CovidV1, Main, Exploration, bibRecord, 001640

Glycosylation and processing of prepro-α-factor through the yeast secretory pathway

Identifieur interne : 001640 ( Main/Exploration ); précédent : 001639; suivant : 001641

Glycosylation and processing of prepro-α-factor through the yeast secretory pathway

Auteurs : David Julius [États-Unis] ; Randy Schekman [États-Unis] ; Jeremy Thorner [États-Unis]

Source :

Cell [ 0092-8674 ] ; 1984.

RBID : ISTEX:A51AA3F9D0779712D69A07B6CED82E83D75856B0

English descriptors

Teeft :
- Animal cells, Biol, Biosynthesis, Brake, Carbohydrate, Carbohydrate chains, Cell lysates, Centrifugation, Cerevisiae, Chem, Cleavage, Core oligosaccharides, Endo, Endoplasmic reticulum, Entire secretory pathway, Equal portions, Equal volume, Esmon, Experimental procedures, Field mata, Glycoprotein, Glycosyl chains, Glycosylated, Glycosylated form, Glycosylated precursor, Glycosylation, Golgi, Golgi apparatus, Granule, Immunoprecipitated, Invertase, Lysates, Mata, Mata cells, Mata secl8, Mature pheromone, Mature secretory granules, Microsome, Minimal medium, Molecular weight, Mutant, Mutation, Novick, Oligosaccharide, Oligosaccharide chains, Pancreas, Pancreas microsomes, Pathway, Peptide, Pheromone, Polypeptide, Precursor, Proteolytic, Proteolytic processing, Restrictive temperature, Saccharomyces, Saccharomyces cerevisiae, Same medium, Schekman, Secl, Secl8, Secl8 cells, Secretion, Secretory, Secretory granules, Secretory pathway, Secretory vesicles, Signal sequence, Thorner, Translation product, Tunicamycin, Tunicamycin treatment, Vesicle, Water bath, Wheat germ, Yeast, Yeast secretory pathway.

Abstract

Abstract: Events in the synthesis and processing of prepro-α-factor have been assessed with the aid of mutants blocked at various stages in the yeast secretory pathway. In normal cells treated with tunicamycin, a precursor accumulates which is identical in molecular weight to the primary translation product synthesized in vitro. At the restrictive temperature in a mutant blocked early in the pathway (sec53), a molecule of similar molecular weight accumulates. In mutants affecting translocation into (sec59) and passage from (sec18) the endoplasmic reticulum, a glycosylated form of the precursor containing three N-linked core oligosaccharides accumulates; however, it appears that the signal peptide is not removed. The glycosylated precursor first experiences proteolytic processing when accumulated in a mutant (sec7) blocked at the stage of the Golgi apparatus. Substantially greater amounts of the mature pheromone are seen in mutants that accumulate secretory vesicles (sec1, sec2, sec3, sec5).

Url:

https://api.istex.fr/ark:/67375/6H6-N183QWFH-4/fulltext.pdf

DOI: 10.1016/0092-8674(84)90224-1

Affiliations:

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

to stream Istex, to step Corpus: 000693
to stream Istex, to step Curation: 000673
to stream Istex, to step Checkpoint: 000767
to stream Main, to step Merge: 001667
to stream Main, to step Curation: 001640

Le document en format XML

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<term>Carbohydrate chains</term>
<term>Cell lysates</term>
<term>Centrifugation</term>
<term>Cerevisiae</term>
<term>Chem</term>
<term>Cleavage</term>
<term>Core oligosaccharides</term>
<term>Endo</term>
<term>Endoplasmic reticulum</term>
<term>Entire secretory pathway</term>
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<term>Equal volume</term>
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<term>Experimental procedures</term>
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<term>Saccharomyces cerevisiae</term>
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<term>Schekman</term>
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<term>Secl8</term>
<term>Secl8 cells</term>
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<term>Secretory</term>
<term>Secretory granules</term>
<term>Secretory pathway</term>
<term>Secretory vesicles</term>
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<term>Thorner</term>
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<term>Tunicamycin</term>
<term>Tunicamycin treatment</term>
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<front><div type="abstract" xml:lang="en">Abstract: Events in the synthesis and processing of prepro-α-factor have been assessed with the aid of mutants blocked at various stages in the yeast secretory pathway. In normal cells treated with tunicamycin, a precursor accumulates which is identical in molecular weight to the primary translation product synthesized in vitro. At the restrictive temperature in a mutant blocked early in the pathway (sec53), a molecule of similar molecular weight accumulates. In mutants affecting translocation into (sec59) and passage from (sec18) the endoplasmic reticulum, a glycosylated form of the precursor containing three N-linked core oligosaccharides accumulates; however, it appears that the signal peptide is not removed. The glycosylated precursor first experiences proteolytic processing when accumulated in a mutant (sec7) blocked at the stage of the Golgi apparatus. Substantially greater amounts of the mature pheromone are seen in mutants that accumulate secretory vesicles (sec1, sec2, sec3, sec5).</div>
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Glycosylation and processing of prepro-α-factor through the yeast secretory pathway

Glycosylation and processing of prepro-α-factor through the yeast secretory pathway

Source :

English descriptors

Abstract

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

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri