Journal
FEBS LETTERS
Volume 527, Issue 1-3, Pages 43-50Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(02)03162-9
Keywords
hypoosmotic stress; hyperosmotic stress; mitogen-activated protein kinase; Arabidopsis thaliana
Ask authors/readers for more resources
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. (C) 2002 Federation of European Biochemical Societies.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available