IntroductionOilseeds store oil in the form of triacylglycerols (TAGs) in the organelles known as oil bodies. TAGs are rapidly converted to soluble metabolites via specialized metabolic pathways upon initiation of seed germination. 1 The protein constituents of oil bodies belong to the three major groups, comprising of structural proteins (oleosins and caleosins), enzymes (steroleosins and lipases) and minor proteins, like aquaporins. 2 The sequence of events prior to TAG hydrolysis by lipases to produce free fatty acids and glycerol, involves degradation of oleosins by a 65 kDa thiol protease 3,4 and phospholipid degradation by phospholipases. 5 This renders TAG matrix susceptible to lipase action. Oleosins are known to provide stability to oil bodies while caleosins play an important role in the biogenesis and degradation of oil bodies. 6,7 Calcium binding capacity of caleosins has been demonstrated in Arabidopsis and Sesamum indicum. 8,9 Recently, calcium concentrations as low as 100 nM have been shown to strongly modify the shape and aggregation state of purified oil bodies, thereby establishing the role of caleosins not only as a target for calcium-binding in artificial and purified oil bodies, but also as an effecter of oil body stability. 2 During seed germination, caleosins are involved in the interaction of lipid bodies with vacuoles and, thus, they play a role in the mobilization of storage lipids. 10 Based on these findings and observations from the author's laboratory on calcium-dependent proteolysis, the possibility of cation channels on/around the oil body surface for facilitating calcium availability could not be ruled out.In plant cells, ion channels permeable to Ca 2+ are so far known to exist on the plasma membrane, endoplasmic reticulum, tonoplast, nuclear and plastid membranes. 11 Electrophysiological studies have elucidated that plants possess Ca 2+ channels with different types of gating mechanisms, namely ligand-, voltageand stretch-activated. 12 Ca 2+ channels in plant cells are similar to the L-type channels characterized in animal systems. 13