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Published on February 16, 2007; 10.1104/pp.106.094953

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Received December 18, 2006
Accepted February 7, 2007

Multiple Roles of ARF1 in Plant Cells Include Spatially-Regulated Recruitment of Coatomer and Elements of the Golgi Matrix

Loren A Matheson , Sally L Hanton , Marika Rossi , Maita Latijnhouwers , Giovanni Stefano , Luciana Renna , and Federica Brandizzi *

Department of Biology, 112 Science Place, University of Saskatchewan, Saskatoon, Saskatchewan S7N 5E2, Canada; Plant Pathology Program, Scottish Crop Research Institute, Invergowrie, Dundee DD2 5DA, UK; Department of Energy, Plant Research Laboratory, Michigan State University, East Lansing, MI 48824, USA

* Corresponding author; email: brandizz{at}msu.edu.

Recent evidence indicates that 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 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.




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