title: Protein acyl thioesterases (Review).
abstract: Many proteins are S-acylated, affecting their localization and function. Dynamic S-acylation in response to various stimuli has been seen for several proteins in vivo. The regulation of S-acylation is beginning to be elucidated. Proteins can autoacylate or be S-acylated by protein acyl transferases (PATs). Deacylation, on the other hand, is an enzymatic process catalyzed by protein thioesterases (APT1 and PPT1) but only APT1 appears to be involved in the regulation of the reversible S-acylation of cytoplasmic proteins seen in vivo. PPT1, on the other hand, is involved in the lysosomal degradation of S-acylated proteins and PPT1 deficiency causes the disease infant neuronal ceroid lipofuscinosis.
authors.affiliation: Molecular Medicine, National Heart & Lung Institute, Sir Alexander Fleming Building, Imperial College London, London, UK.
authors.forename: Ruth
authors.initials: R
authors.lastname: Zeidman
authors.forename: Caroline S
authors.initials: CS
authors.lastname: Jackson
authors.forename: Anthony I
authors.initials: AI
authors.lastname: Magee
mesh_terms: D000215:Acylation; D000217:Acyltransferases / Q000378:metabolism*; D006801:Humans; D011506:Proteins / Q000378:metabolism*; D013869:Thiolester Hydrolases / Q000378:metabolism*
chemical_list: D011506:Proteins; D000217:Acyltransferases; D013869:Thiolester Hydrolases