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Zinc finger DHHC domain-containing protein 7 (ZDHHC7) is an enzyme belonging to the DHHC family of protein S-acyltransferases, characterized by their zinc finger Asp-His-His-Cys (DHHC) motif[3][5]. ZDHHC7 catalyzes S-palmitoylation, the covalent attachment of fatty acids like palmitate to specific cysteine residues on substrate proteins, which regulates their membrane localization, stability, and signaling properties[3][5][1]. ZDHHC7 exhibits broad substrate selectivity and modifies various proteins, including steroid hormone receptors (ER, PR, AR), G proteins (e.g., GNAQ), glucose transporters (GLUT4), neuronal and synaptic proteins (e.g., SNAP25, DLG4/PSD95), and components of cell polarity and cell death pathways[1][5][3]. These activities link it to crucial roles in signal transduction, membrane trafficking, hormone signaling, neuronal function, and potentially to disease mechanisms in neurodegenerative, inflammatory, and metabolic disorders[6][2][1]. ZDHHC7 is membrane-associated and primarily localized in the Golgi apparatus, with highest expression in brain, liver, and kidney[5][1]. If you require more focused data on drug interactions or recent therapeutic developments, direct research or clinical studies using ZDHHC7-specific chemical probes should be consulted, as current approved pharmaceuticals do not directly target ZDHHC7.
Inhibition of ZDHHC7 enzymatic (palmitoyltransferase) activity blocks S-palmitoylation of substrate proteins, altering their membrane association, trafficking, and signaling functions, and may affect disease-relevant processes (e.g., synaptic plasticity or inflammatory signaling)[2][6].
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