Journal
PLANT CELL AND ENVIRONMENT
Volume 31, Issue 2, Pages 218-226Publisher
BLACKWELL PUBLISHING
DOI: 10.1111/j.1365-3040.2007.01754.x
Keywords
HSP70; signal transduction
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A heat-activated MAP kinase (HAMK), immunologically related to the extracellular signal-regulated kinase (ERK) super-family of protein kinases, has been identified in BY2 cells of tobacco. The activation of HAMK at 37 degrees C was transient and detected within 2 min and reached a maximum level within 5 min. Ca2+ chelators and channel blockers, and the known inhibitors of MEK, a MAP kinase kinase, prevented the heat activation of HAMK. This suggests that HAMK activation is part of a heat-triggered MAP kinase cascade that requires Ca2+ influx. The heat shock protein HSP70 accumulated at 37 degrees C, but not when HAMK activation was prevented with the inhibitors of MEK or with Ca2+ chelators or channel blockers. As previously shown for heat activation of HAMK, heat-induced accumulation of HSP70 requires membrane fluidization and reorganization of cytoskeleton. We concluded that heat-triggered HAMK cascade might play an essential role in the launching of heat shock response and hsp gene expression in tobacco cells.
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