An Acylation Cycle Regulates Localization and Activity of Palmitoylated Ras Isoforms
By Oliver Rocks, A. Peyker, Martin Kahms, Peter J. Verveer, C. Koerner, Maria Lumbierres, J. Kuhlmann, H. Waldmann, A. Wittinghofer, P. Bastiaens. Science, 2005
851 citations recorded by the source corpus.
Subfields: Cell Biology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/fc2963f707108bd96a5a8b0d82614b163e5295e5
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Citations in the corpus
- Coronavirus envelope protein: current knowledge (2019, background): “Palmitoylation functions in the subcellular trafficking of proteins between membrane compartments and can also modulate protein-protein interactions (PPIs) [110, 111].”
- Palmitoylation: policing protein stability and traffic (2007, methodology): “The significance of reversible palmitoylation in Ras trafficking has been elegantly demonstrated using quantitative fluorescence microscopy and photobleaching technique”
- Targeting Protein Lipidation in Disease (2012, background): “Removal of palmitate by thioesterases results in dissociation of depalmitoylated H-Ras and N-Ras from the plasma membrane and retrograde trafficking to the Golgi, where H-Ras and N-Ras accumulate as a result of being re-palmitoylated [39, 40].”
- Riding the DUBway: regulation of protein trafficking by deubiquitylating enzymes (2006, neutral): “It is not clear whether this oxidative signaling is restricted to the local mitochondrial environment or what the proximal oxidant target is; however, both JNK and JNK scaffolds, as well as the putative downstream target GSK-3β, associate with mitochondria, allowing the possibility of a locally…”
- Integrating signals from RTKs to ERK/MAPK (2007, background): “In contrast, H-Ras and N-Ras constantly shuttle between the Golgi and plasma membrane as a result of a constitutive depalmitoylation/repalmitoylation cycle (Goodwin et al., 2005; Rocks et al., 2005).”
- Palmitic Acid: Physiological Role, Metabolism and Nutritional Implications (2017, background): “S-palmitoylation of proteins includes: soluble proteins, in which allows their controlled association with membranes, trafficking and domain localization (Rocks et al., 2005; Merrick et al., 2011); the cytosolic domains of membrane proteins (Blaskovic et al., 2013); and transmembrane proteins.”