Plasma Membrane H+-ATPase and 14-3-3 Isoforms of Arabidopsis Leaves: Evidence for Isoform Specificity in the 14-3-3/H+-ATPase Interaction. Alsterfjord, M., Sehnke, P. C., Arkell, A., Larsson, H., Svennelid, F., Rosenquist, M., Ferl, R. J., Sommarin, M., & Larsson, C. Plant and Cell Physiology, 45(9):1202–1210, September, 2004. ![Plasma Membrane H+-ATPase and 14-3-3 Isoforms of Arabidopsis Leaves: Evidence for Isoform Specificity in the 14-3-3/H+-ATPase Interaction [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex The plasma membrane H+-ATPase is activated by binding of 14-3-3 protein to the phosphorylated C terminus. Considering the large number of 14-3-3 and H+-ATPase isoforms in Arabidopsis (13 and 11 expressed genes, respectively), specificity in binding may exist between 14-3-3 and H+-ATPase isoforms. We now show that the H+-ATPase is the main target for 14-3-3 binding at the plasma membrane, and that all twelve 14-3-3 isoforms tested bind to the H+-ATPase in vitro. Using specific antibodies for nine of the 14-3-3 isoforms, we show that GF14epsilon, mu, lambda, omega, chi, phi, nu, and upsilon are present in leaves, but that isolated plasma membranes lack GF14chi, phi and upsilon. Northern blots using isoform-specific probes for all 14-3-3 and H+-ATPase isoforms showed that transcripts were present for most of the isoforms. Based on mRNA levels, GF14epsilon, mu, lambda and chi are highly expressed 14-3-3 isoforms, and AHA1, 3, and 11 highly expressed H+-ATPase isoforms in leaves. However, mass peptide fingerprinting identified AHA1 and 2 with the highest score, and their presence could be confirmed by MS/MS. It may be calculated that under ‘unstressed’ conditions less than one percent of total 14-3-3 is attached to the H+-ATPase. However, during a condition requiring full activation of H+ pumping, as induced here by the presence of the fungal toxin fusicoccin, several percent of total 14-3-3 may be engaged in activation of the H+-ATPase.
@article{alsterfjord_plasma_2004,
title = {Plasma {Membrane} {H}+-{ATPase} and 14-3-3 {Isoforms} of {Arabidopsis} {Leaves}: {Evidence} for {Isoform} {Specificity} in the 14-3-3/{H}+-{ATPase} {Interaction}},
volume = {45},
issn = {0032-0781},
shorttitle = {Plasma {Membrane} {H}+-{ATPase} and 14-3-3 {Isoforms} of {Arabidopsis} {Leaves}},
url = {https://doi.org/10.1093/pcp/pch136},
doi = {10/cbp4j9},
abstract = {The plasma membrane H+-ATPase is activated by binding of 14-3-3 protein to the phosphorylated C terminus. Considering the large number of 14-3-3 and H+-ATPase isoforms in Arabidopsis (13 and 11 expressed genes, respectively), specificity in binding may exist between 14-3-3 and H+-ATPase isoforms. We now show that the H+-ATPase is the main target for 14-3-3 binding at the plasma membrane, and that all twelve 14-3-3 isoforms tested bind to the H+-ATPase in vitro. Using specific antibodies for nine of the 14-3-3 isoforms, we show that GF14epsilon, mu, lambda, omega, chi, phi, nu, and upsilon are present in leaves, but that isolated plasma membranes lack GF14chi, phi and upsilon. Northern blots using isoform-specific probes for all 14-3-3 and H+-ATPase isoforms showed that transcripts were present for most of the isoforms. Based on mRNA levels, GF14epsilon, mu, lambda and chi are highly expressed 14-3-3 isoforms, and AHA1, 3, and 11 highly expressed H+-ATPase isoforms in leaves. However, mass peptide fingerprinting identified AHA1 and 2 with the highest score, and their presence could be confirmed by MS/MS. It may be calculated that under ‘unstressed’ conditions less than one percent of total 14-3-3 is attached to the H+-ATPase. However, during a condition requiring full activation of H+ pumping, as induced here by the presence of the fungal toxin fusicoccin, several percent of total 14-3-3 may be engaged in activation of the H+-ATPase.},
number = {9},
urldate = {2021-06-15},
journal = {Plant and Cell Physiology},
author = {Alsterfjord, Magnus and Sehnke, Paul C. and Arkell, Annika and Larsson, Håkan and Svennelid, Fredrik and Rosenquist, Magnus and Ferl, Robert J. and Sommarin, Marianne and Larsson, Christer},
month = sep,
year = {2004},
pages = {1202--1210},
}
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Considering the large number of 14-3-3 and H+-ATPase isoforms in Arabidopsis (13 and 11 expressed genes, respectively), specificity in binding may exist between 14-3-3 and H+-ATPase isoforms. We now show that the H+-ATPase is the main target for 14-3-3 binding at the plasma membrane, and that all twelve 14-3-3 isoforms tested bind to the H+-ATPase in vitro. Using specific antibodies for nine of the 14-3-3 isoforms, we show that GF14epsilon, mu, lambda, omega, chi, phi, nu, and upsilon are present in leaves, but that isolated plasma membranes lack GF14chi, phi and upsilon. Northern blots using isoform-specific probes for all 14-3-3 and H+-ATPase isoforms showed that transcripts were present for most of the isoforms. Based on mRNA levels, GF14epsilon, mu, lambda and chi are highly expressed 14-3-3 isoforms, and AHA1, 3, and 11 highly expressed H+-ATPase isoforms in leaves. However, mass peptide fingerprinting identified AHA1 and 2 with the highest score, and their presence could be confirmed by MS/MS. It may be calculated that under ‘unstressed’ conditions less than one percent of total 14-3-3 is attached to the H+-ATPase. 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