RapamycinFungusV1, Main, Exploration, bibRecord, 001435

Exit from the Golgi is required for the expansion of the autophagosomal phagophore in yeast Saccharomyces cerevisiae.

Identifieur interne : 001435 ( Main/Exploration ); précédent : 001434; suivant : 001436

Exit from the Golgi is required for the expansion of the autophagosomal phagophore in yeast Saccharomyces cerevisiae.

Auteurs : Aniek Van Der Vaart [Pays-Bas] ; Janice Griffith ; Fulvio Reggiori

Source :

Molecular biology of the cell [ 1939-4586 ] ; 2010.

RBID : pubmed:20444982

Descripteurs français

English descriptors

KwdEn :
- ADP-Ribosylation Factor 1 (genetics), ADP-Ribosylation Factor 1 (metabolism), ADP-Ribosylation Factors (genetics), ADP-Ribosylation Factors (metabolism), Antifungal Agents (pharmacology), Autophagy (physiology), Autophagy-Related Protein 8 Family (MeSH), Golgi Apparatus (metabolism), Golgi Apparatus (ultrastructure), Guanine Nucleotide Exchange Factors (genetics), Guanine Nucleotide Exchange Factors (metabolism), Intracellular Membranes (metabolism), Intracellular Membranes (ultrastructure), Microtubule-Associated Proteins (genetics), Microtubule-Associated Proteins (metabolism), Phagosomes (metabolism), Phagosomes (ultrastructure), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (metabolism), Saccharomyces cerevisiae (cytology), Saccharomyces cerevisiae (drug effects), Saccharomyces cerevisiae (physiology), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Sirolimus (pharmacology), Vacuoles (metabolism).
MESH :
- chemical , genetics : ADP-Ribosylation Factor 1, ADP-Ribosylation Factors, Guanine Nucleotide Exchange Factors, Microtubule-Associated Proteins, Recombinant Fusion Proteins, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : ADP-Ribosylation Factor 1, ADP-Ribosylation Factors, Guanine Nucleotide Exchange Factors, Microtubule-Associated Proteins, Recombinant Fusion Proteins, Saccharomyces cerevisiae Proteins.
- chemical , pharmacology : Antifungal Agents, Sirolimus.
- cytology : Saccharomyces cerevisiae.
- drug effects : Saccharomyces cerevisiae.
- metabolism : Golgi Apparatus, Intracellular Membranes, Phagosomes, Vacuoles.
- physiology : Autophagy, Saccharomyces cerevisiae.
- ultrastructure : Golgi Apparatus, Intracellular Membranes, Phagosomes.
- chemical : Autophagy-Related Protein 8 Family.

Abstract

The delivery of proteins and organelles to the vacuole by autophagy involves membrane rearrangements that result in the formation of large vesicles called autophagosomes. The mechanism underlying autophagosome biogenesis and the origin of the membranes composing these vesicles remains largely unclear. We have investigated the role of the Golgi complex in autophagy and have determined that in yeast, activation of ADP-ribosylation factor (Arf)1 and Arf2 GTPases by Sec7, Gea1, and Gea2 is essential for this catabolic process. The two main events catalyzed by these components, the biogenesis of COPI- and clathrin-coated vesicles, do not play a critical role in autophagy. Analysis of the sec7 strain under starvation conditions revealed that the autophagy machinery is correctly assembled and the precursor membrane cisterna of autophagosomes, the phagophore, is normally formed. However, the expansion of the phagophore into an autophagosome is severely impaired. Our data show that the Golgi complex plays a crucial role in supplying the lipid bilayers necessary for the biogenesis of double-membrane vesicles possibly through a new class of transport carriers or a new mechanism.

DOI: 10.1091/mbc.e09-04-0345
PubMed: 20444982
PubMed Central: PMC2893990

Affiliations:

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

to stream Main, to step Corpus: 001411
to stream Main, to step Curation: 001411

Le document en format XML

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<term>Famille de la protéine-8 associée à l'autophagie (MeSH)</term>
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<term>Protéines de fusion recombinantes</term>
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<term>Intracellular Membranes</term>
<term>Phagosomes</term>
<term>Vacuoles</term>
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<front><div type="abstract" xml:lang="en">The delivery of proteins and organelles to the vacuole by autophagy involves membrane rearrangements that result in the formation of large vesicles called autophagosomes. The mechanism underlying autophagosome biogenesis and the origin of the membranes composing these vesicles remains largely unclear. We have investigated the role of the Golgi complex in autophagy and have determined that in yeast, activation of ADP-ribosylation factor (Arf)1 and Arf2 GTPases by Sec7, Gea1, and Gea2 is essential for this catabolic process. The two main events catalyzed by these components, the biogenesis of COPI- and clathrin-coated vesicles, do not play a critical role in autophagy. Analysis of the sec7 strain under starvation conditions revealed that the autophagy machinery is correctly assembled and the precursor membrane cisterna of autophagosomes, the phagophore, is normally formed. However, the expansion of the phagophore into an autophagosome is severely impaired. Our data show that the Golgi complex plays a crucial role in supplying the lipid bilayers necessary for the biogenesis of double-membrane vesicles possibly through a new class of transport carriers or a new mechanism.</div>
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Exit from the Golgi is required for the expansion of the autophagosomal phagophore in yeast Saccharomyces cerevisiae.

Exit from the Golgi is required for the expansion of the autophagosomal phagophore in yeast Saccharomyces cerevisiae.

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