TY - JOUR
T1 - The amino-terminal domain of the golgi protein Giantin interacts directly with the vesicle-tethering protein p115
AU - Lesa, Giovanni M.
AU - Seemann, Joachim
AU - Shortert, James
AU - Vandekerckhove, Joël
AU - Warren, Graham
PY - 2000/1/28
Y1 - 2000/1/28
N2 - 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 NH2-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.
AB - 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 NH2-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.
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U2 - 10.1074/jbc.275.4.2831
DO - 10.1074/jbc.275.4.2831
M3 - Article
C2 - 10644749
AN - SCOPUS:0034723203
SN - 0021-9258
VL - 275
SP - 2831
EP - 2836
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 4
ER -