spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search    

The fully linked HTML version of this article has now been published.
JCS ePress online publication date 20 Jan 2004
doi: 10.1242/jcs.00896

This Article
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
jcs.00896v1
117/5/711    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Chantalat, S.
Right arrow Articles by Jackson, C. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Chantalat, S.
Right arrow Articles by Jackson, C. L.

Research Article

The Arf activator Gea2p and the P-type ATPase Drs2p interact at the Golgi in Saccharomyces cerevisiae


Sophie Chantalat, Sei-Kyoung Park, Zhaolin Hua, Ke Liu, Renée Gobin, Anne Peyroche, Alain Rambourg, Todd R. Graham, and Catherine L. Jackson*
* Author for correspondence (e-mail: cathyj{at}helix.nih.gov)

Arf GTPases regulate both the morphological and protein sorting events that are essential for membrane trafficking. Guanine nucleotide exchange factors (GEFs) specific for Arf proteins determine when and where Arf GTPases will be activated in cells. The yeast Gea2p Arf GEF is a member of an evolutionarily conserved family of high molecular mass Arf GEFs that are peripherally associated with membranes. Nothing is known about how these proteins are localized to membranes, and few direct binding partners have been identified. In yeast, Gea2p has been implicated in trafficking through the Golgi apparatus and in maintaining Golgi structure. A major function of the Golgi apparatus is the packaging of cargo into secretory granules or vesicles. This process occurs through a series of membrane transformation events starting with fenestration of a saccular membrane, and subsequent remodeling of the fenestrated membrane into a mesh-like tubular network. Concentration of secretory cargo into nodes of the tubular network leads to enlargement of the nodes, which correspond to forming vesicles/granules, and thinning of the surrounding tubules. The tubules eventually break to release the secretory vesicles/granules into the cytoplasm. This process is highly conserved at the morphological level from yeast to mammalian cells. Drs2p, a multi-span transmembrane domain protein and putative aminophospholipid translocase, is required for the formation of a class of secretory granules/vesicles in yeast. Here we show that Drs2p interacts directly with Gea2p, both in vitro and in vivo. We mapped the domain of interaction of Drs2p to a 20-amino-acid region of the C-terminal cytoplasmic tail of the protein, adjacent to a region essential for Drs2p function. Mutations in Gea2p that abolish interaction with Drs2p are clustered in the C-terminal third of the Sec7 domain, and are important for Gea2p function. We characterize one such mutant that has a thermosensitive phenotype, and show that it has morphological defects along the secretory pathway in the formation of secretory granules/vesicles.


This article has been cited by other articles:


Home page
 Mol. Biol. CellHome page
K. Liu, K. Surendhran, S. F. Nothwehr, and T. R. Graham
P4-ATPase Requirement for AP-1/Clathrin Function in Protein Transport from the trans-Golgi Network and Early Endosomes
Mol. Biol. Cell, August 1, 2008; 19(8): 3526 - 3535.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
T. Szul, R. Grabski, S. Lyons, Y. Morohashi, S. Shestopal, M. Lowe, and E. Sztul
Dissecting the role of the ARF guanine nucleotide exchange factor GBF1 in Golgi biogenesis and protein trafficking
J. Cell Sci., November 15, 2007; 120(22): 3929 - 3940.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
K. Liu, Z. Hua, J. A. Nepute, and T. R. Graham
Yeast P4-ATPases Drs2p and Dnf1p Are Essential Cargos of the NPFXD/Sla1p Endocytic Pathway
Mol. Biol. Cell, February 1, 2007; 18(2): 487 - 500.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. K. Gillingham, J. R. C. Whyte, B. Panic, and S. Munro
Mon2, a Relative of Large Arf Exchange Factors, Recruits Dop1 to the Golgi Apparatus
J. Biol. Chem., January 27, 2006; 281(4): 2273 - 2280.
[Abstract] [Full Text] [PDF]

Home page
 J BiochemHome page
H.-W. Shin and K. Nakayama
Guanine Nucleotide-Exchange Factors for Arf GTPases: Their Diverse Functions in Membrane Traffic
J. Biochem., December 1, 2004; 136(6): 761 - 767.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
S. Wicky, H. Schwarz, and B. Singer-Kruger
Molecular Interactions of Yeast Neo1p, an Essential Member of the Drs2 Family of Aminophospholipid Translocases, and Its Role in Membrane Trafficking within the Endomembrane System
Mol. Cell. Biol., September 1, 2004; 24(17): 7402 - 7418.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
P. Natarajan, J. Wang, Z. Hua, and T. R. Graham
Drs2p-coupled aminophospholipid translocase activity in yeast Golgi membranes and relationship to in vivo function
PNAS, July 20, 2004; 101(29): 10614 - 10619.
[Abstract] [Full Text] [PDF]


© The Company of Biologists Ltd 2004