SOS2 promotes salt tolerance in part by interacting with the vacuolar H+-ATPase and upregulating its transport activity.

SOS2 promotes salt tolerance in part by interacting with the vacuolar H+-ATPase and upregulating its transport activity. Research Abstract Details 

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SOS2 promotes salt tolerance in part by interacting with the vacuolar H+-ATPase and upregulating its transport activity. Abstract Text:

Giorgia Batelli,Paul E Verslues,Fernanda Agius,Quansheng Qiu,Hiroaki Fujii,Songqin Pan,Karen S Schumaker,Stefania Grillo,Jian-Kang Zhu,Giorgia Batelli,Paul E Verslues,Fernanda Agius,Quansheng Qiu,Hiroaki Fujii,Songqin Pan,Karen S Schumaker,Stefania Grillo,Jian-Kang Zhu,

The salt overly sensitive (SOS) pathway is critical for plant salt stress tolerance and has a key role in regulating ion transport under salt stress. To further investigate salt tolerance factors regulated by the SOS pathway, we expressed an N-terminal fusion of the improved tandem affinity purification tag to SOS2 (NTAP-SOS2) in sos2-2 mutant plants. Expression of NTAP-SOS2 rescued the salt tolerance defect of sos2-2 plants, indicating that the fusion protein was functional in vivo. Tandem affinity purification of NTAP-SOS2-containing protein complexes and subsequent liquid chromatography-tandem mass spectrometry analysis indicated that subunits A, B, C, E, and G of the peripheral cytoplasmic domain of the vacuolar H+-ATPase (V-ATPase) were present in a SOS2-containing protein complex. Parallel purification of samples from control and salt-stressed NTAP-SOS2/sos2-2 plants demonstrated that each of these V-ATPase subunits was more abundant in NTAP-SOS2 complexes isolated from salt-stressed plants, suggesting that the interaction may be enhanced by salt stress. Yeast two-hybrid analysis showed that SOS2 interacted directly with V-ATPase regulatory subunits B1 and B2. The importance of the SOS2 interaction with the V-ATPase was shown at the cellular level by reduced H+ transport activity of tonoplast vesicles isolated from sos2-2 cells relative to vesicles from wild-type cells. In addition, seedlings of the det3 mutant, which has reduced V-ATPase activity, were found to be severely salt sensitive. Our results suggest that regulation of V-ATPase activity is an additional key function of SOS2 in coordinating changes in ion transport during salt stress and in promoting salt tolerance.

SOS2 promotes salt tolerance in part by interacting with the vacuolar H+-ATPase and upregulating its transport activity. Publishing Authors By Initials

G Batelli,PE Verslues,F Agius,Q Qiu,H Fujii,S Pan,KS Schumaker,S Grillo,JK Zhu,G Batelli,PE Verslues,F Agius,Q Qiu,H Fujii,S Pan,KS Schumaker,S Grillo,JK Zhu,

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SOS2 promotes salt tolerance in part by interacting with the vacuolar H+-ATPase and upregulating its transport activity. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Molecular and cellular biology

VOLUME: 27

Page Numbers: 7781-90

Journal Abbreviation: Mol. Cell. Biol.

ISSN: 1098-5549

DAY: 17

MONTH: 09

YEAR: 2007

SOS2 promotes salt tolerance in part by interacting with the vacuolar H+-ATPase and upregulating its transport activity. Information

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LANGUAGE: eng

NlmUniqueID: 8109087

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Grant and Affiliation Information for SOS2 promotes salt tolerance in part by interacting with the vacuolar H+-ATPase and upregulating its transport activity.

AFFILIATION: Institute for Integrative Genome Biology and Department of Botany and Plant Sciences, University of California, Riverside, California 92521, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: R01GM59138

ACRONYM: GM

MEDLINETA: Mol Cell Biol

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