ArticleThe Journal of cell biology2002
Activated K-Ras and H-Ras display different interactions with saturable nonraft sites at the surface of live cells.
Article in The Journal of cell biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.
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Who cites it
97 citing papers in PubMed.
- Dysregulation of cellular membrane homeostasis as a crucial modulator of cancer risk.The FEBS journal · 2024Review
- Regulation of T cell function by protein S-acylation.Frontiers in physiology · 2022Review
- Signaling in the crowded cell.Current opinion in structural biology · 2021Review
- Lipids in Pathophysiology and Development of the Membrane Lipid Therapy: New Bioactive Lipids.Membranes · 2021Review
- Compartmentalization of phosphatidylinositol 4,5-bisphosphate metabolism into plasma membrane liquid-ordered/raft domains.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The balance of protein farnesylation and geranylgeranylation during the progression of nonalcoholic fatty liver disease.The Journal of biological chemistry · 2020Review
- Oligomer β-amyloid Induces Hyperactivation of Ras to Impede NMDA Receptor-Dependent Long-Term Potentiation in Hippocampal CA1 of Mice.Frontiers in pharmacology · 2020Article
- The quaternary assembly of KRas4B with Raf-1 at the membrane.Computational and structural biotechnology journal · 2020Article
- The role of PS 18:0/18:1 in membrane function.Nature communications · 2019Review
- Concepts and advances in cancer therapeutic vulnerabilities in RAS membrane targeting.Seminars in cancer biology · 2019Review
- Neuroprotective Effect of S-trans, Trans-farnesylthiosalicylic Acid via Inhibition of RAS/ERK Pathway for the Treatment of Alzheimer's Disease.Drug design, development and therapy · 2019Article
- Functional link between plasma membrane spatiotemporal dynamics, cancer biology, and dietary membrane-altering agents.Cancer metastasis reviews · 2018Review
- Exploration and stabilization of Ras1 mating zone: A mechanism with positive and negative feedbacks.PLoS computational biology · 2018Article
- The microdomain-organizing protein MPP1 is required for insulin-stimulated activation of H-Ras.Oncotarget · 2018Article
- Raf-1 Cysteine-Rich Domain Increases the Affinity of K-Ras/Raf at the Membrane, Promoting MAPK Signaling.Structure (London, England : 1993) · 2018Article
- Oncogenic Ras Isoforms Signaling Specificity at the Membrane.Cancer research · 2018Review
- Corrected and Republished from: Activation Status-Coupled Transient S-Acylation Determines Membrane Partitioning of a Plant Rho-Related GTPase.Molecular and cellular biology · 2017Article
- Bistable front dynamics in a contractile medium: Travelling wave fronts and cortical advection define stable zones of RhoA signaling at epithelial adherens junctions.PLoS computational biology · 2017Article
- Reversible Effects of Peptide Concentration and Lipid Composition on H-Ras Lipid Anchor Clustering.Biophysical journal · 2015Article
- Dissecting protein reaction dynamics in living cells by fluorescence recovery after photobleaching.Nature protocols · 2015Article
37 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ras-membrane interactions play important roles in signaling and oncogenesis. H-Ras and K-Ras have nonidentical membrane anchoring moieties that can direct them to different membrane compartments. Ras-lipid raft interactions were reported, but recent studies suggest that activated K-Ras and H-Ras are not raft resident. However, specific interactions of activated Ras proteins with nonraft sites, which may underlie functional differences and phenotypic variation between different Ras isoforms, are unexplored. Here we used lateral mobility studies by FRAP to investigate the membrane interactions of green fluorescent protein-tagged H- and K-Ras in live cells. All Ras isoforms displayed stable membrane association, moving by lateral diffusion and not by exchange with a cytoplasmic pool. The lateral diffusion rates of constitutively active K- and H-Ras increased with their expression levels in a saturable manner, suggesting dynamic association with saturable sites or domains. These sites are distinct from lipid rafts, as the activated Ras mutants are not raft resident. Moreover, they appear to be different for H- and K-Ras. However, wild-type H-Ras, the only isoform preferentially localized in rafts, displayed cholesterol-sensitive interactions with rafts that were independent of its expression level. Our findings provide a mechanism for selective signaling by different Ras isoforms.
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