SERINE THREONINE PHOSPHORYLATION REGULATES BINDING OF C-HNRNP PROTEINS TO PREMESSENGER RNA

被引：69

作者：

MAYRAND, SH ^{[1
]}

DWEN, P ^{[1
]}

PEDERSON, T ^{[1
]}

机构：

[1] WORCESTER FDN EXPTL BIOL INC, CELL BIOL GRP, SHREWSBURY, MA 01545 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1993年 / 90卷 / 16期

关键词：

CASEIN KINASE-II; OKADAIC ACID; PROTEIN PHOSPHATASE; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN; MESSENGER RNA SPLICING;

D O I：

10.1073/pnas.90.16.7764

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The C hnRNP proteins bind to nascent preMRNA and are thought to participate in an early step of the pre-mRNA splicing pathway. We report here that C hnRNP proteins are phosphorylated by a casein kinase II activity in a HeLa cell nuclear extract and that dephosphorylation of C hnRNP proteins is inhibited by the specific protein-serine/threonine-phosphatase 1/2A inhibitor okadaic acid. We further find that dephosphorylation of C hnRNP proteins is required for their binding to adenovirus and human beta-globin pre-mRNAs. These results indicate that the participation of C hnRNP proteins in pre-spliceosome assembly is coupled to a dynamic cycle of their phosphorylation and dephosphorylation.

引用

页码：7764 / 7768

页数：5

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