RUVBL1-RUVBL2 AAA-ATPase: a versatile scaffold for multiple complexes and functions

被引：48

作者：

Dauden, Maria, I ^{[1
]}

Lopez-Perrote, Andres ^{[1
]}

Llorca, Oscar ^{[1
]}

机构：

[1] Spanish Natl Canc Res Ctr CNIO, Struct Biol Programme, Melchor Fernandez Almagro 3, Madrid 28029, Spain

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2021年 / 67卷

关键词：

STRUCTURAL BASIS; R2TP COMPLEX; CHROMATIN; ARCHITECTURE; CHAPERONE; HSP90; TEL2;

D O I：

10.1016/j.sbi.2020.08.010

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：

RUVBL1 and RUVBL2 are two highly conserved AAA+ ATPases that form a hetero-hexameric complex that participates in a wide range of unrelated cellular processes, including chromatin remodeling, Fanconi Anemia (FA), nonsense-mediated mRNA decay (NMD), and assembly and maturation of several large macromolecular complexes such as RNA polymerases, the box C/D small nucleolar ribonucleoprotein (snoRNP) and mTOR complexes. How the RUVBL1-RUVBL2 complex works in such a variety of processes, sometimes antagonistic, has been obscure for a long time. Recent cryo-electron microscopy (cryo-EM) studies have started to reveal how RUVBL1- RUVBL2 forms a scaffold for complex protein-protein interactions and how the structure and ATPase activity of RUVBL1-RUVBL2 can be affected and regulated by the interaction with clients.

引用

页码：78 / 85

页数：8

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