ArticleJournal of molecular biology2008
Peptide-based interactions with calnexin target misassembled membrane proteins into endoplasmic reticulum-derived multilamellar bodies.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 33 citations in OpenAlex.
- IER3IP1-mutations cause microcephaly by selective inhibition of ER-Golgi transport.Cellular and molecular life sciences : CMLS · 2024Article
- A transporter's doom or destiny:Frontiers in molecular neuroscience · 2024Review
- Overproduction of mycotoxin biosynthetic enzymes triggers Fusarium toxisome-shaped structure formation via endoplasmic reticulum remodeling.PLoS pathogens · 2024Article
- Article
- Functional and Biochemical Consequences of Disease Variants in Neurotransmitter Transporters: A Special Emphasis on Folding and Trafficking Deficits.Pharmacology & therapeutics · 2021Review
- Tropane-Based Ibogaine Analog Rescues Folding-Deficient Serotonin and Dopamine Transporters.ACS pharmacology & translational science · 2021Article
- IntEResting structures: formation and applications of organized smooth endoplasmic reticulum in plant cells.Plant physiology · 2021Article
- How to rescue misfolded SERT, DAT and NET: targeting conformational intermediates with atypical inhibitors and partial releasers.Biochemical Society transactions · 2019Review
- Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis.Chemical reviews · 2019Article
- Relax, Cool Down and Scaffold: How to Restore Surface Expression of Folding-Deficient Mutant GPCRs and SLC6 Transporters.International journal of molecular sciences · 2017Review
- An unfolding story: Small molecules remedy misfolded monoamine transporters.The international journal of biochemistry & cell biology · 2017Review
- When transporters fail to be transported: how to rescue folding-deficient SLC6 transporters.Journal of neurology & neuromedicine · 2016Article
- Model-Driven Understanding of Palmitoylation Dynamics: Regulated Acylation of the Endoplasmic Reticulum Chaperone Calnexin.PLoS computational biology · 2016Article
- A cytosolic relay of heat shock proteins HSP70-1A and HSP90β monitors the folding trajectory of the serotonin transporter.The Journal of biological chemistry · 2014Article
- Defining the blanks--pharmacochaperoning of SLC6 transporters and ABC transporters.Pharmacological research · 2014Review
- Recruitment of a cytoplasmic chaperone relay by the A2A adenosine receptor.The Journal of biological chemistry · 2013Article
- Article
- Psychiatric drugs bind to classical targets within early exocytotic pathways: therapeutic effects.Biological psychiatry · 2012Review
- Structural basis for the Trembler-J phenotype of Charcot-Marie-Tooth disease.Structure (London, England : 1993) · 2011Article
- Mutations in the carboxyl-terminal SEC24 binding motif of the serotonin transporter impair folding of the transporter.The Journal of biological chemistry · 2010Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Oligomeric assembly of neurotransmitter transporters is a prerequisite for their export from the endoplasmic reticulum (ER) and their subsequent delivery to the neuronal synapse. We previously identified mutations, e.g., in the gamma-aminobutyric acid (GABA) transporter-1 (GAT1), which disrupted assembly and caused retention of the transporter in the ER. Using one representative mutant, GAT1-E101D, we showed here that ER retention was due to association of the transporter with the ER chaperone calnexin: interaction with calnexin led to accumulation of GAT1 in concentric bodies corresponding to previously described multilamellar ER-derived structures. The transmembrane domain of calnexin was necessary and sufficient to direct the protein into these concentric bodies. Both yellow fluorescent protein-tagged versions of wild-type GAT1 and of the GAT1-E101D mutant remained in disperse (i.e., non-aggregated) form in these concentric bodies, because fluorescence recovered rapidly (t(1/2) approximately 500 ms) upon photobleaching. Fluorescence energy resonance transfer microscopy was employed to visualize a tight interaction of GAT1-E101D with calnexin. Recognition by calnexin occurred largely in a glycan-independent manner and, at least in part, at the level of the transmembrane domain. Our findings are consistent with a model in which the transmembrane segment of calnexin participates in chaperoning the inter- and intramolecular arrangement of hydrophobic segment in oligomeric proteins.
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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.