Ontology highlight
ABSTRACT:
SUBMITTER: Locatelli C
PROVIDER: S-EPMC7657471 | biostudies-literature | 2020 Nov
REPOSITORIES: biostudies-literature
Locatelli Carolina C Lemonidis Kimon K Salaun Christine C Tomkinson Nicholas C O NCO Chamberlain Luke H LH
Journal of cell science 20201105 21
Sprouty-2 is an important regulator of growth factor signalling and a tumour suppressor protein. The defining feature of this protein is a cysteine-rich domain (CRD) that contains twenty-six cysteine residues and is modified by S-acylation. In this study, we show that the CRD of sprouty-2 is differentially modified by S-acyltransferase enzymes. The high specificity/low activity zDHHC17 enzyme mediated restricted S-acylation of sprouty-2, and cysteine-265 and -268 were identified as key targets o ...[more]