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Clathrin-coated vesicles (CCVs) selectively sort cargo at the cell membrane, trans-Golgi network, and endosomal compartments for multiple membrane traffic pathways. After a vesicle buds into the cytoplasm, the coat rapidly disassembles, allowing the clathrin to recycle while the vesicle gets transported to a variety of locations.
Coat complexes that have been well characterized so far include coat protein-I (COP-I), COP-II, and clathrin. [24] [25] Clathrin coats are involved in two crucial transport steps: (i) receptor-mediated and fluid-phase endocytosis from the plasma membrane to early endosome and (ii) transport from the TGN to endosomes. In endocytosis, the ...
Receptor-mediated endocytosis (RME), also called clathrin-mediated endocytosis, is a process by which cells absorb metabolites, hormones, proteins – and in some cases viruses – by the inward budding of the plasma membrane (invagination).
CDC42 is a small, Rho family GTPase involved in the pinching off and remodeling of the cellular plasma membrane. CDC42-regulated dynamin independent pathways are the main route of non-clathrin, non-caveolar uptake of fluid-phase internalization. Most CDC42-regulated endocytic pathways have large and wide surface invaginations and sometimes ...
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 ).
Material to be taken-in is surrounded by the plasma membrane, and then transferred to a vacuole. There are two types of endocytosis, phagocytosis (cell eating) and pinocytosis (cell drinking). In phagocytosis, cells engulf large particles such as bacteria. Pinocytosis is the same process, except the substances being ingested are in the fluid ...
Clathrin coats contain both clathrin (acts as a scaffold) and adaptor complexes that link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins , leading to their selection and concentration.
The presence of a di-aromatic FENTLY (Phe-Glu-Asn-Thr-Leu-Tyr) sequence motif in the cytoplasmic tail of the receptor is vital for its clathrin-mediated internalization. [6] This is supported by the evidence that Cos-1 cells transfected with the mannose receptor lacking its C-terminal tail are unable to endocytose C. albicans and P. carinii. [6]