Antibodies to the CFTR modulate the turgor pressure of guard cell protoplasts via slow anion channels

FEBS Letters

Richaud, Pierre¹  Forestier, Cyrille¹  Leonhardt, Nathalie¹  Marin, Elena¹  Bazin, Ingrid¹  Vavasseur, Alain¹ 

[1] CEA Cadarache, Direction des Sciences du Vivant, Département d'Ecophysiologie Végétale et de Microbiologie, Laboratoire des Echanges Membranaires et Signalisation, UMR 6000 CNRS-CEA, P.O. Box 1, F-13108 St Paul-lez-Durance Cedex, France

关键词: Guard cell;    Anion channel;    Cystic fibrosis transmembrane conductance regulator;    ATP-binding cassette protein;    Vicia faba;    ABC;    ATP-binding cassette;    BSA;    bovine serum albumin;    CFTR;    cystic fibrosis transmembrane conductance regulator;    GCPs;    guard cell protoplasts;    PVDF;    polyvinylidene difluoride;    SUR;    sulfonylurea receptor;   

DOI  :  10.1016/S0014-5793(01)02289-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The plasma membrane guard cell slow anion channel is a key element at the basis of water loss control in plants allowing prolonged osmolite efflux necessary for stomatal closure. This channel has been extensively studied by electrophysiological approaches but its molecular identification is still lacking. Recently, we described that this channel was sharing some similarities with the mammalian ATP-binding cassette protein, cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel [Leonhardt, N. et al. (1999) Plant Cell 11, 1141–1151]. Here, using the patch-clamp technique and a bioassay, consisting in the observation of the change in guard cell protoplasts volume, we demonstrated that a functional antibody raised against the mammalian CFTR prevented ABA-induced guard cell protoplasts shrinking and partially inhibited the slow anion current. Moreover, this antibody immunoprecipitated a polypeptide from guard cell protein extracts and immunolabeled stomata in Vicia faba leaf sections. These results indicate that the guard cell slow anion channel is, or is closely controlled by a polypeptide, exhibiting one epitope shared with the mammalian CFTR.

【 授权许可】

Unknown