Naotada Ishihara

ORCID: 0000-0002-6305-7149
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About
Contact & Profiles
Research Areas
  • Mitochondrial Function and Pathology
  • ATP Synthase and ATPases Research
  • Metabolism and Genetic Disorders
  • Autophagy in Disease and Therapy
  • Endoplasmic Reticulum Stress and Disease
  • Photosynthetic Processes and Mechanisms
  • Cellular transport and secretion
  • Cancer, Hypoxia, and Metabolism
  • Pancreatic function and diabetes
  • interferon and immune responses
  • Metabolism, Diabetes, and Cancer
  • RNA modifications and cancer
  • RNA Research and Splicing
  • Cell death mechanisms and regulation
  • Lipid metabolism and biosynthesis
  • Metabolomics and Mass Spectrometry Studies
  • Cancer Treatment and Pharmacology
  • Cancer-related molecular mechanisms research
  • Muscle Physiology and Disorders
  • Liver Disease Diagnosis and Treatment
  • Reproductive Biology and Fertility
  • Chemotherapy-induced cardiotoxicity and mitigation
  • CRISPR and Genetic Engineering
  • Peroxisome Proliferator-Activated Receptors
  • Amino Acid Enzymes and Metabolism

Kurume University
2015-2025

Osaka University
2018-2025

Graduate School USA
2022

Kobe University
2022

Osaka Health Science University
2018

Institute of Life Sciences
2016-2017

Life Science Institute
2017

Tokyo Medical and Dental University
2008-2014

Terumo (Japan)
2013

Kyushu University
1995-2007

Vps30p/Apg6p is required for both autophagy and sorting of carboxypeptidase Y (CPY). Although Vps30p known to interact with Apg14p, its precise role remains unclear. We found that two proteins copurify Vps30p. They were identified by mass spectrometry be Vps38p Vps34p, a phosphatidylinositol (PtdIns) 3–kinase. Vps38p, Vps15p, an activator coimmunoprecipitated These results indicate functions as subunit Vps34 PtdIns 3–kinase complex(es). Phenotypic analyses indicated Apg14p are each CPY...

10.1083/jcb.152.3.519 article EN The Journal of Cell Biology 2001-01-29

We characterized Apg8/Aut7p essential for autophagy in yeast. Apg8p was transcriptionally upregulated response to starvation and mostly existed as a protein bound membrane under both growing conditions. Immunofluorescence microscopy revealed that the intracellular localization of changed drastically after shift starvation. resided on unidentified tiny dot structures dispersed cytoplasm at phase. During starvation, it localized large punctate structures, some which were confirmed be...

10.1083/jcb.147.2.435 article EN The Journal of Cell Biology 1999-10-18

The mammalian homologues of yeast and Drosophila Fzo, mitofusin (Mfn) 1 2, are both essential for mitochondrial fusion maintenance morphology. Though the GTPase domain is required Mfn protein function, molecular mechanisms GTPase-dependent reaction as well functional division two proteins unknown. To examine function proteins, tethering membranes was measured in vitro by fluorescence microscopy using green protein- or red fluorescent protein-tagged Mfn1-expressing mitochondria,...

10.1242/jcs.01565 article EN Journal of Cell Science 2004-12-01

Upon mitochondrial depolarization, Parkin, a Parkinson disease-related E3 ubiquitin ligase, translocates from the cytosol to mitochondria and promotes their degradation by mitophagy, selective type of autophagy. Here, we report that in addition Parkin mediates proteasome-dependent outer membrane proteins such as Tom20, Tom40, Tom70, Omp25 depolarized mitochondria. By contrast, inner matrix largely depends on mitophagy. Furthermore, induces rupture mitochondria, which also proteasomal...

