pICln inhibits snRNP biogenesis by binding core spliceosomal proteins.
pICln inhibits snRNP biogenesis by binding core spliceosomal proteins.
复制标题
pICln 通过结合核心剪接体蛋白来抑制 snRNP 生物发生。
DOI：
10.1128/mcb.19.6.4113
复制
发表时间：
1999
影响因子：
5.3
通讯作者：
Clapham,DE
中科院分区：
文献类型：
--
作者：
Pu,WT;Krapivinsky,GB;Krapivinsky,L;Clapham,DE
The U1, U2, U4, U5, and U6 small nuclear ribonucleoproteins (snRNPs) form essential components of spliceosomes, the machinery that removes introns from pre-mRNAs in eukaryotic cells. A critical initial step in the complex process of snRNP biogenesis is the assembly of a group of common core proteins (Sm proteins) on spliceosomal snRNA. In this study we show by multiple independent methods that the protein pICln associates with Sm proteins in vivo and in vitro. The binding of pICln to Sm proteins interferes with Sm protein assembly on spliceosomal snRNAs and inhibits import of snRNAs into the nucleus. Furthermore, pICln prevents the interaction of Sm proteins with the survival of motor neurons (SMN) protein, an interaction that has been shown to be critical for snRNP biogenesis. These findings lead us to propose a model in which pICln participates in the regulation of snRNP biogenesis, at least in part by interfering with Sm protein interaction with SMN protein.
