ArticleMolecular and cellular biology2000
H-ras but not K-ras traffics to the plasma membrane through the exocytic pathway.
Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 185 papers.
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Who cites it
185 citing papers in PubMed, 428 citations in OpenAlex.
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- Targeting the cell membrane in established and emerging model organisms.bioRxiv : the preprint server for biology · 2025Article
- Necroptosis in cancer: insight from epigenetic, post-transcriptional and post-translational modifications.Journal of hematology & oncology · 2025Review
- Spatiotemporal HNature communications · 2025Article
- Review
- S-acylation of NLRP3 provides a nigericin sensitive gating mechanism that controls access to the Golgi.eLife · 2024Article
- Genetically encodable biosensors for Ras activity.RSC chemical biology · 2024Review
- Identification of the growth cone as a probe and driver of neuronal migration in the injured brain.Nature communications · 2024Article
- Regulation of RAS palmitoyltransferases by accessory proteins and palmitoylation.Nature structural & molecular biology · 2024Article
- GOLGA7 is essential for NRAS trafficking from the Golgi to the plasma membrane but not for its palmitoylation.Cell communication and signaling : CCS · 2024Article
- Mediating kinase activity in Ras-mutant cancer: potential for an individualised approach?Frontiers in pharmacology · 2024Review
- Fibroblast-derived extracellular vesicles as trackable efficient transporters of an experimental nanodrug with fibrotic heart and lung targeting.Theranostics · 2024Article
- A new ferrocene derivative blocks K-Ras localization and function by oxidative modification at His95.Life science alliance · 2023Article
- CaaX-motif adjacent residues control G protein prenylation under suboptimal conditions.bioRxiv : the preprint server for biology · 2023Article
- Membrane phase separation drives responsive assembly of receptor signaling domains.Nature chemical biology · 2023Article
- CD59-Regulated Ras Compartmentalization Orchestrates Antitumor T-cell Immunity.Cancer immunology research · 2022Article
- TGFβ-induced changes in membrane curvature influence Ras oncoprotein membrane localization.Scientific reports · 2022Article
- WFS1 functions in ER export of vesicular cargo proteins in pancreatic β-cells.Nature communications · 2021Article
- TC10 regulates breast cancer invasion and metastasis by controlling membrane type-1 matrix metalloproteinase at invadopodia.Communications biology · 2021Article
- Oncogenic KRAS is dependent upon an EFR3A-PI4KA signaling axis for potent tumorigenic activity.Nature communications · 2021Article
125 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ras proteins must be localized to the inner surface of the plasma membrane to be biologically active. The motifs that effect Ras plasma membrane targeting consist of a C-terminal CAAX motif plus a second signal comprising palmitoylation of adjacent cysteine residues or the presence of a polybasic domain. In this study, we examined how Ras proteins access the cell surface after processing of the CAAX motif is completed in the endoplasmic reticulum (ER). We show that palmitoylated CAAX proteins, in addition to being localized at the plasma membrane, are found throughout the exocytic pathway and accumulate in the Golgi region when cells are incubated at 15 degrees C. In contrast, polybasic CAAX proteins are found only at the cell surface and not in the exocytic pathway. CAAX proteins which lack a second signal for plasma membrane targeting accumulate in the ER and Golgi. Brefeldin A (BFA) significantly inhibits the plasma membrane accumulation of newly synthesized, palmitoylated CAAX proteins without inhibiting their palmitoylation. BFA has no effect on the trafficking of polybasic CAAX proteins. We conclude that H-ras and K-ras traffic to the cell surface through different routes and that the polybasic domain is a sorting signal diverting K-Ras out of the classical exocytic pathway proximal to the Golgi. Farnesylated Ras proteins that lack a polybasic domain reach the Golgi but require palmitoylation in order to traffic further to the cell surface. These data also indicate that a Ras palmitoyltransferase is present in an early compartment of the exocytic pathway.
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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.