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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 ...
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.
palmitoylation (a type of acylation), attachment of palmitate, a C 16 saturated acid; isoprenylation or prenylation, the addition of an isoprenoid group (e.g. farnesol and geranylgeraniol) farnesylation; geranylgeranylation; glypiation, glycosylphosphatidylinositol (GPI) anchor formation via an amide bond to C-terminal tail
In palmitoleoylation, a palmitoleoyl group (derived from palmitoleic acid, pictured above) is added.. Palmitoleoylation is type of protein lipidation where the monounsaturated fatty acid palmitoleic acid is covalently attached to serine or threonine residues of proteins.
Some members of the family such as ZDHHC3 and ZDHHC7 enhance palmitoylation of proteins such as PSD-95, SNAP-25, GAP43, Gαs. Others such as ZDHHC9 showed specificity only toward the H-Ras protein. [3] However, a recent study questions the involvement of classical enzyme-substrate recognition and specificity in the palmitoylation reaction. [4]
Palmitoylation is known to contribute to membrane association [27] because it contributes to enhanced hydrophobicity. [6] Palmitoylation is known to play a role in the modulation of proteins' trafficking, [28] stability [29] and sorting. [30] Palmitoylation is also involved in cellular signaling [31] and neuronal transmission. [32]
Within the N-terminus, SMIM14 is predicted to have three palmitoylation sites, [20] which facilitates the clustering of proteins, and one disulfide bridge, stabilizing the structure of the protein. There is also a predicted glycosaminoglycan site spanning residues 45–48, proximal to the transmembrane domain. [ 21 ]
SNARE proteins – "SNAP REceptors" – are a large protein family consisting of at least 24 members in yeasts and more than 60 members in mammalian and plant cells. [2] [3] [4] The primary role of SNARE proteins is to mediate the fusion of vesicles with the target membrane; this notably mediates exocytosis, but can also mediate the fusion of vesicles with membrane-bound compartments (such as ...