Herrmann C, Kellner R, Volknandt W
AK Neurochemie, Biozentrum, Zoologisches Institut der Universität Frankfurt, Frankfurt am Main, Germany.
Neurochem Res. 1998 Jan;23(1):39-46. doi: 10.1023/a:1022445302710.
The major vault protein is the predominant member of a large cytosolic ribonucleoprotein particle, named vaults. Vaults are abundant in nerve terminals of the electric organ of Torpedo marmorata. Negative staining of isolated vaults reveals particle dimensions of 45x65 nm in size. Comparison of the major vault protein (MVP100) from the two electric ray species Torpedo marmorata and Discopyge ommata reveals few microheterogeneities in amino acid sequence. Potential phosphorylation sites for various protein kinases are highly conserved. Phosphorylation studies demonstrate that the major vault protein of Torpedo is a substrate of various protein kinases. MVP100 is phosphorylated by protein tyrosine kinase in vivo and protein kinase C and casein kinase II in vitro. Inhibitors and activators of protein kinases specifically modulate the phosphorylation of MVP100.
主要穹窿蛋白是一种名为穹窿体的大型胞质核糖核蛋白颗粒中的主要成分。穹窿体在电鳐电器官的神经末梢中含量丰富。对分离出的穹窿体进行负染色显示,颗粒尺寸为45×65纳米。对电鳐属的电鳐和眼斑电鲼这两种电鳐的主要穹窿蛋白(MVP100)进行比较,发现氨基酸序列中几乎没有微小异质性。各种蛋白激酶的潜在磷酸化位点高度保守。磷酸化研究表明,电鳐的主要穹窿蛋白是各种蛋白激酶的底物。MVP100在体内被蛋白酪氨酸激酶磷酸化,在体外被蛋白激酶C和酪蛋白激酶II磷酸化。蛋白激酶的抑制剂和激活剂能特异性调节MVP100的磷酸化。