Affinage

Showing MPHOSPH10 — MPP10 is a alias.

MPHOSPH10

U3 small nucleolar ribonucleoprotein protein MPP10 · UniProt O00566

Length
681 aa
Mass
78.9 kDa
Annotated
2026-06-10
38 papers in source corpus 21 papers cited in narrative 21 extracted findings
Cross-family judge vs UniProt: tie faithfulness: 6/6 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

MPHOSPH10/MPP10 is an essential nucleolar protein that functions as a core component of the U3 snoRNP/SSU processome, where it is required for endonucleolytic cleavage of pre-rRNA at the A0, A1, and A2 sites to generate mature 18S rRNA (PMID:9315638, PMID:9450966). Within the 90S pre-ribosome, Mpp10 forms a discrete structural module with its direct partners Imp3 and Imp4 — interactions identified by two-hybrid screening, confirmed in vivo, and resolved at atomic resolution by crystallography and cryo-EM — that organizes around the 5'-ETS and immature 18S rRNA near the unprocessed A1 cleavage site (PMID:10409734, PMID:27419870, PMID:28967883, PMID:28813493). Mpp10 association with the U3 snoRNP depends on a conserved element in the U3 snoRNA hinge region, placing the module at the functional U3 snoRNA–pre-rRNA base-pairing interface, and its C-terminus is specifically required for A1/A2 (but not A0) cleavage, defining a discrete mechanistic role beyond maintenance of U3 base-pairing (PMID:9391061, PMID:11421365, PMID:12242301, PMID:21890904). Mpp10 acts as a multi-protein interaction platform, additionally binding Utp3/Sas10 and ribosomal protein uS7, and is delivered to the nucleolus through a UTP3/Sas10–importin-α–dependent route required for A0 cleavage (PMID:28813493, PMID:30773582, PMID:39036955). Mpp10 abundance is controlled by the nucleolar Def–CAPN3 (Calpain3) degradation pathway, with Sas10 protecting Mpp10 by masking the CAPN3 recognition site, and Mpp10 is also subject to arginine methylation by Hmt1 (PMID:26572822, PMID:30773582, PMID:34452850, PMID:35878425). In interphase Mpp10 is nucleolar, but it becomes an M-phase phosphoprotein and redistributes onto chromosome surfaces during mitosis (PMID:8885239, PMID:9450966).

Mechanistic history

Synthesis pass · year-by-year structured walk · 15 steps
  1. 1996 Medium

    Established MPHOSPH10 as a nucleolar protein that is cell-cycle regulated, becoming an M-phase phosphoprotein that redistributes during mitosis — the first link between this protein and dynamic nuclear/nucleolar behavior.

    Evidence Immunofluorescence and MPM2-antibody immunoprecipitation from M-phase cell lysates

    PMID:8885239

    Open questions at the time
    • Kinase responsible for M-phase phosphorylation not identified
    • Functional consequence of mitotic redistribution unknown
  2. 1997 High

    Defined the core molecular function: Mpp10 is an essential U3 snoRNP component required for pre-rRNA cleavage at A0, A1, and A2, answering what process the protein serves.

    Evidence U3 snoRNA Co-IP, conditional depletion, Northern blot and pulse-chase analysis of pre-rRNA processing in yeast

    PMID:9315638

    Open questions at the time
    • Did not resolve whether Mpp10 acts catalytically or as a scaffold
    • Partner proteins within the U3 snoRNP not yet defined
  3. 1997 High

    Dissected Mpp10 into separable functional domains by showing the C-terminus is specifically required for A1/A2 but not A0 cleavage, establishing distinct mechanistic steps within the protein.

    Evidence C-terminal truncation mutagenesis with pre-rRNA Northern analysis and Co-IP in yeast

    PMID:9391061

    Open questions at the time
    • Molecular basis of A1/A2-specific requirement not defined
    • C-terminal interaction partners unidentified at this stage
  4. 1998 High

    Extended the U3 snoRNP role to human MPP10, with detailed subnucleolar localization and U3-specific snoRNA association, showing functional conservation.

