DePFth Perception in Clathrin-Mediated Endocytosis Derek C. Prosser, Beverly Wendland  Developmental Cell  Volume 37, Issue 5, Pages 387-388 (June 2016) DOI: 10.1016/j.devcel.2016.05.017 Copyright © 2016 Elsevier Inc. Terms and Conditions

Figure 1 Coordination of Early-Arriving “Pioneer” Proteins at Clathrin-Coated Structures (1) In its closed state, the endocytic adaptor complex AP-2 stochastically associates with PtdIns(4,5)P2-enriched plasma membrane sites in a manner that does not require Fcho1/2. This membrane association is transient unless AP-2 is further stabilized by interaction with other accessory proteins. (2) Fcho1 and Fcho2 form dimers that associate with the plasma membrane through the EFC/F-BAR domain. As shown by Ma et al. in this issue of Developmental Cell, Fcho1/2 bind with high affinity to a region of the Eps15 C-terminal tail containing three closely spaced DPF motifs. (3) The Fcho1/2-Eps15 interaction brings the Eps15 tail into close proximity with the membrane, allowing it to associate with AP-2 through additional DPF motifs. The ternary complex is thought to stabilize AP-2 at the CCS, promoting a switch to the “open” conformation that is capable of binding clathrin and cargo proteins. Developmental Cell 2016 37, 387-388DOI: (10.1016/j.devcel.2016.05.017) Copyright © 2016 Elsevier Inc. Terms and Conditions