10.1074/jbc.m110.209338 article EN cc-by Journal of Biological Chemistry 2011-03-19

Autophagy, responsible for the delivery of cytoplasmic components to lysosome/vacuole degradation, is major degradative pathway in eukaryotic cells. This process requires a ubiquitin-like protein conjugation system, which Apg12 covalently bound Apg5. In yeast <i>Saccharomyces cerevisiae</i>, Apg12-Apg5 conjugate further interacts with small coiled-coil protein, Apg16. The and Apg16 are localized cytosol pre-autophagosomal structures play an essential role autophagosome formation. Here we...

10.1074/jbc.m111889200 article EN cc-by Journal of Biological Chemistry 2002-05-01

Macroautophagy is an intracellular degradation system by which cytoplasmic materials are enclosed the autophagosome and delivered to lysosome. Autophagosome formation considered take place on endoplasmic reticulum involves functions of autophagy-related (Atg) proteins. Here, we report identification characterization mammalian Atg2 homologues Atg2A Atg2B. Simultaneous silencing Atg2B causes a block in autophagic flux accumulation unclosed structures containing most Atg localizes membrane, as...

10.1091/mbc.e11-09-0785 article EN cc-by-nc-sa Molecular Biology of the Cell 2012-01-05

Mammalian cells typically contain thousands of copies mitochondrial DNA assembled into hundreds nucleoids. Here we analyzed the dynamic features nucleoids in terms membrane dynamics involving balanced fusion and fission. In fission GTPase dynamin-related protein (Drp1)-deficient cells, were enlarged by their clustering within hyperfused mitochondria. normal often occurred adjacent to nucleoids, since localization Mff Drp1 is dependent on Thus, should prevent maintaining small fragmented The...

10.1073/pnas.1301951110 article EN Proceedings of the National Academy of Sciences 2013-07-02

Loss of mitochondrial membrane potential (ΔΨm) triggers dramatic structural changes in mitochondria from a tubular to globular shape, referred as fragmentation; the resulting are called swelled or ring/doughnut mitochondria. We evaluated early period during ΔΨm loss-induced transformation after carbonyl cyanide m-chlorophenyl hydrazine (CCCP) administration using newly developed correlative microscopic method combined with fluorescence live imaging and volume electron microscopy. found that...

10.1038/s41598-017-18582-6 article EN cc-by Scientific Reports 2018-01-04

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

A protein that mediates mitochondrial fusion also suppresses innate immune responses to viral infection.

10.1126/scisignal.2000287 article EN Science Signaling 2009-08-18

Regulated intramembrane proteolysis is a widely conserved mechanism for controlling diverse biological processes. Considering that irreversible, it must be precisely regulated in context-dependent manner. Here, we show phosphoglycerate mutase 5 (PGAM5), mitochondrial Ser/Thr protein phosphatase, cleaved its N-terminal transmembrane domain response to membrane potential (ΔΨm) loss. This ΔΨm loss-dependent cleavage of PGAM5 was mediated by presenilin-associated rhomboid-like (PARL). PARL...

10.1074/jbc.m112.357509 article EN cc-by Journal of Biological Chemistry 2012-08-23

Mitochondria are dynamic organelles, and their fusion fission regulate cellular signaling, development, mitochondrial homeostasis, including DNA (mtDNA) distribution. Cardiac myocytes have a specialized cytoplasmic structure where large mitochondria aligned into tightly packed myofibril bundles; however, recent studies revealed that dynamics also plays an important role in the formation maintenance of cardiomyocytes. Here, we precisely analyzed vivo. The GTPase, Drp1, is highly expressed...

10.1128/mcb.01054-14 article EN Molecular and Cellular Biology 2014-10-28

In yeast, C-tail-anchored mitochondrial outer membrane protein Fis1 recruits the mitochondrial-fission-regulating GTPase Dnm1 to fission sites. However, function of its mammalian homologue remains enigmatic because it has been reported be dispensable for recruitment Drp1, a Dnm1. We identified TBC1D15 as Fis1-binding in HeLa cell extracts. Immunoprecipitation revealed that efficiently interacts with but not Drp1. Bacterially expressed and formed direct stable complex. Exogenously localized...

10.1242/jcs.111211 article EN Journal of Cell Science 2012-10-18
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