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Sorting of integral membrane proteins at various stages of the endocytic and secretory pathways is mediated by vesicular trafficking between a variety of organelles. Two sorting signals are tyrosine-based and dileucine-based signals that interact with heterotetrameric adaptor protein complexes (AP-1, AP-2, AP-3, and AP-4), which are associated with the vesicle coats. These coatomers contain two large Adaptin proteins (γ, α, δ, or ε and β1, β2, β3, β4 respectively) that are noncovalently linked to one medium chain (μ1, μ2, μ3, or μ4) and one small chain ( σ1, σ2, σ3, or σ4). The AP-1 and AP-3 complexes are involved in protein sorting from the TGN and endosomes, while AP-2 adaptor complexes are involved in clathrin-mediated endocytosis. Adaptin ? shows more homology with Adaptin α than with Adaptin β. The conserved regions between Adaptins γ and α could be important for binding to other components of the AP-1 and AP-2 complexes, respectively.Immunofluorescence, Immunohistochemistry, Immunoprecipitation, Western Blotting