    Evidence Cell fractionation, immunofluorescence with fibrillarin, salt-stable snoRNA Co-IP, actinomycin D treatment in human cells

    PMID:9450966

    Open questions at the time
    • Human protein interactors beyond U3 snoRNA not defined
    • Mechanism of mitotic chromosome-surface localization unresolved
  5. 1999 High

    Identified the direct binding partners Imp3 and Imp4 as novel U3 snoRNP proteins, revealing Mpp10 operates as part of a defined protein module.

    Evidence Yeast two-hybrid screen, in vivo Co-IP, conditional depletion with Northern analysis

    PMID:10409734

    Open questions at the time
    • Stoichiometry and architecture of the Mpp10-Imp3-Imp4 module not yet known
    • Direct interfaces between the three proteins not mapped
  6. 2001 Medium

    Mapped Mpp10 to the functional center of the U3 snoRNP by showing its association requires the U3 hinge region rather than the 3' domain used by other U3 proteins.

    Evidence U3 snoRNA deletion/truncation mapping by Co-IP

    PMID:11421365

    Open questions at the time
    • Direct RNA-protein contact residues not defined
    • Single-lab RNA mapping
  7. 2002 High

    Showed interdependent stability and U3 association of Mpp10, Imp3, and Imp4, and via epistasis that Mpp10 acts at a step beyond U3 base-pairing maintenance.

    Evidence Double-mutant epistasis, heterologous complementation, stability assays, Co-IP in yeast

    PMID:12242301

    Open questions at the time
    • Identity of the additional A2 mechanistic step not defined
    • Temperature-specific requirement of the terminal 95 residues mechanistically unexplained
  8. 2004 Medium

    Linked Mpp10 association with the 80S processing complex to U3 snoRNA subnucleolar trafficking from the DFC to the GC.

    Evidence U3 snoRNA mutational analysis, immunoprecipitation, subnucleolar fractionation

    PMID:15367679

    Open questions at the time
    • Causality between Mpp10 binding and trafficking not proven
    • Single-lab data
  9. 2004 Medium

    Probed the Mpp10-Imp4 interaction within the intact processome, finding processing-defective Imp4 mutants retain Mpp10 association, implying redundant contacts maintain the module.

    Evidence Reverse two-hybrid, in-complex Co-IP, pre-rRNA Northern analysis

    PMID:14990745

    Open questions at the time
    • Other complex members maintaining the interaction not identified
    • Decoupling of processing defect from interaction loss unexplained
  10. 2009 Medium

    Placed the Mpp10 complex in the SSU processome assembly hierarchy, showing its recruitment depends on active pre-rRNA transcription and prior tUTP assembly in both yeast and human systems.

    Evidence Sucrose gradient sedimentation, IP, tUTP RNAi, transcription inhibition (human); biochemical fractionation and assembly modeling (yeast)

    PMID:17515605 PMID:19332556

    Open questions at the time
    • Direct recruitment signal/receptor for the Mpp10 complex not identified
    • Single-lab assembly models
  11. 2011 Medium

    Refined the RNA contact, showing U3 hinge segment VI (the 11-bp helix with 5'-ETS) is required for Mpp10/Imp3/Imp4 association, positioning the module at the U3-pre-rRNA interface.

    Evidence Compensatory mutation rescue in vivo plus Co-IP with U3 variants

    PMID:21890904

    Open questions at the time
    • Direct protein contacts to helix VI not resolved at residue level
    • Single-lab data
  12. 2017 High

    Resolved the architecture of the Mpp10 module at atomic detail and revealed Mpp10 as a multi-protein hub binding Imp4, Utp3/Sas10, and ribosomal protein uS7 near the A1 cleavage site.

    Evidence Crystal structure of Imp4-Mpp10 helix at 1.88 Å plus binding assays; cryo-EM of the C. thermophilum 90S at 3.2 Å with atomic model building (building on the 2016 90S cryo-EM)

    PMID:27419870 PMID:28813493 PMID:28967883

    Open questions at the time
    • Structures are from thermophilic fungi; human-specific features not modeled
    • Catalytic mechanism of A1/A2 cleavage not assigned to a specific factor
  13. 2019 High

    Identified Sas10/Utp3 as both a protector that masks the CAPN3 cleavage site on Mpp10 and a delivery factor required for nucleolar localization of the Mpp10-Imp3-Imp4 complex, with Def promoting CAPN3-mediated cleavage.

