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Published on January 12, 2007; 10.1104/pp.106.093583

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Received November 22, 2006
Accepted December 31, 2006

Dual Lipid Modification of Arabidopsis Gamma Subunits Is Required for Efficient Plasma Membrane Targeting

Qin Zeng , Xuejun Wang , and Mark P. Running *

Donald Danforth Plant Science Center, 975 North Warson Road, St. Louis, MO 63132

* Corresponding author; email: mrunning{at}danforthcenter.org.

Posttranslational lipid modifications are important for proper localization of many proteins in eukaryotic cells. However, the functional interrelationships between lipid modification processes in plants remain unclear. Here we demonstrate that the two heterotrimeric G-protein {gamma}-subunits from Arabidopsis thaliana, AGG1 and AGG2, are prenylated, and AGG2 is S-acylated. In wild type, EYFP fused AGG1 and AGG2 are associated with plasma membranes, with AGG1 associated with internal membranes as well. Both can be prenylated by either protein geranylgeranyltransferase I (PGGT-I) or protein farnesyltransferase (PFT). Their membrane localization is intact in mutants lacking PFT activity and largely intact in mutants lacking PGGT-I activity, but is disrupted in mutants lacking both PFT and PGGT-I activity. Unlike in mammals, Arabidopsis G{gamma}s do not rely on functional G{alpha} for membrane targeting. Mutation of the 6th to last cysteine, the putative S-acylation acceptor site, causes a dramatic change in AGG2 but not AGG1 localization pattern, suggesting S-acylation serves as an important additional signal for AGG2 to be targeted to the plasma membrane. Domain swapping experiments suggest that a short charged sequence at the AGG2 C-terminus contributes to AGG2's efficient membrane targeting compared to AGG1. Our data show the large degree to which PFT and PGGT-I can compensate for each other in plants, and suggest that differential lipid modification plays an important regulatory role in plant protein localization.




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