RapamycinFungusV1, Main, Exploration, bibRecord, 001374

Trafficking and signaling in mammalian autophagy.

Identifieur interne : 001374 ( Main/Exploration ); précédent : 001373; suivant : 001375

Trafficking and signaling in mammalian autophagy.

Auteurs : Sharon A. Tooze [Royaume-Uni] ; Harold B J. Jefferies ; Eyal Kalie ; Andrea Longatti ; Fiona E. Mcalpine ; Nicole C. Mcknight ; Andrea Orsi ; Hannah E J. Polson ; Minoo Razi ; Deborah J. Robinson ; Jemma L. Webber

Source :

IUBMB life [ 1521-6551 ] ; 2010.

RBID : pubmed:20552641

Descripteurs français

English descriptors

KwdEn :
- Adaptor Proteins, Signal Transducing (physiology), Autophagy (physiology), Autophagy-Related Protein-1 Homolog (MeSH), Autophagy-Related Proteins (MeSH), Carrier Proteins (metabolism), Humans (MeSH), Intracellular Signaling Peptides and Proteins (physiology), Mechanistic Target of Rapamycin Complex 1 (MeSH), Membrane Proteins (physiology), Models, Biological (MeSH), Multiprotein Complexes (MeSH), Phagosomes (physiology), Phosphatidylinositol 3-Kinases (physiology), Phosphatidylinositol Phosphates (metabolism), Protein-Serine-Threonine Kinases (physiology), Proteins (MeSH), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (physiology), TOR Serine-Threonine Kinases (MeSH), Transcription Factors (physiology).
MESH :
- chemical , metabolism : Carrier Proteins, Phosphatidylinositol Phosphates.
- chemical , physiology : Adaptor Proteins, Signal Transducing, Intracellular Signaling Peptides and Proteins, Membrane Proteins, Phosphatidylinositol 3-Kinases, Protein-Serine-Threonine Kinases, Saccharomyces cerevisiae Proteins, Transcription Factors.
- metabolism : Saccharomyces cerevisiae.
- physiology : Autophagy, Phagosomes.
- chemical : Autophagy-Related Protein-1 Homolog, Autophagy-Related Proteins, Humans, Mechanistic Target of Rapamycin Complex 1, Models, Biological, Multiprotein Complexes, Proteins, TOR Serine-Threonine Kinases.

Abstract

Macroautophagy, here called autophagy, is literally a "self-eating" catabolic process, which is evolutionarily conserved. Autophagy is initiated by cellular stress pathways, resulting in the sequestration or engulfment of cytosolic proteins, membranes, and organelles in a double membrane structure that fuses with endosomes and lysosomes, thus delivering the sequestered material for degradation. Autophagy is implicated in a number of human diseases, many of which can either be characterized by an imbalance in protein, organelle, or cellular homeostasis, ultimately resulting in an alteration of the autophagic response. Here, we will review the recent progress made in understanding the induction of autophagy, with emphasis on the contributions from our laboratory.

DOI: 10.1002/iub.334
PubMed: 20552641

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 001399
to stream Main, to step Curation: 001399

