The major vault protein is the predominant member of a large cytosolic
ribonucleoprotein particle, named vaults. Vaults are abundant in nerv
e terminals of the electric organ of Torpedo marmorata. Negative stain
ing of isolated vaults reveals particle dimensions of 45 X 65 nm in si
ze. Comparison of the major vault protein (MVP100) from the two electr
ic ray species Torpedo marmorata and Discopyge ommata reveals few micr
oheterogeneities in amino acid sequence. Potential phosphorylation sit
es for various protein kinases are highly conserved. Phosphorylation s
tudies demonstrate that the major vault protein of Torpedo is a substr
ate of various protein kinases. MVP100 is phosphorylated by protein ty
rosine kinase in vivo and protein kinase C and casein kinase II in vit
ro. Inhibitors and activators of protein kinases specifically modulate
the phosphorylation of MVP100.