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The development of photoswitchable peptide inhibitors of protein-protein interactions involved in clathrin-mediated endocytosis (Traffic Lights peptides) [9] [10] [11] and photoswitchable small molecule inhibitors of dynamin (Dynazos) [12] has been reported. These photopharmacological compounds allow spatiotemporal control of the endocytosis ...
The bafilomycins are a family of macrolide antibiotics produced from a variety of Streptomycetes. Their chemical structure is defined by a 16-membered lactone ring scaffold. [2] Bafilomycins exhibit a wide range of biological activity, including anti-tumor, [3] anti-parasitic, [4] [5] immunosuppressant [6] and anti-fungal [7] activity.
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 ...
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.
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). There are different AP complexes in mammals.
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.
Fast endophilin-mediated endocytosis is a form of clathrin-independent endocytosis uses cargo capture by cytolytic proteins to allow for endophilin and receptor endocytosis. [7] Endophilin, a BAR protein, is typically bound in distinct patches to the plasma membrane by lamellipodin. [8]
AP180 is a protein that plays an important role in clathrin-mediated endocytosis of synaptic vesicles.It is capable of simultaneously binding both membrane lipids (via an ANTH domain) and clathrin and is therefore thought to recruit clathrin to the membrane of newly invaginating vesicles.