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CELL BIOLOGY AND SIGNAL TRANSDUCTION

Mutations in the Arabidopsis Phosphoinositide Phosphatase Gene SAC9 Lead to Overaccumulation of PtdIns(4,5)P₂ and Constitutive Expression of the Stress-Response Pathway¹

Biology Department, Harvey Mudd College, Claremont, California 91711 (M.E.W., E.C., K.P., M.H.); and Department of Biology, Utah State University, Logan, Utah 84322 (J.T., E.J.D., J.E.T., D.B.D.)

Phosphoinositides (PIs) are signaling molecules that regulate cellular events including vesicle targeting and interactions between membrane and cytoskeleton. Phosphatidylinositol (PtdIns)(4,5)P₂ is one of the best characterized PIs; studies in which PtdIns(4,5)P₂ localization or concentration is altered lead to defects in the actin cytoskeleton and exocytosis. PtdIns(4,5)P₂ and its derivative Ins(1,4,5)P₃ accumulate in salt, cold, and osmotically stressed plants. PtdIns(4,5)P₂ signaling is terminated through the action of inositol polyphosphate phosphatases and PI phosphatases including supressor of actin mutation (SAC) domain phosphatases. In some cases, these phosphatases also act on Ins(1,4,5)P₃. We have characterized the Arabidopsis (Arabidopsis thaliana) sac9 mutants. The SAC9 protein is different from other SAC domain proteins in several ways including the presence of a WW protein interaction domain within the SAC domain. The rice (Oryza sativa) and Arabidopsis SAC9 protein sequences are similar, but no apparent homologs are found in nonplant genomes. High-performance liquid chromatography studies show that unstressed sac9 mutants accumulate elevated levels of PtdIns(4,5)P₂ and Ins(1,4,5)P₃ as compared to wild-type plants. The sac9 mutants have characteristics of a constitutive stress response, including dwarfism, closed stomata, and anthocyanin accumulation, and they overexpress stress-induced genes and overaccumulate reactive-oxygen species. These results suggest that the SAC9 phosphatase is involved in modulating phosphoinsitide signals during the stress response.

² Present address: Department of Biochemistry, Virginia Tech University, 306 Fralin Biotechnology Center, West Campus Drive, Blacksburg, VA 24061.

Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.105.061317.

^* Corresponding author; e-mail mary_williams{at}hmc.edu; fax 909–607–7172.

Received February 14, 2005; returned for revision March 25, 2005; accepted March 28, 2005.

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Plant Physiol. 2005 138: 571-572. [Full Text]