| First Author | He M | Year | 2014 |
| Journal | J Cell Biol | Volume | 206 |
| Issue | 2 | Pages | 273-88 |
| PubMed ID | 25049274 | Mgi Jnum | J:217227 |
| Mgi Id | MGI:5613420 | Doi | 10.1083/jcb.201401016 |
| Citation | He M, et al. (2014) Ankyrin-G palmitoylation and betaII-spectrin binding to phosphoinositide lipids drive lateral membrane assembly. J Cell Biol 206(2):273-88 |
| abstractText | Ankyrin-G and betaII-spectrin colocalize at sites of cell-cell contact in columnar epithelial cells and promote lateral membrane assembly. This study identifies two critical inputs from lipids that together provide a rationale for how ankyrin-G and betaII-spectrin selectively localize to Madin-Darby canine kidney (MDCK) cell lateral membranes. We identify aspartate-histidine-histidine-cysteine 5/8 (DHHC5/8) as ankyrin-G palmitoyltransferases required for ankyrin-G lateral membrane localization and for assembly of lateral membranes. We also find that betaII-spectrin functions as a coincidence detector that requires recognition of both ankyrin-G and phosphoinositide lipids for its lateral membrane localization. DHHC5/8 and betaII-spectrin colocalize with ankyrin-G in micrometer-scale subdomains within the lateral membrane that are likely sites for palmitoylation of ankyrin-G. Loss of either DHHC5/8 or ankyrin-G-betaII-spectrin interaction or betaII-spectrin-phosphoinositide recognition through its pleckstrin homology domain all result in failure to build the lateral membrane. In summary, we identify a functional network connecting palmitoyltransferases DHHC5/8 with ankyrin-G, ankyrin-G with betaII-spectrin, and betaII-spectrin with phosphoinositides that is required for the columnar morphology of MDCK epithelial cells. |