    Evidence Co-IP, zebrafish knockdown, localization and stability assays

    PMID:30773582

    Open questions at the time
    • Quantitative balance between protection and degradation in vivo not defined
    • Signals triggering Def-Sas10-Mpp10 complex formation unknown
  14. 2022 Medium

    Defined the Def-CAPN3 turnover pathway controlling Mpp10 abundance, mapping the CAPN3 and Def interaction motifs that assemble the nucleolar degradation complex acting on Mpp10.

    Evidence Def-depletion with fractionation and rRNA analysis; truncation/deletion mapping of CAPN3-Def interaction by Co-IP

    PMID:34452850 PMID:35878425

    Open questions at the time
    • Physiological cue that activates Mpp10 cleavage not defined
    • Whether turnover is cell-cycle-coupled not directly shown
  15. 2024 Medium

    Defined the nucleolar import route, showing UTP3/SAS10 conveys MPP10 to the nucleolus via importin-α, with loss impairing MPP10 localization and A0 cleavage.

    Evidence Systematic localization screen, siRNA knockdown, importin α interaction assay, rRNA processing analysis in human cells

    PMID:39036955

    Open questions at the time
    • Direct MPP10 nuclear localization signal not mapped
    • Single-lab screen

Open questions

Synthesis pass · forward-looking unresolved questions
  • How M-phase phosphorylation drives MPP10's mitotic redistribution and whether arginine methylation by Hmt1 regulates its processing or trafficking functions remain unresolved.
  • No identified kinase or functional readout for the M-phase phosphosite
  • Functional consequence of Hmt1-mediated arginine methylation not established
  • No direct human disease link characterized in the corpus

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003723 RNA binding 4 GO:0060090 molecular adaptor activity 2
Localization
GO:0005730 nucleolus 4 GO:0005694 chromosome 2
Pathway
R-HSA-8953854 Metabolism of RNA 3
Partners
CAPN3IMP3IMP4U3 SNORNAUS7UTP11UTP3
Complex memberships
Def-Sas10-Mpp10 complexMpp10-Imp3-Imp4 moduleSSU processome / 90S pre-ribosomeU3 snoRNP

