Journal
PLANT CELL
Volume 12, Issue 1, Pages 165-178Publisher
AMER SOC PLANT PHYSIOLOGISTS
DOI: 10.1105/tpc.12.1.165
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In tobacco cells, osmotic stress induced the rapid activation of two protein kinases that phosphorylate myelin basic protein. Immunological studies demonstrated that the 48-kD kinase is the salicylic acid-induced protein kinase (SIPK), a member of the mitogen-activated protein kinase family. SIPK was activated 5 to 10 min after the cells were exposed to osmotic stresses, and its activity persisted for similar to 30 min. In contrast, the 42-kD kinase was activated within 1 min after osmotic stress, and its activity was maintained for similar to 2 hr Moreover, in addition to myelin basic protein, the 42-kD kinase phosphorylated casein and two transcription factors, c-Jun and ATF-2. This latter enzyme was inactivated by a serine/threonine-specific phosphatase but, unlike SIPK, was not affected by a tyrosine-specific phosphatase. After the 42-kD kinase was purified to apparent homogeneity, tryptic peptide analysis indicated that it is a homolog of Arabidopsis serine/threonine kinase 1 (ASK1).
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