Adaptins are essential for the formation of adaptor complexes of clathrin-coded vesicles. Adaptins interact with the cytoplasmic domains of membrane-spanning receptors in the course of their endocytic/exocytic transport. They represent 1 of at least 4 components of intracellular transport and receptor downregulation pathways, the others being α/β/γ-adaptins, receptors, and ligand molecules. β-adaptins have a bipartite structure with invariant N-terminal and variable C-terminal domains. The former interact with the uniform component of coded vesicles, the clathrin lattice. In contrast, the C-terminal domain provides a set of recognition sequences for other proteins and therefore functions as part of a selector domain responsible for the specific entrapment of membrane-bound proteins in vesicles.
References
Western blot of human Jurkat cell lysate. The blot was probed with mouse monoclonal anti-β-Adaptin (N-terminal region) antibody at 1:500 (lane 1) and 1:2000 (lane 2).
*For more information, see UniProt Accession Q10567
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blotmobilities of known proteins with similar MW.
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