RapamycinFungusV1, Main, Exploration, bibRecord, 000049

Selective autophagy degrades nuclear pore complexes.

Identifieur interne : 000049 ( Main/Exploration ); précédent : 000048; suivant : 000050

Selective autophagy degrades nuclear pore complexes.

Auteurs : Chia-Wei Lee [Allemagne] ; Florian Wilfling [Allemagne] ; Paolo Ronchi [Allemagne] ; Matteo Allegretti [Allemagne] ; Shyamal Mosalaganti [Allemagne] ; Stefan Jentsch [Allemagne] ; Martin Beck [Allemagne] ; Boris Pfander [Allemagne]

Source :

Nature cell biology [ 1476-4679 ] ; 2020.

RBID : pubmed:32029894

Descripteurs français

English descriptors

KwdEn :
- Active Transport, Cell Nucleus (drug effects), Amino Acid Sequence (MeSH), Autophagy (drug effects), Autophagy (genetics), Autophagy-Related Protein 8 Family (genetics), Autophagy-Related Protein 8 Family (metabolism), Cytoplasm (metabolism), Gene Expression Regulation, Fungal (MeSH), Glucose (pharmacology), Multiprotein Complexes (genetics), Multiprotein Complexes (metabolism), Nitrogen (pharmacology), Nuclear Pore (metabolism), Nuclear Pore Complex Proteins (genetics), Nuclear Pore Complex Proteins (metabolism), Protein Isoforms (genetics), Protein Isoforms (metabolism), Proteolysis (drug effects), Saccharomyces cerevisiae (drug effects), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae (ultrastructure), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Sirolimus (pharmacology).
MESH :
- chemical , genetics : Autophagy-Related Protein 8 Family, Multiprotein Complexes, Nuclear Pore Complex Proteins, Protein Isoforms, Saccharomyces cerevisiae Proteins.
- drug effects : Active Transport, Cell Nucleus, Autophagy, Proteolysis, Saccharomyces cerevisiae.
- genetics : Autophagy, Saccharomyces cerevisiae.
- chemical , metabolism : Autophagy-Related Protein 8 Family, Cytoplasm, Multiprotein Complexes, Nuclear Pore, Nuclear Pore Complex Proteins, Protein Isoforms, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins.
- chemical , pharmacology : Glucose, Nitrogen, Sirolimus.
- ultrastructure : Saccharomyces cerevisiae.
- Amino Acid Sequence, Gene Expression Regulation, Fungal.

Abstract

Nuclear pore complexes (NPCs) are very large proteinaceous assemblies that consist of more than 500 individual proteins^1,2. NPCs are essential for nucleocytoplasmic transport of different cellular components, and disruption of the integrity of NPCs has been linked to aging, cancer and neurodegenerative diseases^3-7. However, the mechanism by which membrane-embedded NPCs are turned over is currently unknown. Here we show that, after nitrogen starvation or genetic interference with the architecture of NPCs, nucleoporins are rapidly degraded in the budding yeast Saccharomyces cerevisiae. We demonstrate that NPC turnover involves vacuolar proteases and the core autophagy machinery. Autophagic degradation is mediated by the cytoplasmically exposed Nup159, which serves as intrinsic cargo receptor and directly binds to the autophagy marker protein Atg8. Autophagic degradation of NPCs is therefore inducible, enabling the removal of individual NPCs from the nuclear envelope.

DOI: 10.1038/s41556-019-0459-2
PubMed: 32029894

Affiliations:

