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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). This process forms vesicles containing the absorbed substances and is strictly mediated by receptors on ...
Dynamin-dependent clathrin-independent pathways include FEME, UFE, ADBE, EGFR-NCE and IL2Rβ uptake. [10] Dynamin-independent clathrin-independent pathways include the CLIC/GEEC pathway (regulated by Graf1), [11] as well as MEND and macropinocytosis. [10] Clathrin-mediated endocytosis is the only pathway dependent on both clathrin and dynamin.
Clathrin-mediated endocytosis (CME) regulates many cellular physiological processes such as the internalization of growth factors and receptors, entry of pathogens, and synaptic transmission. It is believed that cellular invaders use the nutrient pathway to gain access to a cell's replicating mechanisms.
AP-2 complex. 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.
However, clathrin-mediated endocytosis may also serve to concentrate the IFNAR receptors and signaling components, thereby amplifying signaling. [15] Electron microscopy experiments show IFNAR receptors concentrated in clathrin-coated pits, and inhibition of clathrin-mediated endocytosis resulted in reduced phosphorylation of JAK1, Tyk2, STATs ...
While clathrin-coated endocytosis is the most efficient and dominant means of cellular cargo entry, endocytic pathways can operate without the presence of the clathrin triskelion. In the absence of clathrin in a plasma membrane, there are many elements of response that allow for the internalization of essential molecules for cellular function.
During clathrin-mediated endocytosis, the cell membrane invaginates to form a budding vesicle. Dynamin binds to and assembles around the neck of the endocytic vesicle, forming a helical polymer arranged such that the GTPase domains dimerize in an asymmetric manner across helical rungs.
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]