ArticleThe EMBO journal2012
Palmitoylated calnexin is a key component of the ribosome-translocon complex.
Article in The EMBO journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.
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Who cites it
98 citing papers in PubMed, 181 citations in OpenAlex.
- ZDHHC5: a pivotal palmitoyltransferase orchestrating signaling networks - unraveling mechanisms and therapeutic horizons.Biomarker research · 2026Review
- Mechanisms controlling the plasma membrane targeting and the nanodomain organization of the plant SPFH protein HIR2.The Plant journal : for cell and molecular biology · 2026Article
- Identification of a lipid oxygen radical defense pathway and its epigenetic control.Nature communications · 2025Article
- Hepatitis B virus core protein promotes liver cancer progression by stabilizing CANX and suppressing IRF7 transcription.Acta pharmacologica Sinica · 2025Article
- Protein palmitoylation in hepatic diseases: Functional insights and therapeutic strategies.Journal of advanced research · 2025Review
- Lipid overload meets S-palmitoylation: a metabolic signalling nexus driving cardiovascular and heart disease.Cell communication and signaling : CCS · 2025Review
- Palmitoylation: an emerging therapeutic target bridging physiology and disease.Cellular & molecular biology letters · 2025Review
- ZDHHC9-mediated CD38 palmitoylation stabilizes CD38 expression and promotes pancreatic cancer growth.Communications biology · 2025Article
- TEX38 localizes ZDHHC19 to the plasma membrane and regulates sperm head morphogenesis in mice.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Review
- Cell Labeling with 15-YNE Is Useful for Tracking Protein Palmitoylation and Metabolic Lipid Flux in the Same Sample.Molecules (Basel, Switzerland) · 2025Article
- Palmitoylation in cancer: decoding its roles in signal transduction, tumor immunity, and emerging therapeutic opportunities.Frontiers in immunology · 2025Review
- Mechanism of NACHO-mediated assembly of pentameric ligand-gated ion channels.bioRxiv : the preprint server for biology · 2024Article
- Article
- Mechanisms and functions of protein S-acylation.Nature reviews. Molecular cell biology · 2024Review
- Refining S-acylation: Structure, regulation, dynamics, and therapeutic implications.The Journal of cell biology · 2023Article
- Competition for calnexin binding regulates secretion and turnover of misfolded GPI-anchored proteins.The Journal of cell biology · 2023Article
- Comparative membrane proteomics reveals diverse cell regulators concentrated at the nuclear envelope.Life science alliance · 2023Article
- Comparative membrane proteomics reveals diverse cell regulators concentrated at the nuclear envelope.bioRxiv : the preprint server for biology · 2023Article
- Calnexin, More Than Just a Molecular Chaperone.Cells · 2023Review
38 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A third of the human genome encodes N-glycosylated proteins. These are co-translationally translocated into the lumen/membrane of the endoplasmic reticulum (ER) where they fold and assemble before they are transported to their final destination. Here, we show that calnexin, a major ER chaperone involved in glycoprotein folding is palmitoylated and that this modification is mediated by the ER palmitoyltransferase DHHC6. This modification leads to the preferential localization of calnexin to the perinuclear rough ER, at the expense of ER tubules. Moreover, palmitoylation mediates the association of calnexin with the ribosome-translocon complex (RTC) leading to the formation of a supercomplex that recruits the actin cytoskeleton, leading to further stabilization of the assembly. When formation of the calnexin-RTC supercomplex was affected by DHHC6 silencing, mutation of calnexin palmitoylation sites or actin depolymerization, folding of glycoproteins was impaired. Our findings thus show that calnexin is a stable component of the RTC in a manner that is exquisitely dependent on its palmitoylation status. This association is essential for the chaperone to capture its client proteins as they emerge from the translocon, acquire their N-linked glycans and initiate folding.
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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.