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

Daudén, María I.; López-Perrote, Andrés; Llorca, Óscar

doi:10.1016/j.sbi.2020.08.010

Cited by 45 publications

(33 citation statements)

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“…RUVBL1 and RUVBL2 are highly conserved AAA+ ATPases with diverse functions ranging from chromatin remodeling and nonsense‐mediated mRNA decay to the assembly of kinases (for example mTORC1, ATM, ATR), RNA polymerases and small nucleolar ribonucleoprotein complexes. [ 61 ] The RUVBL1‐RUVBL2 ring exposes two interfaces, an AAA‐face that harbors the ATPase activity and a DII‐face that binds different co‐factors and interacting partners that are required for the diverse functions of RUVBL1‐RUVBL2 (Figure 4A). For instance, recruitment of the additional subunits RPAP3 (Tah1 in yeast) and PIH1D1 to the RUVBL1‐RUVBL2 AAA+ ATPase forms the R2TP core complex, which can bind additional molecular chaperones (Hsp70 and Hsp90).…”

Section: The Ruvbl1‐ruvbl2 Aaa+ Atpase Assists In γ‐Turc Assemblymentioning

confidence: 99%

The gamma‐tubulin ring complex: Deciphering the molecular organization and assembly mechanism of a major vertebrate microtubule nucleator

et al. 2021

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Microtubules are protein cylinders with functions in cell motility, signal sensing, cell organization, intracellular transport, and chromosome segregation. One of the key properties of microtubules is their dynamic architecture, allowing them to grow and shrink in length by adding or removing copies of their basic subunit, the heterodimer αβ-tubulin. In higher eukaryotes, de novo assembly of microtubules from αβ-tubulin is initiated by a 2 MDa multi-subunit complex, the gamma-tubulin ring complex (γ-TuRC). For many years, the structure of the γ-TuRC and the function of its subunits remained enigmatic, although structural data from the much simpler yeast counterpart, the γ-tubulin small complex (γ-TuSC), were available. Two recent breakthroughs in the field, high-resolution structural analysis and recombinant reconstitution of the complex, have revolutionized our knowledge about the architecture and function of the γ-TuRC and will form the basis for addressing outstanding questions about biogenesis and regulation of this essential microtubule organizer. K E Y W O R D Sgamma-tubulin ring complex, gamma-tubulin small complex, gamma-tubulin, microtubule nucleation, microtubules, recombinant gamma-tubulin ring complex Abbreviations: AAA+, adenosine triphosphatases associated with various cellular activities;Arps, actin-related proteins; CDK5RAP2, CDK5 regulatory subunit-associated protein 2; CEP192, centrosomal protein of 192 kDa; ch-TOG, colonic hepatic tumor-overexpressed gene; CM1, centrosomin motif 1; GCP, γ-TuC component protein; γ-TuCs, γ-tubulin complexes; γ-TuRC, γ-tubulin ring complex; γ-TuSC, γ-tubulin small complex; GRIP1/2, γ-tubulin ring protein 1/2; HSP90, heat shock protein 90; INO80, inositol-requiring mutant 80 complex; MZT1/2, mitotic spindle organizing protein 1/2; NEDD1, neural precursor cell expressed, developmentally down-regulated 1; NME7, nucleotide diphosphate kinase 7; PCM, pericentriolar material; PIH1D1, PIH1 domain containing 1; R2TP, Rvb1-Rvb2-Tah1-Pih1; RPAP3, RNA polymerase II associated protein 3; RUVBL1/2, RuvB-like 1/2; SPB, spindle pole body; SWR1, SWI2/SNF2-related 1 complex; XMAP215, Xenopus microtubule assembly protein with 215 kDThis is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

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Section: The Ruvbl1‐ruvbl2 Aaa+ Atpase Assists In γ‐Turc Assemblymentioning

confidence: 99%

The gamma‐tubulin ring complex: Deciphering the molecular organization and assembly mechanism of a major vertebrate microtubule nucleator

et al. 2021

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“…For example, CDC5L, part of the Prp19 complex that participates in pre-mRNA splicing and DNA damage repair (Sihn et al, 2007), and RUVBL2, together with TIP60, regulated transcription via chromatin remodelling by participating in diverse multi-protein complexes (Nishitsuji et al, 2018;Idauden et al, 2020). Studies have shown that there are at least 20 members of the heterogeneous nuclear ribonucleoprotein (HNRNP) family identified in mammals (Han et al, 2010), which perform a variety of functions related to transcription, splicing, RNA stability and degradation (Lu et al, 2006;Gittings et al, 2019).…”

