Clathrin locks up vesicle structure
نویسندگان
چکیده
منابع مشابه
Crm1 locks up replication factors
e already knew the players—MgcRacGAP, Aurora B, and RhoA—and that knocking out any one of them caused failure of cytokinesis; but it wasn’t clear how they were connected. Now, it appears that Aurora B phosphorylates the GAP domain of MgcRacGAP, allowing it to turn its GAP activity toward RhoA, according to data from Yukinori Minoshima, Toshiyuki Kawashima, Toshio Kitamura (University of Tokyo, ...
متن کاملClathrin-coated vesicle formation: a paradigm for coated-vesicle formation.
Clathrin-coated pits are the major ports of entry into the cell and are responsible for the internalization of a variety of biologically important macromolecules. These transport intermediates form as a result of the co-ordinated assembly of a number of cytosolic proteins on to the membrane which results in specific cargo recruitment. We have used a variety of approaches including permeabilized...
متن کاملRegulation of clathrin-coated vesicle formation.
The formation of clathrin-coated pits at the plasma membrane requires the concerted action of many different molecules. The real challenge lies in determining the hierarchy of these interactions. We are using assays in both intact and permeabilized cells to dissect the temporal requirements for clathrin-coated vesicle formation, and also to examine the role of phosphorylation of the coat proteins.
متن کاملDeterminants of clathrin-coated vesicle acidification.
The proton-translocating ATPase of clathrin-coated vesicles of bovine brain is characterized by ATP specificity. Chloride or bromide serve as co-ions balancing electrogenic proton pumping. ATP-driven proton translocation can be observed in the absence of chloride, provided the membrane potential is collapsed by K+ moving out in the presence of valinomycin. Chloride transport can be observed ind...
متن کاملStructure of Coatomer Cage Proteins and the Relationship among COPI, COPII, and Clathrin Vesicle Coats
COPI-coated vesicles form at the Golgi apparatus from two cytosolic components, ARF G protein and coatomer, a heptameric complex that can polymerize into a cage to deform the membrane into a bud. Although coatomer shares a common evolutionary origin with COPII and clathrin vesicle coat proteins, the architectural relationship among the three cages is unclear. Strikingly, the alphabeta'-COP core...
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ژورنال
عنوان ژورنال: Nature
سال: 1982
ISSN: 0028-0836,1476-4687
DOI: 10.1038/298228a0