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The significance of Ras is further evidenced by the fact that Ras genes are among the most mutated oncogenes in different types of cancers. After translation, Ras proteins can be targets of post-translational modifications (PTM), which can alter the intracellular dynamics of the protein. In this review, we will focus on how S-nitrosylation of Ras affects the way these proteins interact with membranes, its cellular localization, and its activity. S-Nitrosylation occurs when a nitrosyl moiety of nitric oxide (NO) is covalently attached to a thiol group of a cysteine residue in a target protein. In Ras, the conserved Cys118 is the most surface-exposed Cys and the preferable residue for NO action, leading to the initiation of transduction events. Ras transduces the mitogen-activated protein kinases (MAPK), the phosphoinositide-3 kinase (PI3K) and the RalGEF cellular pathways. S-Nitrosylation of elements of the RalGEF cascade remains to be identified. On the contrary, it is well established that several components of the MAPK and PI3K pathways, as well as different proteins associated with these cascades, can be modified by S-nitrosylation. Overall, this review presents a better understanding of Ras S-nitrosylation, increasing the knowledge on the dynamics of these proteins in the presence of NO and the underlying implications in cellular signaling.<\/jats:p>","DOI":"10.3390\/antiox12081562","type":"journal-article","created":{"date-parts":[[2023,8,4]],"date-time":"2023-08-04T09:28:04Z","timestamp":1691141284000},"page":"1562","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["Regulation of Ras Signaling by S-Nitrosylation"],"prefix":"10.3390","volume":"12","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-0245-0633","authenticated-orcid":false,"given":"S\u00f3nia","family":"Sim\u00e3o","sequence":"first","affiliation":[{"name":"Algarve Biomedical Center Research Institute (ABC-RI), University of Algarve, 8005-139 Faro, Portugal"},{"name":"Faculty of Medicine and Biomedical Sciences, University of Algarve, 8005-139 Faro, Portugal"}]},{"given":"Rafaela Ribeiro","family":"Agostinho","sequence":"additional","affiliation":[{"name":"Algarve Biomedical Center Research Institute (ABC-RI), University of Algarve, 8005-139 Faro, Portugal"},{"name":"Faculty of Medicine and Biomedical Sciences, University of Algarve, 8005-139 Faro, Portugal"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5394-9824","authenticated-orcid":false,"given":"Antonio","family":"Mart\u00ednez-Ruiz","sequence":"additional","affiliation":[{"name":"Unidad de Investigaci\u00f3n, Hospital Universitario Santa Cristina, Instituto de Investigaci\u00f3n Sanitaria Princesa, 28009 Madrid, Spain"},{"name":"Departamento de Bioqu\u00edmica y Biolog\u00eda Molecular, Facultad de Farmacia, Universidad Complutense de Madrid, 28040 Madrid, Spain"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2438-0111","authenticated-orcid":false,"given":"In\u00eas Maria","family":"Ara\u00fajo","sequence":"additional","affiliation":[{"name":"Algarve Biomedical Center Research Institute (ABC-RI), University of Algarve, 8005-139 Faro, Portugal"},{"name":"Faculty of Medicine and Biomedical Sciences, University of Algarve, 8005-139 Faro, Portugal"},{"name":"Champalimaud Research Program, 1400-038 Lisbon, Portugal"}]}],"member":"1968","published-online":{"date-parts":[[2023,8,4]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/bs.acr.2020.05.002","article-title":"Biology, pathology, and therapeutic targeting of RAS","volume":"148","author":"Rhett","year":"2020","journal-title":"Adv. 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