Section: Chbrd2 Is Involved In Gene Expression Regulationmentioning

confidence: 99%

Screening and bioinformatics analysis of cellular proteins interacting with chicken bromodomain-containing protein 2 in DF-1 cells

Zhou

Han

Yuan

et al. 2021

British Poultry Science

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1. Bromodomain-containing protein 2 (BRD2) is an important member of the BET protein family, which can specifically bind histone acetylated lysine to participate in gene transcriptional regulation, chromatin remodelling, cell proliferation and apoptosis. The following investigation of cellular proteins interacting with chBRD2 will be helpful in understanding the new functions of chBRD2 and the mechanism of NDV replication.

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“…RUVBL1/2 function as co-chaperones for HSP90 and are involved in diverse cellular processes as components of several different multiprotein complexes (48,49). In the cytoplasm, RUVBL1/2-containing complexes function in the assembly of several essential multi-molecular complexes such as snRNPs, snoRNPs, the telomerase RNP complex, RNA Pol2, the TRAPP chromatin remodeling complex, and the PIKK family of multi-subunit protein kinases including mTORC1, which regulates ribosome and protein synthesis, and SMG-1 required for nonsense-mediated mRNA decay (NMD).…”

Section: E1a-dcaf10 Targeting Of Ruvbl1/2 Prevents Irf3 Stabilizationmentioning

confidence: 99%

“…These three interactions are mediated The N-terminal ~15 aa residues plus the portion of CR1 diagrammed in green (aa 54-82) are intrinsically disordered protein (IDP) regions that fold and are bound by the p300/CBP TAZ2 domain (14), inhibiting p300/CBP histone acetyl transferase activity (10,15). The N-terminal portion of CR1 (aa [37][38][39][40][41][42][43][44][45][46][47][48][49] and CR2 (aa 121-129, both blue) are bound by the "pocket" domains of RB-family proteins (14,16). Between the N-terminal domain and CR1, aa 26-35 (brown region) mediate an interaction with p400 and TRRAP (17).…”

Section: Introductionmentioning

confidence: 99%

Adenovirus E1A Binding to DCAF10 Targets Degradation of AAA+ ATPases Required for Quaternary Assembly of Multiprotein Machines and Innate Immunity

Zemke

Barshop

Sha

et al. 2020

Preprint

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SUMMARYAdenovirus E1A early proteins modify host cell physiology to optimize virus replication. The N-terminal half of small e1a interacts with RB-family proteins to de-repress dNTP and DNA synthesis, and with p300/CBP to inhibit host anti-viral innate immune responses. These e1a N-terminal interactions activate a strong, late host anti-viral response due to stabilization and activation of interferon response factor 3 (IRF3). However, the C-terminal half of e1a inhibits this through interactions with three host proteins with seemingly unrelated functions. Proteomic analysis showed that all three C-terminal interactions are required for e1a-association into an ∼1 MDa multi-protein complex with scaffold subunits of a CRL4 E3 ubiquitin ligase and DCAF10, a presumed specificity subunit. This e1a-DCAF10-CRL4 prevents IRF3 stabilization indirectly by directing degradation of the essential AAA+ ATPases RUVBL1/2, subunits of several HSP90 co-chaperones required for quaternary assembly of cellular protein machines required for anti-viral defenses and responses to genotoxic and metabolic stress.

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

Cited by 45 publications

References 46 publications

The gamma‐tubulin ring complex: Deciphering the molecular organization and assembly mechanism of a major vertebrate microtubule nucleator

The gamma‐tubulin ring complex: Deciphering the molecular organization and assembly mechanism of a major vertebrate microtubule nucleator

Screening and bioinformatics analysis of cellular proteins interacting with chicken bromodomain-containing protein 2 in DF-1 cells

Adenovirus E1A Binding to DCAF10 Targets Degradation of AAA+ ATPases Required for Quaternary Assembly of Multiprotein Machines and Innate Immunity

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