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

Giovanni M. Lesa, Joachim Seemann, James Shortert, Joël Vandekerckhove, Graham Warren

Research output: Contribution to journalArticlepeer-review

51 Scopus citations

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 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.

Original languageEnglish (US)
Pages (from-to)2831-2836
Number of pages6
JournalJournal of Biological Chemistry
Volume275
Issue number4
DOIs
StatePublished - Jan 28 2000

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'The amino-terminal domain of the golgi protein Giantin interacts directly with the vesicle-tethering protein p115'. Together they form a unique fingerprint.

Cite this