Direct interaction between hnRNP-M and CDC5L/PLRG1 proteins affects alternative splice site choice

被引：56

作者：

Lleres, David ^{[1
]}

Denegri, Marco ^{[1
]}

Biggiogera, Marco ^{[2
,3
]}

Ajuh, Paul ^{[1
]}

Lamond, Angus I. ^{[1
]}

机构：

[1] Univ Dundee, Coll Life Sci, Wellcome Trust Ctr Gene Regulat & Express, Dundee DD1 5EH, Scotland

[2] Univ Pavia, Dipartimento Biol Anim, Lab Biol Cellulare, I-27100 Pavia, Italy

[3] Univ Pavia, Dipartimento Biol Anim, Ctr Studio Istochim CNR, I-27100 Pavia, Italy

来源：

EMBO REPORTS | 2010年 / 11卷 / 06期

基金：

英国惠康基金;

关键词：

alternative pre-mRNA splicing; FLIM-FRET; CDC5L; hnRNP-M; spliceosome; MESSENGER-RNA; IN-VIVO; RIBONUCLEOPROTEIN-M; HEAT-SHOCK; IDENTIFICATION; COMPLEX; SUBSET; BODIES; CELLS; CDC5L;

D O I：

10.1038/embor.2010.64

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：

Heterogeneous nuclear ribonucleoprotein-M (hnRNP-M) is an abundant nuclear protein that binds to pre-mRNA and is a component of the spliceosome complex. A direct interaction was detected in vivo between hnRNP-M and the human spliceosome proteins cell division cycle 5-like (CDC5L) and pleiotropic regulator 1 (PLRG1) that was inhibited during the heat-shock stress response. A central region in hnRNP-M is required for interaction with CDC5L/PLRG1. hnRNP-M affects both 50 and 30 alternative splice site choices, and an hnRNP-M mutant lacking the CDC5L/PLRG1 interaction domain is unable to modulate alternative splicing of an adeno-E1A mini-gene substrate.

引用

页码：445 / 451

页数：7

共 28 条

[1] Functional analysis of the human CDC5L complex and identification of its components by mass spectrometry [J].