Plasma Membrane H+-ATPase and 14-3-3 Isoforms of Arabidopsis Leaves: Evidence for Isoform Specificity in the 14-3-3/H+-ATPase Interaction-Reference-Cited by-同舟云学术

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Plasma Membrane H+-ATPase and 14-3-3 Isoforms of Arabidopsis Leaves: Evidence for Isoform Specificity in the 14-3-3/H+-ATPase Interaction

Published:2004-09-15 Issue:9 Volume:45 Page:1202-1210
ISSN:1471-9053
Container-title:Plant and Cell Physiology
language:en
Short-container-title:

Author:

Alsterfjord Magnus,Sehnke Paul C.,Arkell Annika,Larsson Håkan,Svennelid Fredrik,Rosenquist Magnus,Ferl Robert J.,Sommarin Marianne,Larsson Christer

Publisher

Oxford University Press (OUP)

Subject

Cell Biology,Plant Science,Physiology,General Medicine

Link

http://academic.oup.com/pcp/article-pdf/45/9/1202/19669670/pch136.pdf

Reference43 articles.

1. Aitken, A. (2002) Functional specificity in 14-3-3 isoform interactions through dimer formation and phosphorylation. Chromosome location of mammalian isoforms and variants. Plant Mol. Biol.50: 993–1010.

2. Arango, M., Gevaudant, F., Oufattole, M. and Boutry, M. (2003) The plasma membrane proton pump ATPase: the significance of gene subfamilies. Planta216: 355–365.

3. Babakov, A.V., Chelysheva, V.V., Klychnikov, O.I., Zorinyanz, S.E., Trofimova, M.S. and De Boer, A.H. (2000) Involvement of 14-3-3 proteins in the osmotic regulation of H+-ATPase in plant plasma membranes. Planta211: 446–448.

4. Bachmann, M., Huber, J.L., Athwal, G.S., Wu, K., Ferl, R.J. and Huber, S.C. (1996) 14-3-3 proteins associate with the regulatory phosphorylation site of spinach leaf nitrate reductase in an isoform-specific manner and reduce dephosphorylation of Ser-543 by endogenous protein phosphatases. FEBS Lett.398: 26–30.

5. Ballio, A., Chain, E.B., De Leo, P., Erlanger, B.F., Mauri, M. and Tonolo, A. (1964) Fusicoccin, a new wilting toxin produced by Fusicoccum amygdali Del. Nature203: 297–298.

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