| 1996 |
RRP5 (yeast ortholog of PDCD11) is essential for pre-rRNA processing at sites A0, A1, and A2 (required for 18S rRNA synthesis) and at site A3 (required for the major short form of 5.8S rRNA synthesis), making it the first cellular component simultaneously required for both snoRNP-dependent and RNase MRP-dependent cleavage events in ribosome biogenesis. |
Genetic depletion of Rrp5p in S. cerevisiae followed by pre-rRNA processing analysis; synthetic lethality screen with snR10 deletion |
The EMBO journal |
High |
8896463
|
| 2008 |
Human NFBP (PDCD11) colocalizes with and co-precipitates U3 snoRNA in the nucleolus, and is essential for 18S rRNA maturation via cleavages at sites A0, 1, and 2, as demonstrated by accumulation of unprocessed rRNA intermediates upon NFBP knockdown. |
Co-immunoprecipitation, immunofluorescence colocalization, Northern blot analysis of pre-rRNA processing upon NFBP depletion |
Journal of cellular physiology |
High |
17654514
|
| 2009 |
Human RRP5 (PDCD11) associates with the U3 snoRNP as part of a 50S SSU processome assembly intermediate, together with nucleolin and DBP4, and is likely recruited to pre-rRNA through RNA-binding activity to form this intermediate before tUTP, bUTP, MPP10 and BMS1/RCL1 subcomplexes join. |
Sucrose gradient sedimentation, co-immunoprecipitation, depletion of tUTP proteins to accumulate intermediate complex |
Molecular and cellular biology |
Medium |
19332556
|
| 2011 |
Yeast Rrp5 binds pre-rRNA at three distinct regions within ITS1 using its 12 tandem S1 RNA-binding domains; the first nine S1 motifs contribute high-affinity but non-specific RNA binding, while the last three S1 domains provide specificity for pre-rRNA. Two truncated forms (Rrp5N and Rrp5C) together fully restore growth in vivo. |
In vitro RNA binding assays, DMS probing of RNA-protein interactions, quantitative affinity measurements with truncated protein fragments, complementation assays in yeast |
RNA (New York, N.Y.) |
High |
21233221
|
| 2013 |
Rrp5 binds pre-rRNA at multiple sites in vivo: the C-terminal domain (CTD) crosslinks to sequences flanking cleavage site A2 and to snoRNAs U3, U14, snR30, and snR10 (required for A0-A2 cleavage), while the N-terminal domain (NTD) crosslinks to sequences flanking site A3 and to the RNA component of RNase MRP. Rrp5 depletion abolishes cotranscriptional cleavage and greatly reduces preribosome compaction. |
In vivo UV crosslinking and site identification, intramolecular complementation analysis, chromatin spreads (electron microscopy) |
Molecular cell |
High |
24239293
|
| 2016 |
The DEAD-box protein Rok1, when ATP-bound, stabilizes Rrp5 binding to pre-40S ribosomes; ATP hydrolysis by Rok1 is required for release of Rrp5 from pre-40S ribosomes in vivo, allowing Rrp5 to subsequently participate in 60S subunit assembly. Rrp5 also interacts with the DEAD-box protein Has1, and blocking Rrp5 release from pre-40S subunits causes accumulation of snR30. |
In vivo and in vitro biochemical analyses; ATP vs ADP-bound Rok1 binding assays; co-immunoprecipitation; genetic experiments with inactivation mutants |
PLoS biology |
High |
27280440
|
| 2018 |
The crystal structure of the Rrp5 TPR (TetratricoPeptide Repeat) module was solved (PDB: 5NLG). In vitro assays demonstrated that the TPR region alone does not bind RNA, whereas the three S1 domains preceding the TPR module can associate with homopolymeric RNA. Association of Rrp5 constructs with several proposed interactors was tested in support of cryo-EM-based models. |
X-ray crystallography, in vitro RNA binding assays with domain deletion constructs, protein interaction assays |
FEBS open bio |
High |
30338212
|
| 2019 |
Rrp5 functions as a checkpoint coupling 40S and 60S ribosome assembly: early in transcription, Rrp5 blocks access of Rcl1 to the nascent rRNA, inhibiting pre-40S rRNA cleavage and separation of the two subunit precursors. Upon transcription of domain I of 25S rRNA, the 60S assembly factors Noc1/Noc2 bind both this RNA and Rrp5, altering Rrp5's RNA-binding mode to allow Rcl1-mediated pre-40S rRNA processing. Noc1 HEAT-repeat domain mutants deficient in subunit separation are rescued by overexpression of wild-type but not catalytically inactive Rcl1. |
