Abstract

PIP2 binding sites are present is proteins with important roles in clathrin-mediated endocytosis such as epsins and AP180, namely cargo recruitment and membrane budding for vesicle formation. Binding to the membrane lipid bilayer allows correct targeting of these proteins and of the proteins they recruit (AP complexes for Epsins and Clahrin itself for AP180 ) to the plasma membrane. In the case of Epsin, the binding of lipid head groups directely induces curvature of the plasma membrane. Epsin and AP180 families are close relatives, both contain N-terminal lipid-binding domains and central clathrin/adaptor binding domains. However, they are distinct in that AP180 N-terminal homology (ANTH) domain binds lipids on its surface, while epsin-N-terminal homology (ENTH) domain binds lipids in a pocket. The functional class is represented by two ELMs corresponding to this two binding features.

 Selected references

 This ELM has been assigned the following Gene Ontology (GO) terms for biological process, cellular component and molecular function.

Biological Process
endocytosis	GO:0006897
receptor mediated endocytosis	GO:0006898
Cellular Component
cytosol	GO:0005829
Molecular Function
phosphatidylinositol-4,5-bisphosphate binding	GO:0005546