| First Author | Quan A | Year | 2012 |
| Journal | Proc Natl Acad Sci U S A | Volume | 109 |
| Issue | 10 | Pages | 3760-5 |
| PubMed ID | 22355135 | Mgi Jnum | J:182137 |
| Mgi Id | MGI:5314824 | Doi | 10.1073/pnas.1108294109 |
| Citation | Quan A, et al. (2012) Phosphorylation of syndapin I F-BAR domain at two helix-capping motifs regulates membrane tubulation. Proc Natl Acad Sci U S A 109(10):3760-5 |
| abstractText | Syndapin I (PACSIN 1) is a synaptically enriched membrane tubulating protein that plays important roles in activity-dependent bulk endocytosis and neuronal morphogenesis. While syndapin I is an in vitro phosphoprotein, it is not known to be phosphorylated in neurons. Here, we report the identification of two phosphorylation sites, S76 and T181, of syndapin I from nerve terminals. Both residues are located at the N-terminal helix-capping motifs (N-Cap) of different alpha-helices in the F-BAR domain, important for F-BAR homodimer curvature and dimer-dimer filament assembly, respectively. Phospho-mimetic mutations of these residues regulate lipid-binding and tubulation both in vitro and in cells. Neither phosphosite regulated syndapin I function in activity-dependent bulk endocytosis. Rather, T181 phosphorylation was developmentally regulated and inhibited syndapin I function in neuronal morphogenesis. This suggests a novel mechanism for phosphorylation control of an F-BAR function through the regulation of alpha-helix interactions and stability within the folded F-BAR domain. |
