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Palmitoylation of Gephyrin Controls Receptor Clustering and Plasticity of GABAergic Synapses [1] In molecular biology, palmitoylation is the covalent attachment of fatty acids, such as palmitic acid, to cysteine (S-palmitoylation) and less frequently to serine and threonine (O-palmitoylation) residues of proteins, which are typically membrane ...
RU-SKI 43 inhibits the activity of SHHat, an enzyme that catalyzes the palmitoylation of Shh. [56] Since palmitoylation is essential for the activity of Shh, [57] inhibition of SHHat by RU-SKI 43 inhibits Shh signaling in cancer cells. [58] [59] 5E1, a monoclonal antibody against Shh, has been shown to inhibit medulloblastoma growth in mouse ...
The protein palmitoylation is a reversible process. The addition of palmitoyl group increase the membrane association of the substrate protein while the removal by palmitoyl thioesterase decreases the membrane association.
Farnesyltransferase inhibitors have been developed to stop the farnesylation of Ras and therefore weaken its affinity to membranes. [2] Other inhibitors are targeting the palmitoylation cycle of Ras through inhibiting depalmitoylation by acyl-protein thioesterases, potentially leading to a destabilization of the Ras cycle. [33]
Palmitoylation. S-palmitoylation (i.e. attachment of palmitic acid) is a reversible protein modification in which a palmitic acid is attached to a specific cysteine residue via thioester linkage. [2] [11] The term S-acylation can also be used when other medium and long fatty acids chains are also attached to palmitoylated proteins.
Inhibition with 2-Bromopalmitate was found to be irreversible, the other however was found to be mostly reversible. [9] Because of the roles of DHHC domain proteins in human diseases it has been suggested that chemical inhibitors of specific DHHC proteins may be a potential route to treatment of disease.
Skeletal formula of the prenyl group. Prenylation (also known as isoprenylation or lipidation) is the addition of hydrophobic molecules to a protein or a biomolecule.It is usually assumed that prenyl groups (3-methylbut-2-en-1-yl) facilitate attachment to cell membranes, similar to lipid anchors like the GPI anchor, though direct evidence of this has not been observed.
GAP43, is a nervous tissue-specific cytoplasmic protein that can be attached to the membrane via a dual palmitoylation sequence on cysteines 3 and 4. This sequence targets GAP43 to lipid rafts. It is a major protein kinase C substrate and is considered to play a key role in neurite formation, regeneration, and plasticity.