The binding of clathrin triskelions to membranes from coated vesicles.
We have developed a quantitative method to study the interaction of radiolabeled clathrin triskelions with membranes from brain coated vesicles. Clathrin triskellions do not bind to coated vesicles unless these are stripped of their clathrin coat. The binding of triskelions is of high affinity (KD congruent to 2 x 10(-9) M), is saturable and depends on vesicle concentration. Triskelions bind to protein-sensitive structures of the stripped vesicles. Polypeptides of about 110,000 daltons appear to be involved in the binding structure. The association of triskelions to stripped vesicles was confirmed by electron microscopy.
D002474:Cell-Free System; D002966:Clathrin; D003594:Cytoplasmic Granules / Q000378:metabolism* / Q000648:ultrastructure; D007425:Intracellular Membranes / Q000378:metabolism*; D007700:Kinetics; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism; D011485:Protein Binding
D002966:Clathrin; D046911:Macromolecular Substances; D008565:Membrane Proteins; D010447:Peptide Hydrolases