Skip Navigation


JXB Advance Access originally published online on July 28, 2003
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow All Versions of this Article:
54/390/2053    most recent
erg230v1
Right arrow E-letters: Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when E-letters are posted
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 ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (29)
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Couchy, I.
Right arrow Articles by Satiat-Jeunemaitre, B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Couchy, I.
Right arrow Articles by Satiat-Jeunemaitre, B.
Agricola
Right arrow Articles by Couchy, I.
Right arrow Articles by Satiat-Jeunemaitre, B.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Journal of Experimental Botany, Vol. 54, No. 390, pp. 2053-2063, September 1, 2003
© 2003 Oxford University Press

Identification and localization of a ß-COP-like protein involved in the morphodynamics of the plant Golgi apparatus

Received 18 March 2003; Accepted 29 May 2003

Isabelle Couchy, Susanne Bolte, Marie-Thérèse Crosnier, Spencer Brown and Béatrice Satiat-Jeunemaitre*,

Laboratoire de Dynamique de la Compartimentation Cellulaire, Institut des Sciences du Végétal, CNRS UPR2355, 91198 Gif-sur-Yvette cedex, France

* To whom correspondence should be addressed. Fax: +33 1 69 82 33 55. E-mail: bsj{at}isv.cnrs-gif.fr

This paper examines the molecular machinery involved in membrane exchange within the plant endomembrane system. A study has been undertaken on ß-COP-like proteins in plant cells using M3A5, an antibody raised against the conserved sequence of mammalian ß-COP proteins. In mammalian cells, ß-COP proteins are part of a complex named the coatomer, which probably recruits some specific areas of the endomembrane system. Immunofluorescence analyses by confocal laser scanning microscopy showed that ß-COP-like proteins marked predominantly the plant Golgi apparatus. Other proteins known to be part of a potential machinery for COPI vesicle formation ({gamma}-COP, ß'-COP and Arf1 proteins) were immunolocalized on the same membraneous structures as ß-COP. Moreover, ß-COP and other COPI antibodies stained the cell plate in dividing cells. It is further shown that, in maize root cells, and in contrast to observations upon mammalian cells, the drug Brefeldin A (BFA) does not induce the release of ß-COP and Arf1 proteins from the Golgi membrane into the cytosol. These data clearly demonstrate that the antibody M3A5 is a valuable marker for studies on trafficking events in plant cells. They also report for the first time the location of COP components in plant tissue at the light level, especially on a model well known for secretion, i.e. the maize root cells. They also suggest that the membrane recruitment machinery may function in a plant-specific way.

Key words: ß-COP, Brefeldin A, coatomer, Golgi apparatus, plant cells.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
Plant Physiol.Home page
D. Van Damme, D. Inze, and E. Russinova
Vesicle Trafficking during Somatic Cytokinesis
Plant Physiology, August 1, 2008; 147(4): 1544 - 1552.
[Full Text] [PDF]


Home page
Plant Physiol.Home page
L. A. Matheson, S. L. Hanton, M. Rossi, M. Latijnhouwers, G. Stefano, L. Renna, and F. Brandizzi
Multiple Roles of ADP-Ribosylation Factor 1 in Plant Cells Include Spatially Regulated Recruitment of Coatomer and Elements of the Golgi Matrix
Plant Physiology, April 1, 2007; 143(4): 1615 - 1627.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
M. K. Min, S. J. Kim, Y. Miao, J. Shin, L. Jiang, and I. Hwang
Overexpression of Arabidopsis AGD7 Causes Relocation of Golgi-Localized Proteins to the Endoplasmic Reticulum and Inhibits Protein Trafficking in Plant Cells
Plant Physiology, April 1, 2007; 143(4): 1601 - 1614.
[Abstract] [Full Text] [PDF]


Home page
Plant CellHome page
D. Van Damme, S. Coutuer, R. De Rycke, F.-Y. Bouget, D. Inze, and D. Geelen
Somatic Cytokinesis and Pollen Maturation in Arabidopsis Depend on TPLATE, Which Has Domains Similar to Coat Proteins
PLANT CELL, December 1, 2006; 18(12): 3502 - 3518.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
Y. Boutte, M.-T. Crosnier, N. Carraro, J. Traas, and B. Satiat-Jeunemaitre
The plasma membrane recycling pathway and cell polarity in plants: studies on PIN proteins
J. Cell Sci., April 1, 2006; 119(7): 1255 - 1265.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
J. Samaj, F. Baluska, B. Voigt, M. Schlicht, D. Volkmann, and D. Menzel
Endocytosis, Actin Cytoskeleton, and Signaling
Plant Physiology, July 1, 2004; 135(3): 1150 - 1161.
[Full Text] [PDF]


Home page
J. Cell Sci.Home page
S. Bolte, S. Brown, and B. Satiat-Jeunemaitre
The N-myristoylated Rab-GTPase m-Rabmc is involved in post-Golgi trafficking events to the lytic vacuole in plant cells
J. Cell Sci., February 22, 2004; 117(6): 943 - 954.
[Abstract] [Full Text] [PDF]



Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.