Fusicoccin: A Tool in Plant Physiology

Marrè, E.

doi:10.1146/annurev.pp.30.060179.001421

Cited by 791 publications

(465 citation statements)

References 53 publications

(38 reference statements)

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“…In plants, 14-3-3 proteins have been suggested to also play a role in the binding of fusicoccin (Korthout and de Boer, 1994;Marra et al, 1994;Oecking et al, 1994). Fusicoccin is known to mimic some of the physiological effects of auxin and has been used as a tool for studying the action of this phytohormone (de Boer, 1997;Marrè , 1979). The role of 14-3-3 proteins in the binding of fusicoccin, however, has remained unresolved.…”

Section: Introductionmentioning

confidence: 99%

“…According to one model, fusicoccin interferes with a signal transduction chain ultimately leading to activation of the plant plasma membrane H ϩ -ATPase by a phosphorylation or dephosphorylation event (de Boer et al, 1994;van der Hoeven et al, 1996;Marra et al, 1994). The other model involves the fusicoccin binding protein directly regulating the H ϩ -ATPase (Marrè , 1979;De Michelis et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

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Summary

Baunsgaard¹,

Fuglsang²,

Jahn³

et al. 1998

The Plant Journal

202

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SummaryThe plasma membrane H ϩ -ATPase in higher plants has been implicated in nutrient uptake, phloem loading, elongation growth and establishment of turgor. Although a C-terminal regulatory domain has been identified, little is known about the physiological factors involved in controlling the activity of the enzyme. To identify components which play a role in the regulation of the plant H ϩ -ATPase, a fusicoccin responsive yeast expressing Arabidopsis plasma membrane H ϩ -ATPase AHA2 was employed. By testing the fusicoccin binding activity of yeast membranes, the C-terminal regulatory domain of AHA2 was found to be part of a functional fusicoccin receptor, a component of which was the 14-3-3 protein. ATP hydrolytic activity of AHA2 expressed in yeast internal membranes was activated by all tested isoforms of the 14-3-3 protein of yeast and Arabidopsis, but only in the presence of fusicoccin, and activation was prevented by a phosphoserine peptide representing a known 14-3-3 protein binding motif in Raf-1. The results demonstrate that the 14-3-3 protein is an activator molecule of the H ϩ -ATPase and provides the first evidence of a protein involved in activation of plant plasma membrane H ϩ -ATPase.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Summary

Baunsgaard¹,

Fuglsang²,

Jahn³

et al. 1998

The Plant Journal

202

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“…The underside of the strips was brushed with a zero size painting brush to remove the adhering mesophyll cells (9). The strips were exposed to ultrasonication (5 The hormonal control of stomatal movement is one of the impressive adaptations of plants to water stress (1,16). However, among several plant growth regulators, only a few exert a marked influence on stomata in isolated epidermis.…”

mentioning

confidence: 99%

“…Stomatal opening is suppressed by ABA (4) and promoted by cytokinins (3) or auxins (14). Fusicoccin, a fungal toxin, enhances remarkably stomatal opening (5).…”

mentioning

confidence: 99%

Action of Proline on Stomata Differs from That of Abscisic Acid, G-Substances, or Methyl Jasmonate

Raghavendra¹,

Reddy²

1987

Plant Physiol.

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“…The fungal phytotoxin fusicoccin (FC) is one of the most powerful effectors of the plasma membrane H--ATPase [5]. Upon binding to plasma membrane receptors [6][7][8], it rapidly and persistently stimulates the enzyme, thus triggering cell growth and membrane transport [5].…”

Section: Introductionmentioning

confidence: 99%

The H⁺‐ATPase purified from maize root plasma membranes retains fusicoccin in vivo activation

et al. 1996

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The activity of 'P-type' ATPases is modulated through the C-terminal autoinhibitory domain. The molecular bases of this regulation are unknown. Their understanding demands functional and structural studies on the activated purified enzyme. In this paper the plasma membrane H+-ATPase from maize roots activated in vivo by fusicoccin was solubilised and fractionated by anion-exchange HPLC. Results showed that the H+-ATPase separated from fusicoccin receptors retained fusicoccin activation and that it was more evident after enzyme insertion into liposomes. These data suggest that fusicoccin stimulation does not depend on a direct action of the fusicoccin receptor on the H+-ATPase, but rather, fusicoccin brings about a permanent modification of the H+-ATPase which very likely represents a general regulatory mechanism for 'P-type' ATPases.

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Fusicoccin: A Tool in Plant Physiology

Cited by 791 publications

References 53 publications

Summary

Summary

Action of Proline on Stomata Differs from That of Abscisic Acid, G-Substances, or Methyl Jasmonate

The H⁺‐ATPase purified from maize root plasma membranes retains fusicoccin in vivo activation

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Fusicoccin: A Tool in Plant Physiology

Cited by 791 publications

References 53 publications

Summary

Summary

Action of Proline on Stomata Differs from That of Abscisic Acid, G-Substances, or Methyl Jasmonate

The H+‐ATPase purified from maize root plasma membranes retains fusicoccin in vivo activation

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The H⁺‐ATPase purified from maize root plasma membranes retains fusicoccin in vivo activation