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Plant Cell Advance Online Publication
Published on January 18, 2008; 10.1105/tpc.107.056515

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Received October 25, 2007
Returned for revision December 19, 2007
Accepted December 30, 2007

Membrane Association of the Arabidopsis ARF Exchange Factor GNOM Involves Interaction of Conserved Domains

Nadine Anders 1, Michael Nielsen 2, Jutta Keicher 1, York-Dieter Stierhof 1, Masahiko Furutani 3, Masao Tasaka 3, Karen Skriver 2, and Gerd Jürgens 1*

1 Center of Molecular Biology of Plants, University of Tübingen, 72076 Tübingen, Germany
2 Institute of Molecular Biology and Physiology, University of Copenhagen, 2100 Copenhagen, Denmark
3 Nara Institute of Science and Technology, Nara 630-0192, Japan

* To whom correspondence should be addressed. E-mail: gerd.juergens{at}zmbp.uni-tuebingen.de.

The GNOM protein plays a fundamental role in Arabidopsis thaliana development by regulating endosome–to–plasma membrane trafficking required for polar localization of the auxin efflux carrier PIN1. GNOM is a family member of large ARF guanine nucleotide exchange factors (ARF-GEFs), which regulate vesicle formation by activating ARF GTPases on specific membranes in animals, plants, and fungi. However, apart from the catalytic exchange activity of the SEC7 domain, the functional significance of other conserved domains is virtually unknown. Here, we show that a distinct N-terminal domain of GNOM mediates dimerization and in addition interacts heterotypically with two other conserved domains in vivo. In contrast with N-terminal dimerization, the heterotypic interaction is essential for GNOM function, as mutations abolishing this interaction inactivate the GNOM protein and compromise its membrane association. Our results suggest a general model of large ARF-GEF function in which regulated changes in protein conformation control membrane association of the exchange factor and, thus, activation of ARFs.




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