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Article

Monoubiquitination is sufficient to signal internalization of the maltose transporter in Saccharomyces cerevisiae.

Journal of bacteriology - 1 Jan 2000

Lucero P, Peñalver E, Vela L, Lagunas R

Abstract excerpt

Monoubiquitination of the 12-transmembrane segment (12-TMS) Saccharomyces cerevisiae maltose transporter promoted the maximal internalization rate of this protein. This modification is similar to that of the 7-TMS alpha-factor receptor but different from that of the 12-TMS uracil and general amino acid permeases. This result shows that binding of ubiquitin-Lys63 chains is not required for maximal internalization...

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Source

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Identifiers

PMID: 10613890
DOI: 10.1128/JB.182.1.241-243.2000
PMCID: PMC94267

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Monoubiquitination is sufficient to signal internalization of the maltose transporter in Saccharomyces cerevisiae.PMID 10613890Read ↗

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A PEST-like sequence mediates phosphorylation and efficient ubiquitination of yeast uracil permease.Semantic proximity Read ↗

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Clathrin and two components of the COPII complex, Sec23p and Sec24p, could be involved in endocytosis of the Saccharomyces cerevisiae maltose transporter.Semantic proximity Read ↗

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The ABC-transporter Ste6 accumulates in the plasma membrane in a ubiquitinated form in endocytosis mutants.Semantic proximity Read ↗

Homo-oligomeric complexes of the yeast alpha-factor pheromone receptor are functional units of endocytosis.Semantic proximity Read ↗

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