PIM3 激酶，一种原癌基因产物，调节麻疹病毒核衣壳蛋白尾部结构域丝氨酸 479 和丝氨酸 510 的磷酸化。

PIM 3 kinase, a proto-oncogene product, regulates phosphorylation of the measles virus nucleoprotein tail domain at Ser 479 and Ser 510.

机构信息

Institute of Industrial Science, The University of Tokyo, 4-6-1 Komaba, Meguro-ku, Tokyo, 153-8505, Japan.

出版信息

Biochem Biophys Res Commun. 2020 Oct 20;531(3):267-274. doi: 10.1016/j.bbrc.2020.06.002. Epub 2020 Aug 14.

DOI:10.1016/j.bbrc.2020.06.002

Abstract

The tail domain of the measles virus (MeV) N protein is typically phosphorylated at S479 and S510. However, the protein kinase responsible for this phosphorylation has not been identified. To identify the protein kinase responsible, we conducted an in vitro kinase assay in the presence of various protein kinase inhibitors. Phosphorylation of S479 and S510 was suppressed in the presence of SP600125. We demonstrated that purified PIM 3 kinase, which is sensitive to SP600125, successfully phosphorylated both phosphorylation sites. Inhibitors of PIM kinase, CX6258 and LY294002, also suppressed phosphorylation of the N protein. These findings indicate that PIM 3 kinase is associated with the tail domain of the N protein and that PIM 3 kinase regulates N protein phosphorylation.

摘要

麻疹病毒（MeV）N 蛋白的尾部结构域通常在 S479 和 S510 处发生磷酸化。然而，负责这种磷酸化的蛋白激酶尚未被鉴定。为了鉴定负责的蛋白激酶，我们在存在各种蛋白激酶抑制剂的情况下进行了体外激酶测定。在 SP600125 的存在下，S479 和 S510 的磷酸化被抑制。我们证明，对 SP600125 敏感的纯化 PIM3 激酶成功地磷酸化了这两个磷酸化位点。PIM 激酶的抑制剂 CX6258 和 LY294002 也抑制了 N 蛋白的磷酸化。这些发现表明，PIM3 激酶与 N 蛋白的尾部结构域相关，并且 PIM3 激酶调节 N 蛋白的磷酸化。