The R2TP complex: Discovery and functions
نویسندگان
چکیده
منابع مشابه
Substrate recognition and function of the R2TP complex in response to cellular stress
The R2TP complex is a HSP90 co-chaperone, which consists of four subunits: PIH1D1, RPAP3, RUVBL1, and RUVBL2. It is involved in the assembly of large protein or protein-RNA complexes such as RNA polymerase, small nucleolar ribonucleoproteins (snoRNPs), phosphatidylinositol 3 kinase-related kinases (PIKKs), and their complexes. While RPAP3 has a HSP90 binding domain and the RUVBLs comprise ATPas...
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HSP90 and its R2TP co-chaperone play central roles in building machineries important for RNA and DNA metabolism (see (1) for a review). These include the nuclear RNA polymerases, complexes containing PIKKs (mTOR, ATM/ATR, DNA-PK, SMG1, and TRRAP), as well as a number of ribonucleoprotein particles, such as the telomerase RNP, the spliceosomal U4 snRNA and the snoRNPs, which are essential to pro...
متن کاملAnalysis of URI Nuclear Interaction with RPB5 and Components of the R2TP/Prefoldin-Like Complex
Unconventional prefoldin RPB5 Interactor (URI) was identified as a transcriptional repressor that binds RNA polymerase II (pol II) through interaction with the RPB5/POLR2E subunit. Despite the fact that many other proteins involved in transcription regulation have been shown to interact with URI, its nuclear function still remains elusive. Previous mass spectrometry analyses reported that URI i...
متن کاملThe role of Hsp90-R2TP complex in snoRNP assembly and ribosomal RNA processing
In a global screen for interactors of the Hsp90 molecular chaperone, we identified a novel complex that we termed the R2TP complex interacting with the chaperone. The complex consists of four proteins: Rvb1, Rvb2, Tah1, and Pih1. Rvb1 and Rvb2 are AAA+ helicases, while Tah1 and Pih1 are novel Hsp90 cofactors/interactors. We subsequently demonstrated that the Hsp90-R2TP complex is involved in bo...
متن کاملPhosphorylation-Dependent PIH1D1 Interactions Define Substrate Specificity of the R2TP Cochaperone Complex
The R2TP cochaperone complex plays a critical role in the assembly of multisubunit machines, including small nucleolar ribonucleoproteins (snoRNPs), RNA polymerase II, and the mTORC1 and SMG1 kinase complexes, but the molecular basis of substrate recognition remains unclear. Here, we describe a phosphopeptide binding domain (PIH-N) in the PIH1D1 subunit of the R2TP complex that preferentially b...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
سال: 2012
ISSN: 0167-4889
DOI: 10.1016/j.bbamcr.2011.08.016