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From: Mimetic peptide of ubiquitin-interacting motif of epsin as a cancer therapeutic-perspective in brain tumor therapy through regulating VEGFR2 signaling

Mimetic peptide of ubiquitin-interacting motif of epsin as a cancer therapeutic-perspective in brain tumor therapy through regulating VEGFR2 signaling

Figure 1. Epsins are adaptor proteins in endocytosis. VEGFR2 is activated by ligand-VEGF binding. Activated VEGFR2 is ubiquitylated, followed by epsin binding via UIM motif. ENTH domain in epsin "hooks" into the plasma membrane (PM) via PiP2. Clathrin and other endocytotic proteins such as AP2 bind to the DPW domain (Asp-Pro-Trp), while the EH-domain (Eps15 homology [EH] domain) proteins bind to the NPF domain (Asn-Pro-Phe) so that a pit is formed on the PM. Receptor-containing vesicles are endocytosed to cytosolic degradation machinery to deactivate cell signaling

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