S-acylated Golga7b stabilises DHHC5 at the plasma membrane to regulate cell adhesion

ABSTRACT: S-acylation (palmitoylation) is the only fully reversible lipid modification of proteins however little is known about how protein S-acyltransferases (PATs) that mediate it are regulated. DHHC5 is a PAT that is mainly localised at the plasma membrane with roles in synaptic plasticity, massive endocytosis and cancer cell growth/invasion. Here we demonstrate that DHHC5 binds to and palmitoylates a novel accessory protein Golga7b. Palmitoylation of Golga7b prevents clathrin-mediated endocytosis of DHHC5 and stabilizes it at the plasma membrane. Proteomic analysis of the composition of DHHC5/Golga7b-associated protein complexes reveals a striking enrichment in adhesion proteins, particularly components of desmosomes. We show that Desmoglein-2 and Plakophilin-3 are substrates of DHHC5 and that

SUBMITTER: Mr. Keith, T Woodley 

PROVIDER: S-SCDT-EMBOR-2018-47472V1 | biostudies-other |

REPOSITORIES: biostudies-other