Abstract
Protein palmitoylation (S-acylation) has emerged as an important player in a range of cellular processes, and as a result, the palmitoyl-acyltransferase (PAT) enzymes which mediate this modification have entered into the spotlight. Palmitoyltransferase ZDHHC5 (ZDHHC5) is among the more unique members of the PAT family as it is mainly localised to the plasma membrane and contains an extended cytoplasmic domain with several regulatory features. ZDHHC5 plays a vital role in a wide range of processes in different cell types. In this review, we offer a summary of the functions of ZDHHC5 in synaptic plasticity, cardiac function, cell adhesion and fatty acid uptake, among other processes. We also explore recent work has revealed several mechanisms to control the activity, localisation and function of ZDHHC5.
Highlights
Post-translational modifications (PTMs) of proteins are used by organisms to regulate almost every cellular process
Recent work focusing on the elucidation of fatty acid uptake by CD36 revealed that CD36 is targeted to the plasma membrane by S-acylation mediated by DHHC4 and ZDHHC5 [69]
A model of ZDHHC5 regulation is emerging that utilises phosphorylation by tyrosine kinases to regulate its activity and localisation; in the case of Y91 by directly regulating enzyme activity and for Y533 by regulating its cell surface expression by blocking its endocytosis
Summary
Post-translational modifications (PTMs) of proteins are used by organisms to regulate almost every cellular process. This amphipathic helix contains three cysteine residues which are palmitoylated [29,30] and forms a binding site for GOLGA7B, which regulates cell surface expression of ZDHHC5 [38]. Receptor stimulation leads to a rapid increase (< 1 min) in the palmitoylation of the C-terminal tail of ZDHHC5, a region known to be important in controlling its localisation in the cells [38] and its lateral motility in the plasma membrane [39].
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