OPEN ACCESS ARTICLE

This Article Free via Open Access: OA OA Full Text Full Text (PDF) Supplemental Data OA All Versions of this Article: 143/4/1615    most recent pp.106.094953v1 Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in ISI Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via ISI Web of Science (8) Citing Articles via Google Scholar Google Scholar Articles by Matheson, L. A. Articles by Brandizzi, F. Search for Related Content PubMed PubMed Citation Articles by Matheson, L. A. Articles by Brandizzi, F. Agricola Articles by Matheson, L. A. Articles by Brandizzi, F.

CELL BIOLOGY AND SIGNAL TRANSDUCTION

Multiple Roles of ADP-Ribosylation Factor 1 in Plant Cells Include Spatially Regulated Recruitment of Coatomer and Elements of the Golgi Matrix^1,[W],[OA]

Department of Biology, University of Saskatchewan, Saskatoon, Saskatchewan S7N 5E2, Canada (L.A.M., S.L.H., M.R., G.S., L.R., F.B.); Plant Pathology Program, Scottish Crop Research Institute, Invergowrie, Dundee DD2 5DA, United Kingdom (M.L.); and Department of Energy, Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824 (M.R., F.B.)

Recent evidence indicates that ADP-ribosylation factor 1 (ARF1) carries out multiple roles in plant cells that may be independent from the established effector complex COPI. To investigate potential COPI-independent functions, we have followed the dynamics of ARF1 and a novel putative effector, the plant golgin GRIP-related ARF-binding domain-containing Arabidopsis (Arabidopsis thaliana) protein 1 (GDAP1) in living plant cells. We present data that ascribe a new role to ARF1 in plant cell membrane traffic by showing that the GTPase functions to recruit GDAP1 to membranes. In addition, although ARF1 appears to be central to the recruitment of both COPI components and the golgin, we have established a different subcellular distribution of these ARF1 effectors. Live cell imaging demonstrates that GDAP1 and COPI are distributed on Golgi membranes. However, GDAP1 is also found on ARF1-labeled structures that lack coatomer, suggesting that the membrane environment, rather than ARF1 alone, influences the differential recruitment of ARF1 effectors. In support of this hypothesis, fluorescence recovery after photobleaching analyses demonstrated that GDAP1 and COPI have different kinetics on membranes during the cycle of activation and inactivation of ARF1. Therefore, our data support a model where modulation of the cellular functions of ARF1 in plant cells encompasses not only the intrinsic activities of the effectors, but also differential recruitment onto membranes that is spatially regulated.

The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: Federica Brandizzi (brandizz{at}msu.edu).

^[W] The online version of this article contains Web-only data.

^[OA] Open Access articles can be viewed online without a subscription.

www.plantphysiol.org/cgi/doi/10.1104/pp.106.094953

^* Corresponding author; e-mail brandizz{at}msu.edu; fax 517–353–9168.

Received December 18, 2006; accepted February 7, 2007; published February 16, 2007.

This article has been cited by other articles:

				M. A. Held, A. Boulaflous, and F. Brandizzi Advances in Fluorescent Protein-Based Imaging for the Analysis of Plant Endomembranes Plant Physiology, August 1, 2008; 147(4): 1469 - 1481. [Full Text] [PDF]

				M. Latijnhouwers, T. Gillespie, P. Boevink, V. Kriechbaumer, C. Hawes, and C. M. Carvalho Localization and domain characterization of Arabidopsis golgin candidates J. Exp. Bot., December 1, 2007; 58(15-16): 4373 - 4386. [Abstract] [Full Text] [PDF]