Fusicoccin Binding to Its Plasma Membrane Receptor and the Activation of the Plasma Membrane H+-ATPase (III. Is There a Direct Interaction between the Fusicoccin Receptor and the Plasma Membrane H+-ATPase?)

Michelis, Maria Ida De; Rasi‐Caldogno, Franca; Pugliarello, Maria Chiara; Olivari, C.

doi:10.1104/pp.110.3.957

Cited by 32 publications

(18 citation statements)

References 39 publications

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“…The evidence presented here is supported by biochemical data on cosedimentation of H +-ATPase and fusicoccin binding activity (Cocucci and Marrè, 1991), copurification of the H+-ATPase and 14-3-3 protein that is abolished by trypsin treatment (Oecking et al, 1997), and recent data of De Michelis et al (1996). Using antibodies specific to fusicoccin, De Michelis et al (1996) showed a linear correlation between the amount of fusicoccin bound to the plasma membrane and activation of the H+-ATPase and suggested that no amplification step was needed but that activation of H+ pumping could be explained by direct interaction between the 14-3-3 protein and the H+-ATPase.…”

Section: Discussionsupporting

confidence: 83%

The 14-3-3 protein interacts directly with the C-terminal region of the plant plasma membrane H(+)-ATPase.

et al. 1997

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Section: Discussionsupporting

confidence: 83%

The 14-3-3 protein interacts directly with the C-terminal region of the plant plasma membrane H(+)-ATPase.

et al. 1997

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“…PM fractions were separated from microsomal preparations by partitioning in an aqueous polymer two-phase system, as described previously (De Michelis et al, 1996). The upper (PM) phase as well as the lower phase were used for immunoblot analysis.…”

Section: Density Gradient Fractionation Of Membrane Vesiclesmentioning

confidence: 99%

PGP4, an ATP Binding Cassette P-Glycoprotein, Catalyzes Auxin Transport in Arabidopsis thaliana Roots

et al. 2005

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Members of the ABC (for ATP binding cassette) superfamily of integral membrane transporters function in cellular detoxification, cell-to-cell signaling, and channel regulation. More recently, members of the multidrug resistance P-glycoprotein (MDR/PGP) subfamily of ABC transporters have been shown to function in the transport of the phytohormone auxin in both monocots and dicots. Here, we report that the Arabidopsis thaliana MDR/PGP PGP4 functions in the basipetal redirection of auxin from the root tip. Reporter gene studies showed that PGP4 was strongly expressed in root cap and epidermal cells. PGP4 exhibits apolar plasma membrane localization in the root cap and polar localization in tissues above. Root gravitropic bending and elongation as well as lateral root formation were reduced in pgp4 mutants compared with the wild type. pgp4 exhibited reduced basipetal auxin transport in roots and a small decrease in shoot-to-root transport consistent with a partial loss of the redirective auxin sink in the root. Seedlings overexpressing PGP4 exhibited increased shoot-to-root auxin transport. Heterologous expression of PGP4 in mammalian cells resulted in 1-N-naphthylthalamic acid-reversible net uptake of [ 3 H]indole-3-acetic acid. These results indicate that PGP4 functions primarily in the uptake of redirected or newly synthesized auxin in epidermal root cells.

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“…In fact, it has been demonstrated that FC in vivo treatment of plant tissues, which produces a strong stimulation of H ϩ -ATPase activity, concomitantly brings about a marked increase in plasma membraneassociated 14-3-3 proteins (4,11). Also, the amount of FC bound to plasma membrane appears to be strictly correlated with stimulation of H ϩ -ATPase activity (12). More recent evidence indicates that administration of FC in vivo or in vitro stabilizes (13) or promotes (14) the interaction between H ϩ -ATPase and 14-3-3 proteins.…”

mentioning

confidence: 99%

Fusicoccin Effect on the in Vitro Interaction between Plant 14-3-3 Proteins and Plasma Membrane H+-ATPase

Fullone¹,

Visconti²,

Marra³

et al. 1998

Journal of Biological Chemistry

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A 17-amino acid peptide was selectively cleaved from the highly variant C terminus of the 33-kDa 14-3-3 isoform occurring in fusicoccin receptor preparations from maize and was sequenced. The determined C-terminal sequence was identical to that of the already known maize 14-3-3 homolog GF14-6, thus prompting the use of recombinant GF14-6 in an in vitro protein-protein interaction study. The cDNA of GF14-6 was expressed in Escherichia coli as a 32 P-phosphorylatable glutathione S-transferase fusion protein and was used as a probe in overlay experiments with H ؉ -ATPase partially purified from maize roots. The results demonstrated that the recombinant protein specifically bound to H ؉ -ATPase. The binding was dependent on Mg 2؉ and was strongly increased by fusicoccin. Controlled trypsin digestion of H ؉ -ATPase abolished the association with GF14-6, a finding that was suggestive of an interaction with the C terminus of the enzyme. To confirm this result, the Cterminal domain of H ؉ -ATPase was expressed as a glutathione S-transferase fusion peptide and was used in overlay experiments. GF14-6 was also able to bind to the isolated C terminus, but only in the presence of fusicoccin.

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Fusicoccin Binding to Its Plasma Membrane Receptor and the Activation of the Plasma Membrane H+-ATPase (III. Is There a Direct Interaction between the Fusicoccin Receptor and the Plasma Membrane H+-ATPase?)

Abstract: A radioimmunoassay using antibodies raised against bovine serum albumin-conjugated fusicoccin (FC) was applied to measure FC bound to the plasma membrane (PM) isolated from seedlings of radish (

Cited by 32 publications

References 39 publications

The 14-3-3 protein interacts directly with the C-terminal region of the plant plasma membrane H(+)-ATPase.

The 14-3-3 protein interacts directly with the C-terminal region of the plant plasma membrane H(+)-ATPase.

PGP4, an ATP Binding Cassette P-Glycoprotein, Catalyzes Auxin Transport in Arabidopsis thaliana Roots

Fusicoccin Effect on the in Vitro Interaction between Plant 14-3-3 Proteins and Plasma Membrane H+-ATPase

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