9HDD
Sla2 C-terminal region (Residues 560-968) (REND and THATCH domains)
Summary for 9HDD
| Entry DOI | 10.2210/pdb9hdd/pdb |
| EMDB information | 52061 |
| Descriptor | Protein SLA2 (1 entity in total) |
| Functional Keywords | actin binding, endocytosis, membrane trafficking |
| Biological source | Saccharomyces cerevisiae (brewer's yeast) |
| Total number of polymer chains | 2 |
| Total formula weight | 139357.34 |
| Authors | Draper-Barr, G.,Gustavsson, E.,Landau, M.,Garcia-Alai, M.M. (deposition date: 2024-11-12, release date: 2025-05-21) |
| Primary citation | Draper-Barr, G.,Defelipe, L.A.,Ruiz-Carrillo, D.,Gustavsson, E.,Landau, M.,Garcia-Alai, M. Sla2 is a core interaction hub for clathrin light chain and the Pan1/End3/Sla1 complex. Structure, 2025 Cited by PubMed Abstract: The interaction network of Sla2, a vital endocytic mid-coat adaptor protein, undergoes constant rearrangement. Sla2 serves as a scaffold linking the membrane to the actin cytoskeleton, with its role modulated by the clathrin light chain (CLC), which inhibits Sla2's function under certain conditions. We show that Sla2 has two independent binding sites for CLC: one previously described in homologs of fungi (Sla2) and metazoa (Hip1R), and a second found only in Fungi. We present the structural model of the Sla2 actin-binding domains in the context of regulatory structural domains by cryoelectron microscopy. We provide an interaction map of Sla2 and the regulatory proteins Sla1 and Pan1, predicted by AI modeling and confirmed by molecular biophysics techniques. Pan1 may compete with CLC for the conserved Sla2-binding site. These results enhance the mapping of crucial interactions at endocytic checkpoints and highlight the divergence between Metazoa and Fungi in this vital process. PubMed: 40347949DOI: 10.1016/j.str.2025.04.013 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.62 Å) |
Structure validation
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