Dresden 2026 – wissenschaftliches Programm

Bereiche | Tage | Auswahl | Suche | Aktualisierungen | Downloads | Hilfe

BP: Fachverband Biologische Physik

BP 20: Protein Structure and Dynamics

BP 20.7: Vortrag

Mittwoch, 11. März 2026, 17:00–17:15, BAR/0106

Dynamics and (self-)interactions of the endocytic protein Eps15 — •Andromachi Papagiannoula, Ida M Vedel, Arbesa Saiti, Kathrin Motzny, and Sigrid Milles — Leibniz-Forschungsinstitut für Molekulare Pharmakologie im Forschungsverbund, Berlin

Eps15 is one of the earliest initiators of clathrin-mediated endocytosis (CME). The dimeric protein carries three EH domains per monomer, which are known to recognize Asn-Pro-Phe (NPF) motifs in intrinsically disordered regions (IDRs). Using nuclear magnetic resonance (NMR) spectroscopy, we examined interactions between EH domains and the IDR of the endocytic partner Dab2. In addition to canonical NPF recognition, we detect a high level of binding promiscuity leading to interaction with other phenylalanine-rich regions. This behavior enables EH domains to also engage with Eps15’s own IDR, creating partial competition with Dab2. Nevertheless, Dab2 and the Eps15 IDR can bind EH domains simultaneously, leading to recruitment of Dab2 into Eps15 condensates. When EH domains are expressed in row, as they naturally occur in the wild type full length protein, EH2 and EH3 tumble together as one entity, while EH1 moves independently. Using single molecule Forster resonance energy transfer (smFRET), we assess the three dimensional organization of the three EH domains with respect to each other and assess binding with both Dab2 and Eps15 IDRs.

Keywords: endocytosis; intrinsically disordered proteins; solution-state NMR; phase separation