The amino-terminal domain of the Golgi protein Giantin interacts directly with the vesicle-tethering protein p115

Citation
Gm. Lesa et al., The amino-terminal domain of the Golgi protein Giantin interacts directly with the vesicle-tethering protein p115, J BIOL CHEM, 275(4), 2000, pp. 2831-2836
Citations number
71
Categorie Soggetti
Biochemistry & Biophysics
Journal title
JOURNAL OF BIOLOGICAL CHEMISTRY
ISSN journal
00219258 → ACNP
Volume
275
Issue
4
Year of publication
2000
Pages
2831 - 2836
Database
ISI
SICI code
0021-9258(20000128)275:4<2831:TADOTG>2.0.ZU;2-L
Abstract
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 cisterna e, 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 Giant in 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 linkin g vesicles and cisternae.