THE MAJOR PHOSPHORYLATION SITE OF NUCLEOPHOSMIN (B23) IS PHOSPHORYLATED BY A NUCLEAR KINASE-II

被引：51

作者：

CHAN, PK

LIU, QR

DURBAN, E

机构：

[1] Department of Pharmacology, Baylor College of Medicine, Houston

来源：

BIOCHEMICAL JOURNAL | 1990年 / 270卷 / 02期

关键词：

D O I：

10.1042/bj2700549

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Nucleophosmin (B23) was phosphorylated in vitro with [γ-32P]ATP and a nuclear kinase (type II) purified from HeLa cells. The phosphorylation was inhibited by heparin and by 2,3-diphosphoglycerate. Peptide mapping analysis indicated that the phosphorylation site in vitro was identical to that in vivo. Purified nucleoli have a similar kinase that phosphorylated nucleophosmin at the same site. These results indicated that nucleophosmin is phosphorylated in vivo by a nucleolar kinase (type II).

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页码：549 / 552

页数：4

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