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Clathrin is a protein that plays a role in the formation of coated vesicles. Clathrin was first isolated by Barbara Pearse in 1976. [1] It forms a triskelion shape composed of three clathrin heavy chains and three light chains. When the triskelia interact they form a polyhedral lattice that surrounds the vesicle.
For example, in AP1 these subunits are gamma-1-adaptin, beta-1-adaptin, mu-1 and sigma-1, while in AP2 they are alpha-adaptin, beta-2-adaptin, mu-2 and sigma-2. Each subunit has a specific function. Adaptins recognise and bind to clathrin through their hinge region (clathrin box), and recruit accessory proteins that modulate AP function through ...
Endocytosis pathways can be subdivided into four categories: namely, receptor-mediated endocytosis (also known as clathrin-mediated endocytosis), caveolae, pinocytosis, and phagocytosis. [3] Clathrin-mediated endocytosis is mediated by the production of small (approx. 100 nm in diameter) vesicles that have a morphologically characteristic coat ...
Although receptors and their ligands can be brought into the cell through a few mechanisms (e.g. caveolin and lipid raft), clathrin-mediated endocytosis remains the best studied. Clathrin-mediated endocytosis of many receptor types begins with the ligands binding to receptors on the cell plasma membrane.
The dynamic nature of such vesicles show that they have a life time from 2 seconds up to 7 minutes and about 85% of cavin 1 protein was digested, indicating that the cavin-positive buds were internalized and degraded. The imaging techniques aided in research about the caveolar destiny and budding as it relates to the Cavin 1 protein. [4]
Clathrin-independent carriers (CLICs) are prevalent tubulovesicular membranes responsible for non-clathrin mediated endocytic events. They appear to endocytose material into GPI-anchored protein -enriched early endosomal compartment ( GEECs ).
Vesicular transport adaptor proteins are proteins involved in forming complexes that function in the trafficking of molecules from one subcellular location to another. [ 2 ] [ 3 ] [ 4 ] These complexes concentrate the correct cargo molecules in vesicles that bud or extrude off of one organelle and travel to another location, where the cargo is ...
The AP2 adaptor complex exists in two primary conformations: the open conformation (active state) and the closed conformation (inactive state). [2] In its active state, the clathrin binding site found on the β subunit and the cargo binding site found on the μ subunit are exposed to the cytosol, [2] allowing their respective interactions to occur.