Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation

Zhao, Rongmin; Kakihara, Yoshito; Gribun, Anna; Huen, Jennifer; Yang, Glen; Khanna, May; Costanzo, Michael; Brost, Renée L.; Boone, Charles; Hughes, Timothy R.; Yip, Christopher M.; Houry, Walid

doi:10.1083/jcb.200709061

Cited by 166 publications

(274 citation statements)

References 53 publications

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“…Thus, the IP-and biotin-GA-mediated purification of structural proteins, including tubulin and kinesin, provides further evidence for the involvement of Hsp90 in the assembly of the tubulin-based cytoskeleton network, cytokinesis, and cellular transport (McClellan et al 2007;Te et al 2007). Isolation of RNA-binding proteins and ribosomal subunits points to the suggested role of Hsp90 in ribosomal subunit nuclear export and RNA processing and maintenance (Schlatter et al 2002;Zhao et al 2008). Similar to Falsone et al, we identified several metabolic enzymes (Falsone et al 2005).…”

Section: Discussionmentioning

confidence: 99%

“…Comprising about 1% of all cellular proteins, Hsp90 is involved in diverse processes ranging from processing and maintenance of RNA to protein sorting and assembly of the tubulin-based cytoskeleton network (Te et al 2007;Lotz et al 2008;Zhao et al 2008). However, one of the most exciting roles of Hsp90 is the stabilization of a set of client proteins.…”

Section: Introductionmentioning

confidence: 99%

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Novel Hsp90 partners discovered using complementary proteomic approaches

Tsaytler

Krijgsveld

Goerdayal

et al. 2009

Cell Stress and Chaperones

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Hsp90 is an essential eukaryotic molecular chaperone that stabilizes a large set of client proteins, many of which are involved in various cellular signaling pathways. The current list of Hsp90 interactors comprises about 200 proteins and this number is growing steadily. In this paper, we report on the application of three complementary proteomic approaches directed towards identification of novel proteins that interact with Hsp90. These methods are coimmunoprecipitation, pull down with biotinylated geldanamycin, and immobilization of Hsp90β on sepharose. In all, this study led to the identification of 42 proteins, including 18 proteins that had not been previously characterized as Hsp90 interactors. These novel Hsp90 partners not only represent abundant protein species, but several proteins were identified at low levels, among which signaling kinase Cdk3 and putative transcription factor tripartite motif-containing protein 29. Identification of tetratricopeptide-repeat-containing mitochondrial import receptor protein Tom34 suggests the involvement of Hsp90 in the early steps of translocation of mitochondrial preproteins. Taken together, our data expand the knowledge of the Hsp90 interactome and provide a further step in our understanding of the Hsp90 chaperone system.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Novel Hsp90 partners discovered using complementary proteomic approaches

Tsaytler

Krijgsveld

Goerdayal

et al. 2009

Cell Stress and Chaperones

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“…Deletion of the Nop17 gene led to dissociation from the nucleolus of all 4 box C/D snoRNP, Nop1, Nop56, Nop58, and snu13 and accumulation of pre-rRNA 35 S . Notably, Pih1/Nop17 is also an unstable protein with a propensity to aggregate in the absence of Tah1 and Hsp90 (Zhao et al 2008).…”

Section: Pih1d1 (Pih1/nop17)mentioning

confidence: 99%

“…Although the exact function of these factors remains elusive, one of these RPAPs, RPAP3, is part of an 11-subunit protein complex that we termed the RPAP3/R2TP/prefoldinlike complex (Fig. 1) based on similarity to the previously characterized R2TP complex, a cofactor of Hsp90 (Zhao et al 2008), and prefoldin complexes (chaperone associated with the CCT/TRiC complex) (Geissler et al 1998;Vainberg et al 1998). Similar complexes have been described in two independent reports.…”

Section: Introductionmentioning

confidence: 99%

New insights into the biogenesis of nuclear RNA polymerases?This paper is one of a selection of papers published in this special issue entitled “Canadian Society of Biochemistry, Molecular & Cellular Biology 52nd Annual Meeting — Protein Folding: Principles and Diseases” and has undergone the Journal's usual peer review process.

Cloutier

Coulombe

2010

Biochem. Cell Biol.

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More than 30 years of research on nuclear RNA polymerases (RNAP I, II, and III) has uncovered numerous factors that regulate the activity of these enzymes during the transcription reaction. However, very little is known about the machinery that regulates the fate of RNAPs before or after transcription. In particular, the mechanisms of biogenesis of the 3 nuclear RNAPs, which comprise both common and specific subunits, remains mostly uncharacterized and the proteins involved are yet to be discovered. Using protein affinity purification coupled to mass spectrometry (AP-MS), we recently unraveled a high-density interaction network formed by nuclear RNAP subunits from the soluble fraction of human cell extracts. Validation of the dataset using a machine learning approach trained to minimize the rate of false positives and false negatives yielded a highconfidence dataset and uncovered novel interactors that regulate the RNAP II transcription machinery, including a set of proteins we named the RNAP II-associated proteins (RPAPs). One of the RPAPs, RPAP3, is part of an 11-subunit complex we termed the RPAP3/R2TP/prefoldin-like complex. Here, we review the literature on the subunits of this complex, which points to a role in nuclear RNAP biogenesis.

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“…Pih1 (Protein interacting with Hsp90), which belongs to Pih1 family of proteins, directly interacts with Rvb1-Rvb2 complex (Rvbs) and Tah1 (TPR [tetratricopeptide repeat-containing protein] associated with Hsp90) (1,3,6). In yeast, Pih1 is an unstable protein and prone to aggregate in vitro, however, the Pih1 aggregates are dissociated by Hsp90 in an ATP-dependent manner, and its disaggregation activity of Hsp90 is enhanced by Tah1 (6). Tah1 is suggested to function as a co-chaperone of Hsp90 in disaggregating Pih1 (6).…”

Section: Introductionmentioning

confidence: 99%

The R2TP chaperone complex: its involvement in snoRNP assembly and tumorigenesis

Kakihara

Saeki

2014

Biomolecular Concepts

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R2TP was originally identified in yeast Saccharomyces cerevisiae as Hsp90 interacting complex, and is composed of four different proteins: Rvb1, Rvb2, Tah1, and Pih1. This complex is well-conserved in eukaryotes, and is involved in many cellular processes such as snoRNP biogenesis, RNA polymerase assembly, PIKK signaling, and apoptosis. An increasing number of research related to R2TP suggests a linkage of its function with tumorigenesis. In this review, we provide an overview of several recent studies on R2TP that are related to cell proliferation and carcinogenesis, and propose a possible role of R2TP in tumorigenesis through regulating snoRNA/snoRNP biogenesis.

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Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation

Cited by 166 publications

References 53 publications

Novel Hsp90 partners discovered using complementary proteomic approaches

Novel Hsp90 partners discovered using complementary proteomic approaches

The R2TP chaperone complex: its involvement in snoRNP assembly and tumorigenesis

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