The amino-terminal domain of the golgi protein giantin interacts directly with the vesicle-tethering protein p115.
Giantin is thought to form a complex with p115 and Golgi matrix protein 130, which is involved in the reassembly of Golgi cisternae and stacks at the end of mitosis. The complex is involved in the tethering of coat protomer I vesicles to Golgi membranes and the initial stacking of reforming cisternae. Here we show that the NH(2)-terminal 15% of Giantin suffices to bind p115 in vitro and in vivo and to block cell-free Golgi reassembly. Because Giantin is a long, rod-like protein anchored to the membrane by its extreme COOH terminus, these results support the idea of a long, flexible tether linking vesicles and cisternae.
Lesa
G M
GM
Cell Biology Laboratory, Imperial Cancer Research Fund, 44 Lincoln's Inn Fields, London, WC2A 3PX, United Kingdom.
Seemann
J
J
Shorter
J
J
Vandekerckhove
J
J
Warren
G
G
D001483:Base Sequence; D001665:Binding Sites; D002352:Carrier Proteins / Q000378:metabolism*; D002384:Catalysis; D017931:DNA Primers; D006056:Golgi Apparatus / Q000378:metabolism*; D000077614:Golgi Matrix Proteins; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D052066:N-Ethylmaleimide-Sensitive Proteins; D011485:Protein Binding; D033921:Vesicular Transport Proteins
D002352:Carrier Proteins; D017931:DNA Primers; D000077614:Golgi Matrix Proteins; D008565:Membrane Proteins; D033921:Vesicular Transport Proteins; C087574:macrogolgin; C091580:vesicular transport factor p115; D052066:N-Ethylmaleimide-Sensitive Proteins