Abhydrolase domain-containing protein 17B (ABHD17B)

Abhydrolase domain-containing protein 17B (ABHD17B) is a membrane-associated serine hydrolase enzyme responsible for removing fatty acids from S-acylated cysteine residues (depalmitoylation) in substrate proteins such as N-Ras, GAP43, MAP6, and PSD95[2][4]. ABHD17B, together with related ABHD17 proteins, enables dynamic regulation of protein palmitoylation, which is essential for the membrane targeting and function of numerous signaling proteins[1][3]. ABHD17B is implicated in several cellular processes, including synaptic plasticity and MAPK pathway signaling, and is associated with diseases such as neurodegenerative disorders and possibly cancer, due to its role in modulating oncogenic N-Ras membrane localization[2][3]. The enzyme's active site includes a critical serine residue (Ser170), and its N-terminal palmitoylation is important for membrane localization and function[5][3]. Research focuses on ABHD17B as a component of the acyl-protein thioesterase family, with ongoing exploration of its roles and as a putative therapeutic target.

Other names

Alpha/beta hydrolase domain-containing 17BABHD17B depalmitoylaseAB17B

Inhibition of ABHD17B impedes depalmitoylation of N-Ras and other substrates, affecting their membrane association and signaling[3].