Protein kinases induced by osmotic stresses and elicitor molecules in tobacco cell suspensions: two crossroad MAP kinases and one osmoregulation-specific protein kinase. - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue FEBS Letters Année : 2000

Protein kinases induced by osmotic stresses and elicitor molecules in tobacco cell suspensions: two crossroad MAP kinases and one osmoregulation-specific protein kinase.

Résumé

Two protein kinases displaying mitogen-activated protein kinase (MAPK) properties are activated both by an hypoosmotic stress and by oligogalacturonides in tobacco cell suspensions [Cazal?t al. (1999) Plant J. 19, 297-307]. Using specific antibodies, they were identified as the salicylic acid-induced protein kinase (SIPK) and wound-induced protein kinase (WIPK). The SIPK was also activated by an hyperosmotic stress, indicating that the same kinase may play a role both in hypo- and hyperosmotic signalling pathways, in addition to its involvement in the transduction of elicitor signals. Using immunoprecipitation followed by two-dimensional in-gel kinase assay, three molecular forms of the SIPK were observed, suggesting that additional modifications of the activated kinase may occur. In contrast to WIPK and SIPK, which are located at the crossroad of several transduction pathways initiated by elicitor or osmotic stimuli, a 44 kDa kinase, that would not belong to the MAPK family, appeared more specific to osmotic stress.

Dates et versions

hal-00161034 , version 1 (09-07-2007)

Identifiants

Citer

M. J. Droillard, S. Thibivilliers, A. C. Cazalé, H. Barbier-Brygoo, C. Laurière. Protein kinases induced by osmotic stresses and elicitor molecules in tobacco cell suspensions: two crossroad MAP kinases and one osmoregulation-specific protein kinase.. FEBS Letters, 2000, 474 (2-3), pp.217-22. ⟨10.1016/S0014-5793(00)01611-2⟩. ⟨hal-00161034⟩
17 Consultations
0 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More