Different protein kinase families are activated by osmotic stresses in Arabidopsis thaliana cell suspensions

FEBS Letters

Droillard, Marie-Jo¹  Barbier-Brygoo, Hélène¹  Boudsocq, Marie¹  Laurière, Christiane¹ 

[1] Institut des Sciences du Végétal, UPR 2355, CNRS, 1 av. de la terrasse, 91198 Gif s/Yvette Cedex, France

关键词: Hypoosmotic stress;    Hyperosmotic stress;    Mitogen-activated protein kinase;    Arabidopsis thaliana;    MAP kinase;    mitogen-activated protein kinase;    MBP;    myelin basic protein;   

DOI  :  10.1016/S0014-5793(02)03162-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Five Ca²⁺-independent protein kinases were rapidly activated by hypoosmotic stress, moderate or high hyperosmolarity induced by several osmolytes, sucrose, mannitol or NaCl. Three of these kinases, transiently activated by hypoosmolarity, recognised by anti-phosphorylated mitogen-activated protein (MAP) kinase antibodies, sensitive to a MAP kinase inhibitor and inactivated by the action of a tyrosine phosphatase, corresponded to MAP kinases. Using specific antibodies, two of the MAP kinases were identified as AtMPK6 and AtMPK3. The two other protein kinases, durably activated by high hyperosmolarity, did not belong to the MAP kinase family. Activation of AtMPK6 and AtMPK3 by hypoosmolarity depended on upstream protein kinases sensitive to staurosporine and on calcium influx. In contrast, these two transduction steps were not involved in the activation of the two protein kinases activated by high hyperosmolarity.

【 授权许可】

Unknown