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Título: | Palmitoylation as a Key Regulator of Ras Localization and Function |
Autor: | Busquets-Hernández, Carla CSIC; Triola Guillem, Gemma CSIC ORCID | Palabras clave: | Ras Palmitoylation Lipid posttranslational modifications Cancer Acylation Membrane subdomains Thioesterases |
Fecha de publicación: | 17-mar-2021 | Editor: | Frontiers Media | Citación: | Frontiers in Molecular Neuroscience 8: 659861 (2021) | Resumen: | Ras proteins require membrane association for proper function. This process is tightly regulated by reversible palmitoylation that controls not only the distribution over different subcellular compartments but also Ras compartmentalization within membrane subdomains. As a result, there is a growing interest in protein palmitoylation and the enzymes that control this process. In this minireview, we discuss how palmitoylation affects the localization and function of Ras proteins. A better understanding of the regulatory mechanism controlling protein lipidation is expected to provide new insights into the functional role of these modifications and may ultimately lead to the development of novel therapeutic approaches. | Versión del editor: | https://doi.org/10.3389/fmolb.2021.659861 | URI: | http://hdl.handle.net/10261/235503 | DOI: | 10.3389/fmolb.2021.659861 |
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2021_fmolb-08-659861.pdf.pdf | Artículo principal | 630,53 kB | Adobe PDF | Visualizar/Abrir |
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