Quantitative RNA binding assays, pre-rRNA cleavage assays, genetic epistasis (Noc1 mutants rescued by Rcl1 overexpression), in vivo co-immunoprecipitation |
RNA (New York, N.Y.) |
High |
31217256
|
| 2002 |
High-dosage snR10 suppresses defects of a bipartite rrp5 allele in yeast; suppression does not restore cleavage at A2 but improves overall pre-rRNA processing rate and increases active ribosome levels, indicating a functional connection between snR10 and Rrp5 in ribosome biogenesis. |
Multicopy suppressor screen, phenotypic analysis (growth, temperature sensitivity), Northern blot analysis of pre-rRNA processing, polysome profiling |
Molecular genetics and genomics |
Medium |
12242501
|
| 2005 |
Human NFBP (PDCD11) physically interacts with HIV-1 Tat protein via Tat residues 37–48, and this interaction is modulated by RNA molecules. NFBP colocalizes with Tat in the nucleus and nucleoli. Functionally, NFBP augments TAR-dependent LTR activation by Tat in the absence of κB-binding sites, but interferes with the synergistic activation of LTR transcription by P65 and Tat together. |
Co-immunoprecipitation, immunofluorescence colocalization, domain mapping with deletion mutants, LTR reporter transcription assays |
Journal of cellular physiology |
Medium |
15887232
|
| 2020 |
In zebrafish, PDCD11 is required for microglia differentiation; pdcd11 deficiency prevents maturation of precursors to brain microglia while augmenting inflammatory macrophage brain colonization. Mechanistically, PDCD11 differentially regulates NF-κB family members: suppressing P65-mediated expression of inflammatory cytokines (e.g., tnfα) and enhancing c-Rel-dependent expression of tgfβ1. |
Zebrafish genetic loss-of-function (pdcd11 deficiency), immunofluorescence, transcriptional pathway analysis, cytokine expression assays |
Cell death and differentiation |
Medium |
32709934
|
| 2022 |
In Drosophila, Rrp5 (PDCD11 ortholog) localizes to the nucleolus and is required for pre-rRNA processing; depletion of Rok1 causes Rrp5 to become enriched in the core of the nucleolus, indicating that Rok1 is required for accurate subcellular localization of Rrp5 within the nucleolus and for its role in ITS1 and ITS2 rRNA processing. |
Genetics (rok1 mutant analysis), fluorescence in situ hybridization (FISH) for ITS1/ITS2 signals, immunofluorescence localization of Rrp5 in nucleolus |
International journal of molecular sciences |
Medium |
35628496
|
| 2025 |
In p53-mutant breast and colon cancer cells, extra-nucleolar PDCD11 binds the transactivation domain (TAD) of C-MYC in the nucleoplasm, preventing SKP2 (an E3 ligase component and transcriptional target of C-MYC) from interacting with and ubiquitinating C-MYC, thereby stabilizing C-MYC and activating downstream signaling for G1/S transition, proliferation, and migration. PDCD11 silencing restores SKP2-mediated C-MYC degradation and suppresses tumor growth and metastasis in vivo. |
Co-immunoprecipitation, domain mapping of C-MYC TAD interaction, ubiquitination assays, PDCD11 knockdown with C-MYC stability and SKP2 interaction readouts, xenograft mouse tumor models |
Advanced science |
Medium |
40051297
|
| 2025 |
PDCD11 was identified as a carrier of HBV RNA/DNA into extracellular vesicles in HBV-infected HCC cells; depletion of PDCD11 reduced accumulation of HBV RNAs (pre-genomic RNA, HBx, HBc, HBs mRNAs) and intact virions in EVs. MRPL2 was found to interact with PDCD11 in the nucleus, where MRPL2 nuclear localization enhances intracellular calcium signaling through this interaction. |
ASO-mediated depletion of PDCD11, qRT-PCR for HBV RNAs in EVs, proteome profiling by LC-MS/MS, protein-protein interaction network analysis, nuclear localization assays |
Frontiers in cell and developmental biology |
Low |
41425093
|