Environmental and hormonal signals control diverse physiological processes in plants. The mechanisms by which plant cells perceive and transduce these signals are poorly understood. Understanding biochemical and molecular events involved in signal transduction pathways has become one of the most active areas of plant research. Research during the last 15 years has established that Ca2+ acts as a messenger in transducing external signals. The evidence in support of Ca2+ as a messenger is unequivocal and fulfills all the requirements of a messenger. The role of Ca2+ becomes even more important because it is the only messenger known so far in plants. Since our last review on the Ca2+ messenger system in 1987, there has been tremendous progress in elucidating various aspects of Ca(2+) -signaling pathways in plants. These include demonstration of signal-induced changes in cytosolic Ca2+, calmodulin and calmodulin-like proteins, identification of different Ca2+ channels, characterization of Ca(2+) -dependent protein kinases (CDPKs) both at the biochemical and molecular levels, evidence for the presence of calmodulin-dependent protein kinases, and increased evidence in support of the role of inositol phospholipids in the Ca(2+) -signaling system. Despite the progress in Ca2+ research in plants, it is still in its infancy and much more needs to be done to understand the precise mechanisms by which Ca2+ regulates a wide variety of physiological processes. The purpose of this review is to summarize some of these recent developments in Ca2+ research as it relates to signal transduction in plants.

Environmental and hormonal signals control diverse physiological processes in plants. The mechanisms by which plant cells perceive and transduce these signals are poorly understood. Understanding biochemical and molecular events involved in signal transduction pathways has become one of the most active areas of plant research. Research during the last 15 years has established that Ca2+ acts as a messenger in transducing external signals. The evidence in support of Ca2+ as a messenger is unequivocal and fulfills all the requirements of a messenger. The role of Ca2+ becomes even more important because it is the only messenger known so far in plants. Since our last review on the Ca2+ messenger system in 1987, there has been tremendous progress in elucidating various aspects of Ca(2+) -signaling pathways in plants. These include demonstration of signal-induced changes in cytosolic Ca2+, calmodulin and calmodulin-like proteins, identification of different Ca2+ channels, characterization of Ca(2+) -dependent protein kinases (CDPKs) both at the biochemical and molecular levels, evidence for the presence of calmodulin-dependent protein kinases, and increased evidence in support of the role of inositol phospholipids in the Ca(2+) -signaling system. Despite the progress in Ca2+ research in plants, it is still in its infancy and much more needs to be done to understand the precise mechanisms by which Ca2+ regulates a wide variety of physiological processes. The purpose of this review is to summarize some of these recent developments in Ca2+ research as it relates to signal transduction in plants.

No abstract

No abstract

The kinesin family motor protein KCBP (kinesin-like calmodulin binding protein) was identified during a screen for Arabidopsis calmodulin-binding proteins [Reddy, et al., 1996b: J. Biol Chem. 271:7052-7060]. KCBP contains a C-terminal motor domain and is unique among kinesin motors in that it has a calmodulin-binding site. We expressed the KCBP motor domain in Escherichia coli and examined its microtubule (MT) binding and ATPase activity. KCBP bound MTs in an ATP-dependent manner and exhibited MT-stimulated ATPase activity. Ca2+/ calmodulin inhibited binding of KCBP to MTs under conditions that normally favor tight motor-MT interactions, and the extent of inhibition was dependent on the concentration of calcium and calmodulin. Ca2+/calmodulin did not affect KCBP's basal ATPase activity, but reduced the motor's MT-stimulated ATPase activity. The substantial reduction in affinity of KCBP for MTs in the presence of Ca2+/calmodulin suggests that Ca2+/calmodulin may modulate the activity of KCBP in vivo by regulating the motor's association with MTs. KCBP is the first MT-dependent motor protein found to be regulated by direct binding of Ca2+/calmodulin to its motor subunit.