Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Ubiquitin-mediated targeting of a mutant plasma membrane ATPase, Pma1-7, to the endosomal/vacuolar system in yeast.

Molecular biology of the cell - 1 May 2004

Pizzirusso Maddalena, Chang Amy

Abstract excerpt

Pma1-7 is a mutant plasma membrane ATPase that is impaired in targeting to the cell surface at 37 degrees C and is delivered instead to the endosomal/vacuolar pathway for degradation. We have proposed that Pma1-7 is a substrate for a Golgibased quality control mechanism. By contrast with wild-type Pma1, Pma1-7 is ubiquitinated. Ubiquitination and endosomal targeting of Pma1-7 is dependent on the Rsp5-Bul1-Bul2...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Endosomal Sorting Complexes Required for Transport
Share to Endosomes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Golgi Apparatus

Share to Protein Sorting Signals

Share to Proton-Translocating ATPases

Share to Ubiquitin

Share to Ubiquitin-Protein Ligase Complexes

Share to Vacuoles

Source

Open in PubMed Open full text

Identifiers

PMID: 15020711
DOI: 10.1091/mbc.e03-10-0727
PMCID: PMC404032

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Ubiquitin-mediated targeting of a mutant plasma membrane ATPase, Pma1-7, to the endosomal/vacuolar system in yeast.PMID 15020711Read ↗

An endosome-to-plasma membrane pathway involved in trafficking of a mutant plasma membrane ATPase in yeast.Semantic proximity Read ↗

Loss of vacuolar H+-ATPase activity in organelles signals ubiquitination and endocytosis of the yeast plasma membrane proton pump Pma1p.Semantic proximity Read ↗

Multiple degradation pathways for misfolded mutants of the yeast plasma membrane ATPase, Pma1.Semantic proximity Read ↗

Compensatory Internalization of Pma1 in V-ATPase Mutants in Saccharomyces cerevisiae Requires Calcium- and Glucose-Sensitive Phosphatases.Semantic proximity Read ↗

Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system.Semantic proximity Read ↗

Sphingoid base synthesis is required for oligomerization and cell surface stability of the yeast plasma membrane ATPase, Pma1.Semantic proximity Read ↗

Eps1, a novel PDI-related protein involved in ER quality control in yeast.Semantic proximity Read ↗

Efficient degradation of misfolded mutant Pma1 by endoplasmic reticulum-associated degradation requires Atg19 and the Cvt/autophagy pathway.Semantic proximity Read ↗

Ubiquitin chain variability directs substrates of the Tul1 ubiquitin ligase complex to different degradation pathways.Semantic proximity Read ↗

Towards defining the substrate of orphan P5A-ATPases.Semantic proximity Read ↗

ULK1 phosphorylates Sec23A and mediates autophagy-induced inhibition of ER-to-Golgi trafficSemantic proximity Read ↗

Multivesicular body sorting: ubiquitin ligase Rsp5 is required for the modification and sorting of carboxypeptidase S.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.