Expression of a constitutively activated plasma membrane H+-ATPase alters plant development and increases salt tolerance (Q24678936)

6

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author name string

Frédéric Gévaudant

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Geoffrey Duby

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Erik von Stedingk

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Rongmin Zhao

Phosphorylation of Thr-948 at the C terminus of the plasma membrane H(+)-ATPase creates a binding site for the regulatory 14-3-3 protein

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language of work or name

English

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publication date

August 2007

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published in

Plant Physiology

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volume

144

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issue

4

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page(s)

1763-76

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cites work

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Activation of the plant plasma membrane H+-ATPase by phosphorylation and binding of 14-3-3 proteins converts a dimer into a hexamer

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The plant plasma membrane H(+)-ATPase: structure, function and regulation

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Arabidopsis protein kinase PKS5 inhibits the plasma membrane H+ -ATPase by preventing interaction with 14-3-3 protein.

28 November 2018

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Syringomycin-Stimulated Phosphorylation of the Plasma Membrane H-ATPase from Red Beet Storage Tissue.

28 November 2018

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28 November 2018

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Targeting of a Nicotiana plumbaginifolia H+ -ATPase to the plasma membrane is not by default and requires cytosolic structural determinants

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Role of the plasma membrane H+-ATPase in auxin-induced elongation growth: historical and new aspects

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Biochemical evidence for the requirement of 14-3-3 protein binding in activation of the guard-cell plasma membrane H+-ATPase by blue light

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1 reference

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1 reference

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Binding of 14-3-3 protein to the plasma membrane H(+)-ATPase AHA2 involves the three C-terminal residues Tyr(946)-Thr-Val and requires phosphorylation of Thr(947).

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1 reference

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