Some membrane cargo is sorted into clathrin-coated pits after ubiquitination of the cytosolic domain (reviewed in Piper et al 2014). Ubiquitinated cargo is recognized by adaptor proteins such as EPS15, EPN1 and EPN2 that contain ubiquitin-binding domains and also interact with components of the clathrin coat (Chen et al, 1998; Rosenthal et al, 1999; Polo et al, 2002; Shih et al, 2002; Haglund et al, 2003; Schmid et al, 2006; reviewed in Sen et al, 2012; Piper et al, 2014). A number of receptor tyrosine kinases, including EGFR, VEGFR, FGFR and others undergo ubiquitination at the plasma membrane, triggering endocytosis. Internalized RTKs can undergo recycling or degradation, the latter of which serves to terminate signaling (reviewed in Sorkin and von Zastrow, 2009; Haglund and Dikic, 2012). Ubiquitin-based sorting into CCPs appears to be dynamic as deubiquitinases have been identified as components of some CCPs (Weinberg and Drubin, 2014).