae, 16 ATG (autophagy-related) genes are essential for autophagosome formation. Most Atg proteins involved PAS, leading to production. However, mechanism PAS organization remains be elucidated. Here,...

10.1111/j.1365-2443.2007.01050.x article EN Genes to Cells 2007-02-01

Autophagy is a degradation process accompanied by dynamic membrane organization. In the yeast, Saccharomyces cerevisiae, about 30 ATG (autophagy-related) genes have been identified as important for autophagy. Among them, 17 are indispensable formation of autophagosome, an organelle enclosed double lipid bilayer during starvation-induced Recently, central structure autophagosome generation, termed pre-autophagosomal structure, was identified. Despite intensive study, many questions regarding...

10.1016/j.febslet.2007.01.096 article EN FEBS Letters 2007-03-12

Autophagy is a bulk degradation system mediated by biogenesis of autophagosomes under starvation conditions. In Saccharomyces cerevisiae, membrane sac called the isolation (IM) generated from pre-autophagosomal structure (PAS); ultimately, IM expands to become mature autophagosome. Eighteen Atg (autophagy-related) proteins are engaged in autophagosome formation at PAS. However, cup-shaped was visualized just as dot fluorescence microscopy, posing challenge further understanding detailed...

10.1242/jcs.122960 article EN cc-by-nc-sa Journal of Cell Science 2013-01-01

Highlights•Ape1 undergoes phase separation to form semi-liquid droplets•Floatability of Atg19 mediates condensation on the surface Ape1 droplets•Atg19 and Atg8-PE are sufficient for selective membrane sequestration droplets•Liquidity droplets is important autophagySummaryClearance biomolecular condensates by autophagy thought play a crucial role in cellular homeostasis. However, mechanism underlying whether liquidity determines condensate's susceptibility degradation remain unknown. Here, we...

10.1016/j.molcel.2019.12.026 article EN publisher-specific-oa Molecular Cell 2020-01-28

Double membrane structure, autophagosome, is formed de novo in the process of autophagy yeastSaccharomyces cerevisiae, and many Apg proteins participate this process. To further understand autophagy, we analyzed involvement factors engaged secretory pathway. First, showed that Sec18p (N-ethylmaleimide-sensitive fusion protein, NSF) Vti1p (solubleN-ethylmaleimide-sensitive protein attachment SNARE), soluble N-ethylmaleimide-sensitive receptor are required for autophagosome to vacuole but not...

10.1091/mbc.12.11.3690 article EN Molecular Biology of the Cell 2001-11-01

Autophagy is a degradation system of cytoplasmic proteins and organelles via formation double-membrane vesicles called autophagosomes. In the yeast Saccharomyces cerevisiae, autophagosomes are formed pre-autophagosomal structure (PAS) in manner dependent on Atg proteins. Under nutrient-rich condition, Atg9 recruited to PAS by binding Atg11 for Cvt pathway. However, because atg11Delta cells starved condition autophagy induced, autophagy-specific mechanism recruitment has been assumed. Here,...

10.1111/j.1365-2443.2009.01299.x article EN Genes to Cells 2009-04-13

In <i>Saccharomyces cerevisiae</i>, aminopeptidase I (Ape1p) and α-mannosidase (Ams1p) are known cargoes of selective autophagy. Atg19p has been identified as an Ape1p receptor targets to the preautophagosomal structure (PAS). Under nutrient-rich conditions, transport Ams1p vacuole largely depends on Atg19p. Here, we show that Atg34p (Yol083wp), a homolog Atg19p, is for during interacted with Ams1p, Atg11p, Atg8p using distinct domains. Homo-oligomerized bound Ams1-binding domain Atg34p;...

10.1074/jbc.m110.143511 article EN cc-by Journal of Biological Chemistry 2010-07-17

Autophagy is a process of self-digestion generally observed in eukaryotes and has been shown to play crucial roles for survival under starvation removal deleterious substances. Despite great advances that have made, many problems mechanisms autophagy remain unsolved. As large number autophagy-related proteins are identified each species, database collects data, identifies their homologs other species makes them available will contribute research advancement. no such resources exist, we built...

10.1093/nar/gkq995 article EN Nucleic Acids Research 2010-10-23

Autophagy is a degradative process in which cytoplasmic components are non-selectively sequestered by double-membrane structures, termed autophagosomes, and transported to the vacuole. We have identified characterized novel protein Apg2p essential for autophagy yeast. Biochemical fluorescence microscopic analyses indicate that functions at step of autophagosome formation. localizes some membranous structure distinct from any known organelle. Using fluorescent protein-tagged Apg2p, we showed...

10.1074/jbc.m102346200 article EN cc-by Journal of Biological Chemistry 2001-08-01

Autophagy, an intracellular degradation system, is highly conserved among eukaryotes from yeast to mammalian cells. In the Saccharomyces cerevisiae, most Atg (autophagy-related) proteins, which are essential for autophagosome formation, recruited a restricted region close vacuole, termed vacuole-isolation membrane contact site (VICS), upon induction of autophagy. Subsequently, isolation (IM) expands and sequesters cytoplasmic materials become closed autophagosome. S. ubiquitin-like protein...

10.1371/journal.pone.0181047 article EN cc-by PLoS ONE 2017-07-13

In the yeast <i>Saccharomyces cerevisiae</i>, a precursor form of aminopeptidase I (prApe1) and α-mannosidase (Ams1) are selectively transported to vacuole through cytoplasm-to-vacuole targeting pathway under vegetative conditions autophagy starvation conditions. Atg19 plays central role in these processes by linking Ams1 prApe1 Atg8 Atg11. However, little is known about molecular mechanisms cargo recognition Atg19. Here, we report structural functional analyses its paralog, Atg34. A...

10.1074/jbc.m110.143545 article EN cc-by Journal of Biological Chemistry 2010-07-22
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