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Adaptor protein (AP) complexes are found in coated vesicles and clathrin-coated pits. AP complexes connect cargo proteins and lipids to clathrin at vesicle budding sites, as well as binding accessory proteins that regulate coat assembly and disassembly (such as AP180 , epsins and auxilin ).
Clathrin adaptor proteins, also known as adaptins, are proteins that mediate the formation of vesicles for intracellular trafficking and secretion. Adaptins are clustered subunits of adaptor protein (AP) complexes. [1] There are several types of adaptin, each related to a different AP complex.
The protein's name refers to this lattice structure, deriving from Latin clathri meaning lattice. [2] Barbara Pearse named the protein clathrin at the suggestion of Graeme Mitchison, selecting it from three possible options. [3] Coat-proteins, like clathrin, are used to build small vesicles in order to transport molecules within cells.
Protein skimming removes certain organic compounds, including proteins and amino acids found in food particles and fish waste, by using the polarity of the protein itself. . Due to their intrinsic charge, water-borne proteins are either repelled or attracted by the air–water interface and these molecules can be described as hydrophobic (such as fats or oils) or hydrophilic (such as salt ...
AP-2 complex subunit alpha-1 is a protein that in humans is encoded by the AP2A1 gene. [5] This gene encodes the alpha 1 adaptin subunit of the adaptor protein 2 (AP2 adaptors) complex found in clathrin coated vesicles. The AP-2 complex is a heterotetramer consisting of two large adaptins (alpha or beta), a medium adaptin (mu), and a small ...
The AP2 adaptor complex is a multimeric protein that works on the cell membrane to internalize cargo in clathrin-mediated endocytosis. [1] It is a stable complex of four adaptins which give rise to a structure that has a core domain and two appendage domains attached to the core domain by polypeptide linkers.