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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.
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 ...
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.
Mechanism of clathrin-dependent endocytosis. Clathrin-coated pits in endocytosis: The membrane of the cell invaginates using the protein clathrin. The clathrin uses actin to pull together the sides of the plasma membrane and form a vesicle inside the cellular cytosol. Receptor-mediated endocytosis Receptor-mediated endocytosis is a mode of ...
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 ...
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]
Dynamin possesses unique mechanochemical properties used to tubulate and sever membranes, and is involved in clathrin-mediated endocytosis and other vesicular trafficking processes. Actin and other cytoskeletal proteins act as binding partners for the dynamin, which can also self-assemble leading to stimulation of GTPase activity.