Plants also have a range of Ca2+-dependent(but calmodulin independent)
protein kinases. Protein kinases are important in signal transduction pathways
as they phosphorylate other proteins at specific sites, altering their activity.
Inositol trisphosphate
Theinositol triphosphate(IP 3 ) pathway begins with the conversion of a plasma
membrane lipid, phosphatidyl inositolintophosphatidyl inositol bisphos-
phate (PIP 2 ) by kinase enzymes in the plasma membrane. PIP 2 is then
hydrolyzed by phospholipase C(PLC) to give IP 3 anddiacylglycerol(DAG).
PLC activity is regulated by a signal transduction pathway initiated by the
binding of a hormone to a receptor, so IP 3 and DAG levels respond to stimuli.
IP 3 causes Ca2+channels to open at the tonoplast (vacuole) and endoplasmic
reticulum, resulting in a Ca2+signal being initiated (see above). DAG activates
protein kinase Cthat regulates other processes. Figure 4summarizes the Ca2+
and inositol trisphosphate signaling pathways.
82 Section F – Growth and development
Hormone receptor Protein kinase C
Cell membrane
G-protein Phospholipase C
PIP 2
DAG
Ca2+ Ca
2+
Ca2+Ca
2+
Ca2+
Ca2+
Ca2+
Ca2+
Ca2+
Ca2+
Ca2+
Ca2+
Ca2+
Ca2+
Protein phosphorylation
(leads to altered cell function)
Endoplasmic reticulum
Vacuole
IP 3 -sensitive calcium channels
IP 3
IP 3 IP 3
IP 3 IP^3
Fig. 4. Intracellular messengers. Release of Ca2+from the endoplasmic reticulum (ER) and
vacuole results in a transient rise in cytoplasmic Ca2+concentration. The Ca2+binds with
proteins like calmodulin- and Ca2+-dependent protein kinases to alter cell function.