RapamycinFungusV1, Main, Exploration, bibRecord, 000282

Methods for studying the regulation of membrane traffic by ubiquitin and the ESCRT pathway.

Identifieur interne : 000282 ( Main/Exploration ); précédent : 000281; suivant : 000283

Methods for studying the regulation of membrane traffic by ubiquitin and the ESCRT pathway.

Auteurs : Evan L. Guiney [États-Unis] ; Lu Zhu [États-Unis] ; Richa Sardana [États-Unis] ; Scott D. Emr [États-Unis] ; Matthew G. Baile [États-Unis]

Source :

Methods in enzymology [ 1557-7988 ] ; 2019.

RBID : pubmed:30910024

Descripteurs français

English descriptors

KwdEn :
- Endocytosis (MeSH), Endosomal Sorting Complexes Required for Transport (metabolism), Protein Transport (MeSH), Saccharomyces cerevisiae (cytology), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (metabolism), Signal Transduction (MeSH), Ubiquitin (metabolism), Ubiquitination (MeSH).
MESH :
- chemical , metabolism : Endosomal Sorting Complexes Required for Transport, Saccharomyces cerevisiae Proteins, Ubiquitin.
- cytology : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- Endocytosis, Protein Transport, Signal Transduction, Ubiquitination.

Abstract

Covalent modification of proteins with ubiquitin dynamically regulates their function and fate. The ubiquitination of most plasma membrane proteins initiates endocytosis and ESCRT-mediated sorting to the lysosomal lumen for degradation. Powerful genetic approaches in the budding yeast Saccharomyces cerevisiae have been particularly instrumental in the discovery and elucidation of these molecular mechanisms, which are conserved in all eukaryotes. Here we provide two detailed protocols and tools for studying ubiquitination-dependent membrane trafficking mechanisms in yeast. The first utilizes fusions between a protein of interest and an auxotrophic marker to screen for mutants that affect ubiquitin-mediated endocytosis. The second method artificially ubiquitinates a protein of interest, allowing downstream trafficking steps to be studied independently from the regulatory signals that initiate endocytosis.

DOI: 10.1016/bs.mie.2018.12.041
PubMed: 30910024

Affiliations:

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Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Endocytosis (MeSH)</term>
<term>Endosomal Sorting Complexes Required for Transport (metabolism)</term>
<term>Protein Transport (MeSH)</term>
<term>Saccharomyces cerevisiae (cytology)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
<term>Signal Transduction (MeSH)</term>
<term>Ubiquitin (metabolism)</term>
<term>Ubiquitination (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Complexes de tri endosomique requis pour le transport (métabolisme)</term>
<term>Endocytose (MeSH)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Saccharomyces cerevisiae (cytologie)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
<term>Transduction du signal (MeSH)</term>
<term>Transport des protéines (MeSH)</term>
<term>Ubiquitination (MeSH)</term>
<term>Ubiquitine (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Endosomal Sorting Complexes Required for Transport</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>Ubiquitin</term>
</keywords>
<keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Complexes de tri endosomique requis pour le transport</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Saccharomyces cerevisiae</term>
<term>Ubiquitine</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Endocytosis</term>
<term>Protein Transport</term>
<term>Signal Transduction</term>
<term>Ubiquitination</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Endocytose</term>
<term>Transduction du signal</term>
<term>Transport des protéines</term>
<term>Ubiquitination</term>
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<front><div type="abstract" xml:lang="en">Covalent modification of proteins with ubiquitin dynamically regulates their function and fate. The ubiquitination of most plasma membrane proteins initiates endocytosis and ESCRT-mediated sorting to the lysosomal lumen for degradation. Powerful genetic approaches in the budding yeast Saccharomyces cerevisiae have been particularly instrumental in the discovery and elucidation of these molecular mechanisms, which are conserved in all eukaryotes. Here we provide two detailed protocols and tools for studying ubiquitination-dependent membrane trafficking mechanisms in yeast. The first utilizes fusions between a protein of interest and an auxotrophic marker to screen for mutants that affect ubiquitin-mediated endocytosis. The second method artificially ubiquitinates a protein of interest, allowing downstream trafficking steps to be studied independently from the regulatory signals that initiate endocytosis.</div>
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<CopyrightInformation>© 2019 Elsevier Inc. All rights reserved.</CopyrightInformation>
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Methods for studying the regulation of membrane traffic by ubiquitin and the ESCRT pathway.

Methods for studying the regulation of membrane traffic by ubiquitin and the ESCRT pathway.

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