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© The Rockefeller University Press, 0021-9525/1999//57 $5.00
The Journal of Cell Biology, Volume 146, Number 1, , 1999 57-70

Original Article

A Role for the Vesicle Tethering Protein, P115, in the Post-Mitotic Stacking of Reassembling Golgi Cisternae in a Cell-Free System



James Shortera and Graham Warrena

a Cell Biology Laboratory, Imperial Cancer Research Fund, London WC2A 3PX, United Kingdom
Cell Biology Laboratory, Imperial Cancer Research Fund, 44 Lincoln's Inn Fields, London WC2A 3PX, UK.0171-269-34170171-269-3403

shorter{at}icrf.icnet.uk

During telophase, Golgi cisternae are regenerated and stacked from a heterogeneous population of tubulovesicular clusters. A cell-free system that reconstructs these events has revealed that cisternal regrowth requires interplay between soluble factors and soluble N-ethylmaleimide (NEM)–sensitive fusion protein (NSF) attachment protein receptors (SNAREs) via two intersecting pathways controlled by the ATPases, p97 and NSF. Golgi reassembly stacking protein 65 (GRASP65), an NEM-sensitive membrane-bound component, is required for the stacking process. NSF-mediated cisternal regrowth requires a vesicle tethering protein, p115, which we now show operates through its two Golgi receptors, GM130 and giantin. p97-mediated cisternal regrowth is p115-independent, but we now demonstrate a role for p115, in conjunction with its receptors, in stacking p97 generated cisternae. Temporal analysis suggests that p115 plays a transient role in stacking that may be upstream of GRASP65-mediated stacking. These results implicate p115 and its receptors in the initial alignment and docking of single cisternae that may be an important prerequisite for stack formation.

Key Words: Golgi apparatus • mitosis • p115 • tethering • stack

© 1999 The Rockefeller University Press

1.used in this paper: COPI, coat protein I; GRASP65, Golgi reassembly stacking protein 65; IQ, illimaquinone; Mann I, {alpha}1,2-mannosidase I; MGF, mitotic Golgi fragments; N73pep, NH2-terminal 73 amino acids of GM130 peptide; NEM, N-ethylmaleimide; NSF, NEM-sensitive fusion protein; RLG, rat liver Golgi membranes; sHeLa, spinner HeLa cells; SNAP, soluble NSF attachment protein; SNARE, SNAP receptor; t, target; v, vesicle

Dr. Warren's current address is Department of Cell Biology, SHM, C441, Yale University School of Medicine, 33 Cedar St., PO Box 208002, New Haven, CT 06520-8002. Tel.: (203) 785-5058. Fax: (203) 785-4301. E-mail: graham.warren@yale.edu


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