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Le document en format XML

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<series><title level="j">Nature cell biology</title>
<idno type="eISSN">1476-4679</idno>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Active Transport, Cell Nucleus (drug effects)</term>
<term>Amino Acid Sequence (MeSH)</term>
<term>Autophagy (drug effects)</term>
<term>Autophagy (genetics)</term>
<term>Autophagy-Related Protein 8 Family (genetics)</term>
<term>Autophagy-Related Protein 8 Family (metabolism)</term>
<term>Cytoplasm (metabolism)</term>
<term>Gene Expression Regulation, Fungal (MeSH)</term>
<term>Glucose (pharmacology)</term>
<term>Multiprotein Complexes (genetics)</term>
<term>Multiprotein Complexes (metabolism)</term>
<term>Nitrogen (pharmacology)</term>
<term>Nuclear Pore (metabolism)</term>
<term>Nuclear Pore Complex Proteins (genetics)</term>
<term>Nuclear Pore Complex Proteins (metabolism)</term>
<term>Protein Isoforms (genetics)</term>
<term>Protein Isoforms (metabolism)</term>
<term>Proteolysis (drug effects)</term>
<term>Saccharomyces cerevisiae (drug effects)</term>
<term>Saccharomyces cerevisiae (genetics)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Saccharomyces cerevisiae (ultrastructure)</term>
<term>Saccharomyces cerevisiae Proteins (genetics)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
<term>Sirolimus (pharmacology)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Autophagie (effets des médicaments et des substances chimiques)</term>
<term>Autophagie (génétique)</term>
<term>Azote (pharmacologie)</term>
<term>Complexe protéique du pore nucléaire (génétique)</term>
<term>Complexe protéique du pore nucléaire (métabolisme)</term>
<term>Complexes multiprotéiques (génétique)</term>
<term>Complexes multiprotéiques (métabolisme)</term>
<term>Cytoplasme (métabolisme)</term>
<term>Famille de la protéine-8 associée à l'autophagie (génétique)</term>
<term>Famille de la protéine-8 associée à l'autophagie (métabolisme)</term>
<term>Glucose (pharmacologie)</term>
<term>Isoformes de protéines (génétique)</term>
<term>Isoformes de protéines (métabolisme)</term>
<term>Pore nucléaire (métabolisme)</term>
<term>Protéines de Saccharomyces cerevisiae (génétique)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Protéolyse (effets des médicaments et des substances chimiques)</term>
<term>Régulation de l'expression des gènes fongiques (MeSH)</term>
<term>Saccharomyces cerevisiae (effets des médicaments et des substances chimiques)</term>
<term>Saccharomyces cerevisiae (génétique)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
<term>Saccharomyces cerevisiae (ultrastructure)</term>
<term>Sirolimus (pharmacologie)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Transport nucléaire actif (effets des médicaments et des substances chimiques)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Autophagy-Related Protein 8 Family</term>
<term>Multiprotein Complexes</term>
<term>Nuclear Pore Complex Proteins</term>
<term>Protein Isoforms</term>
<term>Saccharomyces cerevisiae Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Active Transport, Cell Nucleus</term>
<term>Autophagy</term>
<term>Proteolysis</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Autophagie</term>
<term>Protéolyse</term>
<term>Saccharomyces cerevisiae</term>
<term>Transport nucléaire actif</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Autophagy</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Autophagie</term>
<term>Complexe protéique du pore nucléaire</term>
<term>Complexes multiprotéiques</term>
<term>Famille de la protéine-8 associée à l'autophagie</term>
<term>Isoformes de protéines</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Autophagy-Related Protein 8 Family</term>
<term>Cytoplasm</term>
<term>Multiprotein Complexes</term>
<term>Nuclear Pore</term>
<term>Nuclear Pore Complex Proteins</term>
<term>Protein Isoforms</term>
<term>Saccharomyces cerevisiae</term>
<term>Saccharomyces cerevisiae Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Complexe protéique du pore nucléaire</term>
<term>Complexes multiprotéiques</term>
<term>Cytoplasme</term>
<term>Famille de la protéine-8 associée à l'autophagie</term>
<term>Isoformes de protéines</term>
<term>Pore nucléaire</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Azote</term>
<term>Glucose</term>
<term>Sirolimus</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Glucose</term>
<term>Nitrogen</term>
<term>Sirolimus</term>
</keywords>
<keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Gene Expression Regulation, Fungal</term>
