A Calcium/Calmodulin-Binding Serine/Threonine Protein Kinase Homologous to the Mammalian Type II Calcium/Calmodulin-Dependent Protein Kinase Is Expressed in Plant Cells

Abstract

cDNA fragments corresponding to an apple (Malus domestica[LI Borkh) calmodulin-binding polypeptide have been isolated and characterized. l h e protein encoded by this messenger contains a serine/threonine protein kinase catalytic domain followed by a calcium/calmodulin-binding regulatory domain, both exhibiting significant sequence similarities to the corresponding regions of the mammalian calcium/calmodulin-dependent protein kinase II subunits. These results confirm a potential regulatory role for calmodulin in phosphorylation-mediated signal transduction events.

Measurement of Ca2+ Fluxes during Elicitation of the Oxidative Burst in Aequorin-transformed Tobacco Cells

“…Moreover, it can be argued that the proximal Ca 2ϩ -dependent effector in the signaling pathway may be similarly transiently activated, returning to its resting state when the activating Ca 2ϩ is removed. Signaling components such as the Ca 2ϩ -dependent protein kinases (55,56), calmodulin (57) and its responsive kinases (58,59), Ca 2ϩ -dependent phosphatases (60), Ca 2ϩ -gated channels (61), and Ca 2ϩ -activated phospholipases (62) are obvious candidates for this downstream effector.…”

Molecular and Biochemical Analysis of Calmodulin Interactions with the Calmodulin-Binding Domain of Plant Glutamate Decarboxylase

“…These include protein kinases (Colbran and Soderling, 1991), protein phosphatases (Guerini et al, 1991), Ca2+ pumps (Hofmann et al, 1994), structural proteins (Hartwig et al, 1992), transcription factors (Corneliussen et al, 1994), and others. In contrast, little is known about the number, localization, identity, and structure of CaM-target proteins in plants (Ling and Assmann, 1992;Baum et al, 1993;Watillon et al, 1993;Hsieh and Roux, 1994;Lu and Harrington, 1994). The lack of information concerning plant CaM-target proteins has been a major obstacle in elucidating Ca2+-mediated signal transduction mechanisms in plants.…”

A plant kinesin heavy chain‐like protein is a calmodulin‐binding protein

“…Although very little is known about the identity and function of calmodulin-binding proteins in plants, gel overlay assays have been used to demonstrate a number of tissue specific proteins that bind to calmodulin in a calcium-dependent manner (Kobayashi and Fukuda, 1994;Ling and Assmann, 1992;Oh et al, 1992). In plants, studies on calmodulin-binding proteins are limited to NAD kinase, calcium ATPase, nuclear nucleoside triphosphatase, a vacuolar ion channel, glutamate decarboxylase, elongation factor-l~, protein kinases and a few other proteins of unknown function (Baum et al, 1993;Bethke and Jones, 1994;Durso and Cyr, 1994;Ling et al, 1994;Lu and Harrington, 1994;Patil et al, 1995;Reddy et al, 1993;Roberts and Harmon, 1992;Watillon et al, 1993). In potato, tuberization is controlled by a number of environmental factors and hormones (Ewing, 1990) and the expression of tuberization stimulus appears to be mediated by calcium and calmodulin (Balamani etal., 1986;Jena et al, 1989).…”