Chemical-genetic disruption of clathrin function spares adaptor complex 3-dependent endosome vesicle biogenesis.

ABSTRACT: A role for clathrin in AP-3-dependent vesicle biogenesis has been inferred from biochemical interactions and colocalization between this adaptor and clathrin. The functionality of these molecular associations, however, is controversial. We comprehensively explore the role of clathrin in AP-3-dependent vesicle budding, using rapid chemical-genetic perturbation of clathrin function with a clathrin light chain-FKBP chimera oligomerizable by the drug AP20187. We find that AP-3 interacts and colocalizes with endogenous and recombinant FKBP chimeric clathrin polypeptides in PC12-cell endosomes. AP-3 displays, however, a divergent behavior from AP-1, AP-2, and clathrin chains. AP-3 cofractionates with clathrin-coated vesicle fractions isolated from PC12 cells even after clathrin function is acute

SUBMITTER: Zlatic SA 

PROVIDER: S-EPMC3727930 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature