| First Author | Woodley KT | Year | 2019 |
| Journal | EMBO Rep | Volume | 20 |
| Issue | 10 | Pages | e47472 |
| PubMed ID | 31402609 | Mgi Jnum | J:280871 |
| Mgi Id | MGI:6364807 | Doi | 10.15252/embr.201847472 |
| Citation | Woodley KT, et al. (2019) S-acylated Golga7b stabilises DHHC5 at the plasma membrane to regulate cell adhesion. EMBO Rep 20(10):e47472 |
| abstractText | 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 stabilises 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 DHHC5 and Golga7b are required for localisation of desmoglein-2 to the plasma membrane and for desmosomal patterning. Loss of DHHC5/Golga7b causes functional impairments in cell adhesion, suggesting these proteins have a wider role in cell adhesion beyond desmosome assembly. This work uncovers a novel mechanism of DHHC5 regulation by Golga7b and demonstrates a role for the DHHC5/Golga7b complex in the regulation of cell adhesion. |
