Protein palmitoylation is a dynamic post-translational modification, where the 16-carbon fatty acid, palmitate, is added to cysteines of proteins to modulate protein sorting, targeting and signalling. Palmitate removal from proteins is mediated by acyl protein thioesterases (APTs). Although initially identified as lysophospholipases, increasing evidence suggests APT1 and APT2 are the major APTs that mediate the depalmitoylation of diverse cellular substrates. Here, we describe the conserved functions of APT1 and APT2 across organisms and discuss the possibility that these enzymes are members of a larger family of depalmitoylation enzymes.
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Conference Article| April 07 2015
Enzymatic protein depalmitoylation by acyl protein thioesterases
David T.S. Lin;
Elizabeth Conibear 1
*Centre for Molecular Medicine & Therapeutics, Department of Medical Genetics, University of British Columbia, Vancouver, British Columbia, Canada, V5Z 4H4
1To whom the correspondence should be addressed (firstname.lastname@example.org).
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David T.S. Lin, Elizabeth Conibear; Enzymatic protein depalmitoylation by acyl protein thioesterases. Biochem Soc Trans 1 April 2015; 43 (2): 193–198. doi: https://doi.org/10.1042/BST20140235
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