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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 (α, γ, δ, or ε and β1, β2, β3 or 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. In the AP-2 complex, Adaptin α is expressed in two very similar isoforms from two different genes. Adaptin α [A] (112kDa) is expressed primarily in brain, while Adaptin α [C] (105kDa) is expressed in brain, liver and other tissues.Immunofluorescence, Immunohistochemistry, Immunoprecipitation, Western Blotting
