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Regulation of endosomal membrane traffic by a Gadkin/AP-1/kinesin KIF5 complex.


ABSTRACT: Endosomes and endosomal vesicles (EVs) rapidly move along cytoskeletal filaments allowing them to exchange proteins and lipids between different endosomal compartments, lysosomes, the trans-Golgi network (TGN), and the plasma membrane. The precise mechanisms that connect membrane traffic between the TGN and perinuclear endosomal compartments with motor-protein driven transport have largely remained elusive. Here we show that Gadkin (also termed gamma-BAR), a peripheral membrane protein localized to the TGN and to TGN-derived EVs, directly associates with the clathrin adaptor AP-1 and with the motor protein kinesin KIF5, thereby potentially regulating EV dynamics. Gadkin overexpression induced the dispersion of transferrin (Tf)- and Rab4-positive EVs to the cell periphery, whereas KIF5B-depleted cells displayed a perinuclear concentration. Functional experiments suggest that the role of Gadkin as a regulator of endosomal membrane traffic critically depends on complex formation with both AP-1 and KIF5. Our data thus provide a direct molecular link between TGN-derived EVs and the microtubule-based cytoskeleton.

SUBMITTER: Schmidt MR 

PROVIDER: S-EPMC2741253 | biostudies-literature | 2009 Sep

REPOSITORIES: biostudies-literature

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Regulation of endosomal membrane traffic by a Gadkin/AP-1/kinesin KIF5 complex.

Schmidt Michael R MR   Maritzen Tanja T   Kukhtina Viktoria V   Higman Victoria A VA   Doglio Laura L   Barak Naomi N NN   Strauss Holger H   Oschkinat Hartmut H   Dotti Carlos G CG   Haucke Volker V  

Proceedings of the National Academy of Sciences of the United States of America 20090821 36


Endosomes and endosomal vesicles (EVs) rapidly move along cytoskeletal filaments allowing them to exchange proteins and lipids between different endosomal compartments, lysosomes, the trans-Golgi network (TGN), and the plasma membrane. The precise mechanisms that connect membrane traffic between the TGN and perinuclear endosomal compartments with motor-protein driven transport have largely remained elusive. Here we show that Gadkin (also termed gamma-BAR), a peripheral membrane protein localized  ...[more]

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