Requirement for GTP hydrolysis in the formation of secretory vesicles.
The specificity of vesicular transport in a cell is determined by the formation of vesicles with specific contents from a donor compartment and their selective fusion with the appropriate acceptor compartment. Several of the latter fusion steps have been investigated in detail using cell-free systems, and work with these systems as well as genetic evidence has revealed a role for GTP-binding proteins in membrane fusion processes. We have reconstituted the formation of constitutive secretory vesicles and immature secretory granules from the trans Golgi network in a cell-free system. We show here that the budding of both types of post-Golgi vesicles is inhibited by non-hydrolysable analogues of GTP, which suggests a more widespread role for GTP-binding proteins in membrane traffic than previously assumed.
Tooze
S A
SA
Cell Biology Programme, European Molecular Biology Laboratory, Heidelberg, FRG.
Weiss
U
U
Huttner
W B
WB
D000818:Animals; D002474:Cell-Free System; D003593:Cytoplasm / Q000187:drug effects / Q000648:ultrastructure*; D003594:Cytoplasmic Granules / Q000187:drug effects / Q000502:physiology* / Q000648:ultrastructure; D019204:GTP-Binding Proteins / Q000502:physiology; D006056:Golgi Apparatus / Q000502:physiology / Q000648:ultrastructure; D016244:Guanosine 5'-O-(3-Thiotriphosphate); D006160:Guanosine Triphosphate / Q000031:analogs & derivatives / Q000378:metabolism* / Q000494:pharmacology; D006868:Hydrolysis; D008561:Membrane Fusion / Q000187:drug effects; D051381:Rats; D013873:Thionucleotides / Q000494:pharmacology; D014407:Tumor Cells, Cultured
D013873:Thionucleotides; D016244:Guanosine 5'-O-(3-Thiotriphosphate); D006160:Guanosine Triphosphate; D019204:GTP-Binding Proteins