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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 ...
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.
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 ...
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.
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-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. The two major types of clathrin adaptor complexes are the heterotetrameric adaptor protein (AP) complexes, and the monomeric GGA (Golgi-localising, Gamma-adaptin ear domain homology, ARF ...
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.