</keywords>
<keywords scheme="MESH" qualifier="ultrastructure" xml:lang="fr"><term>Régulation de l'expression des gènes fongiques</term>
<term>Saccharomyces cerevisiae</term>
<term>Séquence d'acides aminés</term>
</keywords>
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<front><div type="abstract" xml:lang="en">Nuclear pore complexes (NPCs) are very large proteinaceous assemblies that consist of more than 500 individual proteins<sup>1,2</sup>
. NPCs are essential for nucleocytoplasmic transport of different cellular components, and disruption of the integrity of NPCs has been linked to aging, cancer and neurodegenerative diseases<sup>3-7</sup>
. However, the mechanism by which membrane-embedded NPCs are turned over is currently unknown. Here we show that, after nitrogen starvation or genetic interference with the architecture of NPCs, nucleoporins are rapidly degraded in the budding yeast Saccharomyces cerevisiae. We demonstrate that NPC turnover involves vacuolar proteases and the core autophagy machinery. Autophagic degradation is mediated by the cytoplasmically exposed Nup159, which serves as intrinsic cargo receptor and directly binds to the autophagy marker protein Atg8. Autophagic degradation of NPCs is therefore inducible, enabling the removal of individual NPCs from the nuclear envelope.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">32029894</PMID>
<DateCompleted><Year>2020</Year>
<Month>04</Month>
<Day>15</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>04</Month>
<Day>15</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1476-4679</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>22</Volume>
<Issue>2</Issue>
<PubDate><Year>2020</Year>
<Month>02</Month>
</PubDate>
</JournalIssue>
<Title>Nature cell biology</Title>
<ISOAbbreviation>Nat Cell Biol</ISOAbbreviation>
</Journal>
<ArticleTitle>Selective autophagy degrades nuclear pore complexes.</ArticleTitle>
<Pagination><MedlinePgn>159-166</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1038/s41556-019-0459-2</ELocationID>
<Abstract><AbstractText>Nuclear pore complexes (NPCs) are very large proteinaceous assemblies that consist of more than 500 individual proteins<sup>1,2</sup>
. NPCs are essential for nucleocytoplasmic transport of different cellular components, and disruption of the integrity of NPCs has been linked to aging, cancer and neurodegenerative diseases<sup>3-7</sup>
. However, the mechanism by which membrane-embedded NPCs are turned over is currently unknown. Here we show that, after nitrogen starvation or genetic interference with the architecture of NPCs, nucleoporins are rapidly degraded in the budding yeast Saccharomyces cerevisiae. We demonstrate that NPC turnover involves vacuolar proteases and the core autophagy machinery. Autophagic degradation is mediated by the cytoplasmically exposed Nup159, which serves as intrinsic cargo receptor and directly binds to the autophagy marker protein Atg8. Autophagic degradation of NPCs is therefore inducible, enabling the removal of individual NPCs from the nuclear envelope.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lee</LastName>
<ForeName>Chia-Wei</ForeName>
<Initials>CW</Initials>
<AffiliationInfo><Affiliation>Molecular Cell Biology, Max Planck Institute of Biochemistry, Martinsried, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Wilfling</LastName>
<ForeName>Florian</ForeName>
<Initials>F</Initials>
<Identifier Source="ORCID">0000-0002-6559-7261</Identifier>
<AffiliationInfo><Affiliation>Molecular Cell Biology, Max Planck Institute of Biochemistry, Martinsried, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Ronchi</LastName>
<ForeName>Paolo</ForeName>
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<AffiliationInfo><Affiliation>Molecular Sociology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany. martin.beck@biophys.mpg.de.</Affiliation>
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<AffiliationInfo><Affiliation>DNA Replication and Genome Integrity, Max Planck Institute of Biochemistry, Martinsried, Germany. bpfander@biochem.mpg.de.</Affiliation>
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   |texte=   Selective autophagy degrades nuclear pore complexes.
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	Serveur d'exploration sur la rapamycine et les champignons
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.

Serveur d'exploration sur la rapamycine et les champignons

Selective autophagy degrades nuclear pore complexes.

Selective autophagy degrades nuclear pore complexes.

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