Hsc70/uncoating ATPase activation--proposal of a new model.
To the best of my knowledge, the signal for the clathrin removal from coated vesicles by the uncoating ATPase is still obscure. I presume that a specific configuration of preexisting, but separately ineffective uncoating ATPase binding sites, is responsible for the triggering of its action. Changes in the geometrical structure of clathrin that inevitably appear during the coated pit-coated vesicle conversion, place the preexisting uncoating ATPase recognition sites into the necessary disposition.
Stantchev
Z S
ZS
Laboratory of Electron Microscopy, Varna Institute of Medicine, Bulgaria.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D002966:Clathrin / Q000378:metabolism; D003034:Coated Pits, Cell-Membrane / Q000378:metabolism; D018699:Coated Vesicles / Q000378:metabolism; D004789:Enzyme Activation; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism*; D006801:Humans; D008956:Models, Chemical
D002966:Clathrin; D018840:HSP70 Heat-Shock Proteins; D000251:Adenosine Triphosphatases