Le document en format XML

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<term>Autophagy-Related Proteins (MeSH)</term>
<term>Carrier Proteins (metabolism)</term>
<term>Humans (MeSH)</term>
<term>Intracellular Signaling Peptides and Proteins (physiology)</term>
<term>Mechanistic Target of Rapamycin Complex 1 (MeSH)</term>
<term>Membrane Proteins (physiology)</term>
<term>Models, Biological (MeSH)</term>
<term>Multiprotein Complexes (MeSH)</term>
<term>Phagosomes (physiology)</term>
<term>Phosphatidylinositol 3-Kinases (physiology)</term>
<term>Phosphatidylinositol Phosphates (metabolism)</term>
<term>Protein-Serine-Threonine Kinases (physiology)</term>
<term>Proteins (MeSH)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Saccharomyces cerevisiae Proteins (physiology)</term>
<term>TOR Serine-Threonine Kinases (MeSH)</term>
<term>Transcription Factors (physiology)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Autophagie (physiologie)</term>
<term>Complexe-1 cible mécanistique de la rapamycine (MeSH)</term>
<term>Complexes multiprotéiques (MeSH)</term>
<term>Facteurs de transcription (physiologie)</term>
<term>Homologue de la protéine-1 associée à l'autophagie (MeSH)</term>
<term>Humains (MeSH)</term>
<term>Modèles biologiques (MeSH)</term>
<term>Phagosomes (physiologie)</term>
<term>Phosphates phosphatidylinositol (métabolisme)</term>
<term>Phosphatidylinositol 3-kinases (physiologie)</term>
<term>Protein-Serine-Threonine Kinases (physiologie)</term>
<term>Protéines (MeSH)</term>
<term>Protéines adaptatrices de la transduction du signal (physiologie)</term>
<term>Protéines associées à l'autophagie (MeSH)</term>
<term>Protéines de Saccharomyces cerevisiae (physiologie)</term>
<term>Protéines de transport (métabolisme)</term>
<term>Protéines et peptides de signalisation intracellulaire (physiologie)</term>
<term>Protéines membranaires (physiologie)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
<term>Sérine-thréonine kinases TOR (MeSH)</term>
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<term>Phosphatidylinositol 3-Kinases</term>
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<term>Saccharomyces cerevisiae Proteins</term>
<term>Transcription Factors</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Phosphates phosphatidylinositol</term>
<term>Protéines de transport</term>
<term>Saccharomyces cerevisiae</term>
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<term>Facteurs de transcription</term>
<term>Phagosomes</term>
<term>Phosphatidylinositol 3-kinases</term>
<term>Protein-Serine-Threonine Kinases</term>
<term>Protéines adaptatrices de la transduction du signal</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines et peptides de signalisation intracellulaire</term>
<term>Protéines membranaires</term>
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<term>Phagosomes</term>
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<term>Autophagy-Related Proteins</term>
<term>Humans</term>
<term>Mechanistic Target of Rapamycin Complex 1</term>
<term>Models, Biological</term>
<term>Multiprotein Complexes</term>
<term>Proteins</term>
<term>TOR Serine-Threonine Kinases</term>
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<term>Complexes multiprotéiques</term>
<term>Homologue de la protéine-1 associée à l'autophagie</term>
<term>Humains</term>
<term>Modèles biologiques</term>
<term>Protéines</term>
<term>Protéines associées à l'autophagie</term>
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<front><div type="abstract" xml:lang="en">Macroautophagy, here called autophagy, is literally a "self-eating" catabolic process, which is evolutionarily conserved. Autophagy is initiated by cellular stress pathways, resulting in the sequestration or engulfment of cytosolic proteins, membranes, and organelles in a double membrane structure that fuses with endosomes and lysosomes, thus delivering the sequestered material for degradation. Autophagy is implicated in a number of human diseases, many of which can either be characterized by an imbalance in protein, organelle, or cellular homeostasis, ultimately resulting in an alteration of the autophagic response. Here, we will review the recent progress made in understanding the induction of autophagy, with emphasis on the contributions from our laboratory.</div>
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<Abstract><AbstractText>Macroautophagy, here called autophagy, is literally a "self-eating" catabolic process, which is evolutionarily conserved. Autophagy is initiated by cellular stress pathways, resulting in the sequestration or engulfment of cytosolic proteins, membranes, and organelles in a double membrane structure that fuses with endosomes and lysosomes, thus delivering the sequestered material for degradation. Autophagy is implicated in a number of human diseases, many of which can either be characterized by an imbalance in protein, organelle, or cellular homeostasis, ultimately resulting in an alteration of the autophagic response. Here, we will review the recent progress made in understanding the induction of autophagy, with emphasis on the contributions from our laboratory.</AbstractText>
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<ForeName>Sharon A</ForeName>
<Initials>SA</Initials>
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<name sortKey="Longatti, Andrea" sort="Longatti, Andrea" uniqKey="Longatti A" first="Andrea" last="Longatti">Andrea Longatti</name>
<name sortKey="Mcalpine, Fiona E" sort="Mcalpine, Fiona E" uniqKey="Mcalpine F" first="Fiona E" last="Mcalpine">Fiona E. Mcalpine</name>
<name sortKey="Mcknight, Nicole C" sort="Mcknight, Nicole C" uniqKey="Mcknight N" first="Nicole C" last="Mcknight">Nicole C. Mcknight</name>
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<name sortKey="Polson, Hannah E J" sort="Polson, Hannah E J" uniqKey="Polson H" first="Hannah E J" last="Polson">Hannah E J. Polson</name>
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   |texte=   Trafficking and signaling in mammalian autophagy.
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	Serveur d'exploration sur la rapamycine et les champignons
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Serveur d'exploration sur la rapamycine et les champignons

Trafficking and signaling in mammalian autophagy.

Trafficking and signaling in mammalian autophagy.

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