Molecular Biology of the Cell click for CBE Life Science Education Page

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
 QUICK SEARCH:   [advanced]


     


Originally published as MBC in Press, 10.1091/mbc.E05-05-0447 on October 26, 2005

Vol. 17, Issue 1, 525-538, January 2006

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental Material
Right arrow All Versions of this Article:
E05-05-0447v1
17/1/525    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
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 Mardones, G. A.
Right arrow Articles by Howell, K. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mardones, G. A.
Right arrow Articles by Howell, K. E.

Cis-Golgi Matrix Proteins Move Directly to Endoplasmic Reticulum Exit Sites by Association with TubulesFormula

Gonzalo A. Mardones *, Christopher M. Snyder {dagger}, and Kathryn E. Howell

Department of Cell and Developmental Biology, University of Colorado School of Medicine, Aurora, CO 80045

Submitted May 23, 2005; Revised September 30, 2005; Accepted October 14, 2005
Monitoring Editor: Benjamin Glick

The role of cis-medial Golgi matrix proteins in retrograde traffic is poorly understood. We have used imaging techniques to understand the relationship between the cis-medial Golgi matrix and transmembrane proteins during retrograde traffic in control and brefeldin A (BFA)-treated cells. All five of the cis-medial matrix proteins tested were associated with retrograde tubules within 2-3 min of initiation of tubule formation. Then, at later time points (3-10 min), transmembrane proteins are apparent in the same tubules. Strikingly, both the matrix proteins and the transmembrane proteins moved directly to endoplasmic reticulum (ER) exit sites labeled with p58 and Sec13, and there seemed to be a specific interaction between the ER exit sites and the tips or branch points of the tubules enriched for the matrix proteins. After the initial interaction, Golgi matrix proteins accumulated rapidly (5-10 min) at ER exit sites, and Golgi transmembrane proteins accumulated at the same sites ~2 h later. Our data suggest that Golgi cis-medial matrix proteins participate in Golgi-to-ER traffic and play a novel role in tubule formation and targeting.


This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E05-05-0447) on October 26, 2005.

Abbreviations used: BFA, brefeldin A; GalT, galactosyltransferase; Man-II, mannosidase II.

Formula The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).

* Present address: Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892

{dagger} Present address: Department of Molecular Microbiology and Immunology, Oregon Health and Science University, Portland, OR 97239.

Address correspondence to: Kathryn E. Howell (kathryn.howell{at}uchsc.edu).




This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
R. K. Morikawa, J. Aoki, F. Kano, M. Murata, A. Yamamoto, M. Tsujimoto, and H. Arai
Intracellular Phospholipase A1{gamma} (iPLA1{gamma}) Is a Novel Factor Involved in Coat Protein Complex I- and Rab6-independent Retrograde Transport between the Endoplasmic Reticulum and the Golgi Complex
J. Biol. Chem., September 25, 2009; 284(39): 26620 - 26630.
[Abstract] [Full Text] [PDF]


Home page
Hum Mol GenetHome page
E. Reynders, F. Foulquier, E. Leao Teles, D. Quelhas, W. Morelle, C. Rabouille, W. Annaert, and G. Matthijs
Golgi function and dysfunction in the first COG4-deficient CDG type II patient
Hum. Mol. Genet., September 1, 2009; 18(17): 3244 - 3256.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
T. Iinuma, T. Aoki, K. Arasaki, H. Hirose, A. Yamamoto, R. Samata, H.-P. Hauri, N. Arimitsu, M. Tagaya, and K. Tani
Role of syntaxin 18 in the organization of endoplasmic reticulum subdomains
J. Cell Sci., May 15, 2009; 122(10): 1680 - 1690.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Cell Physiol.Home page
M. L. Styers, A. K. O'Connor, R. Grabski, E. Cormet-Boyaka, and E. Sztul
Depletion of {beta}-COP reveals a role for COP-I in compartmentalization of secretory compartments and in biosynthetic transport of caveolin-1
Am J Physiol Cell Physiol, June 1, 2008; 294(6): C1485 - C1498.
[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
J. Cell Sci.Home page
C. Williams, R. Choudhury, E. McKenzie, and M. Lowe
Targeting of the type II inositol polyphosphate 5-phosphatase INPP5B to the early secretory pathway
J. Cell Sci., November 15, 2007; 120(22): 3941 - 3951.
[Abstract] [Full Text] [PDF]


Home page
Mol. Biol. CellHome page
G. A. Mardones, P. V. Burgos, D. A. Brooks, E. Parkinson-Lawrence, R. Mattera, and J. S. Bonifacino
The Trans-Golgi Network Accessory Protein p56 Promotes Long-Range Movement of GGA/Clathrin-containing Transport Carriers and Lysosomal Enzyme Sorting
Mol. Biol. Cell, September 1, 2007; 18(9): 3486 - 3501.
[Abstract] [Full Text] [PDF]


Home page
Mol. Biol. CellHome page
S. Jiang, S. W. Rhee, P. A. Gleeson, and B. Storrie
Capacity of the Golgi Apparatus for Cargo Transport Prior to Complete Assembly
Mol. Biol. Cell, September 1, 2006; 17(9): 4105 - 4117.
[Abstract] [Full Text] [PDF]


Home page
Mol. Biol. CellHome page
R. Steet and S. Kornfeld
COG-7-deficient Human Fibroblasts Exhibit Altered Recycling of Golgi Proteins
Mol. Biol. Cell, May 1, 2006; 17(5): 2312 - 2321.
[Abstract] [Full Text] [PDF]




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Copyright © 2006 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.