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Titolo:
14-3-3 proteins double the number of outward-rectifying K+ channels available for activation in tomato cells
Autore:
Booij, PP; Roberts, MR; Vogelzang, SA; Kraayenhof, R; de Boer, AH;
Indirizzi:
Free Univ Amsterdam, Biocentrum Amsterdam, Dept Dev Genet, NL-1081 HV Amsterdam, Netherlands Free Univ Amsterdam Amsterdam Netherlands NL-1081 HV terdam, Netherlands Free Univ Amsterdam, Biocentrum Amsterdam, Dept Biol Struct, NL-1081 HV Amsterdam, Netherlands Free Univ Amsterdam Amsterdam Netherlands NL-1081 HVterdam, Netherlands Univ York, Dept Biol, Plant Lab, York YO1 5DD, N Yorkshire, England Univ York York N Yorkshire England YO1 5DD YO1 5DD, N Yorkshire, England
Titolo Testata:
PLANT JOURNAL
fascicolo: 6, volume: 20, anno: 1999,
pagine: 673 - 683
SICI:
0960-7412(199912)20:6<673:1PDTNO>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
MEMBRANE H+-ATPASE; XYLEM PARENCHYMA CELLS; PLASMA-MEMBRANE; GUARD-CELLS; VICIA-FABA; 14-3-3-PROTEINS ASSOCIATE; PLANT 14-3-3-PROTEINS; POTASSIUM CURRENT; MESOPHYLL-CELLS; PROTOPLASTS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
51
Recensione:
Indirizzi per estratti:
Indirizzo: de Boer, AH Free Univ Amsterdam, Biocentrum Amsterdam, Dept Dev Genet, Boelelaan 1087,NL-1081 HV Amsterdam, Netherlands Free Univ Amsterdam Boelelaan1087 Amsterdam Netherlands NL-1081 HV
Citazione:
P.P. Booij et al., "14-3-3 proteins double the number of outward-rectifying K+ channels available for activation in tomato cells", PLANT J, 20(6), 1999, pp. 673-683

Abstract

Outward-rectifying K+ channels are modulated in response to environmental stimuli by a range of intracellular factors, such as cytoplasmic Ca2+, pH, kinases and phosphatases. Here we report that voltage-dependent outward-rectifying K+ channels in tomato cells are also targets for modulation by 14-3-3 proteins. In whole-cell patch-clamp experiments, recombinant 14-3-3 protein (tomato isoform TFT7) was introduced into tomato cell protoplasts via the patch pipette. As a result the steady-state outward K+ current increasedtwofold and this increase was not dependent upon the presence of cytoplasmic ATP. A phosphorylated peptide that contained a phosphorylated 14-3-3 target-binding motif (RSTS*TP), derived from nitrate reductase, blocked the effect of 14-3-3, thus showing the specific nature of 14-3-3 action. Kinetic parameters of the conductance, like (de)activation kinetics, voltage dependence of gating and activation potential, were not significantly different between control and 14-3-3 infused cells. Analysis of single-channel activity and whole-cell noise indicated that the single-channel conductance was not affected by 14-3-3 infusion. We conclude that 14-3-3 proteins recruit 'sleepy' channels into a voltage-activatable state. The molecular mechanism underlying the 1 : 1 ratio of constitutively active and 14-3-3 recruited channels is discussed in the light of known functions of 14-3-3 dimers.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 01:56:52