ArticlePloS one2009
Inefficient quality control of thermosensitive proteins on the plasma membrane.
Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed, 25 citations in OpenAlex.
- A two-tiered system for selective receptor and transporter protein degradation.PLoS genetics · 2022Article
- Volleying plasma membrane proteins from birth to death: Role of J-domain proteins.Frontiers in molecular biosciences · 2022Review
- Article
- The intralumenal fragment pathway mediates ESCRT-independent surface transporter down-regulation.Nature communications · 2018Article
- Hsp40/70/110 chaperones adapt nuclear protein quality control to serve cytosolic clients.The Journal of cell biology · 2018Article
- Pharmacoperones as Novel Therapeutics for Diverse Protein Conformational Diseases.Physiological reviews · 2018Review
- Degradation Signals for Ubiquitin-Proteasome Dependent Cytosolic Protein Quality Control (CytoQC) in Yeast.G3 (Bethesda, Md.) · 2016Article
- Protein quality control in the nucleus.Current opinion in cell biology · 2016Review
- Actin and endocytosis in budding yeast.Genetics · 2015Review
- Cellular maintenance of nuclear protein homeostasis.Cellular and molecular life sciences : CMLS · 2014Review
- Quality control: quality control at the plasma membrane: one mechanism does not fit all.The Journal of cell biology · 2014Review
- The Type II Hsp40 Sis1 cooperates with Hsp70 and the E3 ligase Ubr1 to promote degradation of terminally misfolded cytosolic protein.PloS one · 2013Article
- The endoplasmic reticulum-associated degradation pathways of budding yeast.Cold Spring Harbor perspectives in biology · 2012Review
- Failure of amino acid homeostasis causes cell death following proteasome inhibition.Molecular cell · 2012Article
- Selective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradation.Seminars in cell & developmental biology · 2012Review
- The yeast ubr1 ubiquitin ligase participates in a prominent pathway that targets cytosolic thermosensitive mutants for degradation.G3 (Bethesda, Md.) · 2012Article
- Exposed hydrophobicity is a key determinant of nuclear quality control degradation.Molecular biology of the cell · 2011Article
- Quality control for unfolded proteins at the plasma membrane.The Journal of cell biology · 2010Article
- A nucleus-based quality control mechanism for cytosolic proteins.Molecular biology of the cell · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
backgroundMisfolded proteins are generally recognised by cellular quality control machinery, which typically results in their ubiquitination and degradation. For soluble cytoplasmic proteins, degradation is mediated by the proteasome. Membrane proteins that fail to fold correctly are subject to ER associated degradation (ERAD), which involves their extraction from the membrane and subsequent proteasome-dependent destruction. Proteins with abnormal transmembrane domains can also be recognised in the Golgi or endosomal system and targeted for destruction in the vacuole/lysosome. It is much less clear what happens to membrane proteins that reach their destination, such as the cell surface, and then suffer damage. METHODOLOGY/PRINCIPAL
findingsWe have tested the ability of yeast cells to degrade membrane proteins to which temperature-sensitive cytoplasmic alleles of the Ura3 protein or of phage lambda repressor have been fused. In soluble form, these proteins are rapidly degraded upon temperature shift, in part due to the action of the Doa10 and San1 ubiquitin ligases and the proteasome. When tethered to the ER protein Use1, they are also degraded. However, when tethered to a plasma membrane protein such as Sso1 they escape degradation, either in the vacuole or by the proteasome. CONCLUSIONS/SIGNIFICANCE: Membrane proteins with a misfolded cytoplasmic domain appear not to be efficiently recognised and degraded once they have escaped the ER, even though their defective domains are exposed to the cytoplasm and potentially to cytoplasmic quality controls. Membrane tethering may provide a way to reduce degradation of unstable proteins.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.