ArticleMolecular biology of the cell2017
Individual S-acylated cysteines differentially contribute to H-Ras endomembrane trafficking and acylation/deacylation cycles.
Article in Molecular biology of the cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 23 citations in OpenAlex.
- Different Ras isoforms regulate synaptic plasticity in opposite directions.The EMBO journal · 2025Article
- Refining S-acylation: Structure, regulation, dynamics, and therapeutic implications.The Journal of cell biology · 2023Article
- Halting ErbB-2 isoforms retrograde transport to the nucleus as a new theragnostic approach for triple-negative breast cancer.Cell death & disease · 2022Article
- Palmitoylated acyl protein thioesterase APT2 deforms membranes to extract substrate acyl chains.Nature chemical biology · 2021Article
- Protein S-Palmitoylation and Lung Diseases.Advances in experimental medicine and biology · 2021Article
- Palmitoylation as a Key Regulator of Ras Localization and Function.Frontiers in molecular biosciences · 2021Review
- PtdIns4P-mediated electrostatic forces influence S-acylation of peripheral proteins at the Golgi complex.Bioscience reports · 2020Article
- Cysteine Oxidations in Mitochondrial Membrane Proteins: The Case of VDAC Isoforms in Mammals.Frontiers in cell and developmental biology · 2020Review
- Dynamic Protein S-Acylation in Plants.International journal of molecular sciences · 2019Review
- Cyclase-associated protein 1 (CAP1) is a prenyl-binding partner of Rap1 GTPase.The Journal of biological chemistry · 2018Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
S-acylation/deacylation cycles and vesicular transport are critical for an adequate subcellular distribution of S-acylated Ras proteins. H-Ras is dually acylated on cysteines 181 and 184, but it is unknown how these residues individually contribute to H-Ras trafficking. In this study, we characterized the acylation and deacylation rates and membrane trafficking of monoacylated H-Ras mutants to analyze their contributions to H-Ras plasma membrane and endomembrane distribution. We demonstrated that dually acylated H-Ras interacts with acyl-protein thioesterases (APTs) 1 and 2 at the plasma membrane. Moreover, single-acylation mutants of H-Ras differed not only in their subcellular distribution, where both proteins localized to different extents at both the Golgi complex and plasma membrane, but also in their deacylation rates, which we showed to be due to different sensitivities to APT1 and APT2. Fluorescence photobleaching and photoactivation experiments also revealed that 1) although S-acylated, single-acylation mutants are incorporated with different efficiencies into Golgi complex to plasma membrane vesicular carriers, and 2) the different deacylation rates of single-acylated H-Ras influence differentially its overall exchange between different compartments by nonvesicular transport. Taken together, our results show that individual S-acylation sites provide singular information about H-Ras subcellular distribution that is required for GTPase signaling.
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