Evidence

Reading pass · 21 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1996 MPHOSPH10/MPP10 is a nucleolar protein in interphase cells that becomes an M phase phosphoprotein recognized by the MPM2 antibody (which recognizes F-phosphoT-P-L-Q motifs), indicating it is phosphorylated at M phase-specific sites during mitosis. In mitosis, it redistributes throughout the cell. Immunofluorescence microscopy and immunoprecipitation with MPM2 antibody from M phase cell lysates Molecular biology of the cell Medium 8885239
1997 Yeast Mpp10p is a component of the U3 snoRNP: antibodies to purified Mpp10p immunoprecipitate U3 snoRNA from yeast extracts. MPP10 is an essential gene, and depletion of Mpp10p causes accumulation of 23S and 35S pre-rRNA precursors and loss of 18S rRNA and its 20S precursor, demonstrating Mpp10p is required for pre-rRNA cleavage at sites A0, A1, and A2. Co-immunoprecipitation of U3 snoRNA, conditional promoter depletion, Northern blot analysis of pre-rRNA processing, pulse-chase analysis Molecular and cellular biology High 9315638
1997 C-terminal truncations of Mpp10p separate U3 snoRNP function into two distinct activities: truncated Mpp10p supports cleavage at A0 but not at A1/A2 sites, without affecting Mpp10p-U3 snoRNA association or protein stability, demonstrating the C-terminus is specifically required for A1/A2 processing. Truncation mutagenesis, Northern blot pre-rRNA processing analysis, cold-sensitivity growth assay, co-immunoprecipitation Proceedings of the National Academy of Sciences of the United States of America High 9391061
1998 Human MPP10 localizes almost entirely to nucleoli by cell fractionation; by immunofluorescence it co-localizes with nucleolar fibrillarin in interphase but not in coiled bodies. Upon actinomycin D treatment, MPP10 is enriched in fibrillar caps (sites of rRNA processing). In early-to-middle M phase, MPP10 co-localizes with fibrillarin on chromosome surfaces, and at telophase appears in nucleolus-derived bodies and prenucleolar bodies. Immunoprecipitation from cell sonicates shows MPP10 specifically associates with U3 snoRNA but not other box C/D snoRNAs, stable to 400 mM salt, establishing human MPP10 as a U3 snoRNP component. Cell fractionation, immunofluorescence microscopy, immunoprecipitation of snoRNA, actinomycin D treatment Molecular biology of the cell High 9450966
1999 Imp3p and Imp4p are two novel U3 snoRNP proteins identified by two-hybrid screening for proteins that physically associate with Mpp10p. Both associate with Mpp10p in vivo and are complexed only with U3 snoRNA. Genetic depletion of either Imp3p or Imp4p causes defects in pre-18S rRNA processing at A0, A1, and A2 sites, and neither is required for U3 snoRNA integrity. Yeast two-hybrid screen, co-immunoprecipitation in vivo, conditional depletion with Northern blot analysis Molecular and cellular biology High 10409734
2001 Association of Mpp10p with the U3 snoRNP requires a conserved sequence element in the U3 snoRNA hinge region (nt 40-72), not the 3' domain sufficient for other U3 snoRNP proteins. This places Mpp10p near the 5' domain that carries out pre-rRNA base-pairing interactions, at the functional center of the U3 snoRNP. U3 snoRNA deletion and truncation analysis by co-immunoprecipitation RNA (New York, N.Y.) Medium 11421365
2002 Imp3p, Imp4p, and Mpp10p show interdependence for their stability and their association with U3 snoRNA. C-terminal truncations of Mpp10p combined with U3 snoRNA processing-defective mutations produce a more severe A2 cleavage defect than either alone, indicating Mpp10p acts at an additional mechanistic step beyond U3 snoRNA base-pairing maintenance. The last 95 amino acids of yeast Mpp10p are specifically required for growth and pre-rRNA processing at low temperatures, as shown by failed heterologous complementation without this region. Genetic epistasis (double-mutant analysis), heterologous complementation, protein stability assays, co-immunoprecipitation Molecular and cellular biology High 12242301
2004 Binding of Mpp10 to the 80S U3 snoRNP processing complex requires sequences within the U3 snoRNA that base pair with the pre-rRNA adjacent to the initial cleavage site. Mutations that inhibit 80S complex formation and/or Mpp10 association cause retention of U3 snoRNA in the dense fibrillar component (DFC) rather than movement to the granular component (GC), indicating Mpp10 association is linked to U3 snoRNA subnucleolar trafficking. U3 snoRNA mutational analysis, immunoprecipitation, subnucleolar fractionation Molecular and cellular biology Medium 15367679
2004 Mpp10p-Imp4p protein-protein interaction was tested by reverse two-hybrid screening; mutations in the N-terminal coiled-coil domain of Imp4 confer cold sensitivity, mutations in C-terminus confer temperature sensitivity. Surprisingly, these mutant Imp4 proteins are not measurably defective for Mpp10p interaction within the intact SSU processome, suggesting other complex members maintain this interaction, while still causing pre-rRNA processing defects. Reverse two-hybrid system, co-immunoprecipitation within SSU processome context, pre-rRNA Northern blot analysis Nucleic acids research Medium 14990745
2007 In the 90S preribosome assembly hierarchy, the Mpp10 complex (with Imp3 and Imp4) assembles as a discrete subunit that enters as part of one of two mutually independent assembly routes. This route also involves U3 snoRNP and UTP-B (Pwp2p) subunit binding, which is downstream of the essential t-UTP subunit assembly step. Biochemical fractionation, proteomics, RNA co-immunoprecipitation, bioinformatic assembly modeling Molecular and cellular biology Medium 17515605
2009 Human MPP10 is part of a distinct subcomplex within the SSU processome. A novel 50S U3 snoRNP intermediate accumulates when pre-rRNA transcription is blocked or tUTP proteins are depleted; this intermediate lacks the tUTP, bUTP, MPP10, and BMS1/RCL1 subcomplexes, establishing that MPP10 complex recruitment to the SSU processome is dependent on active pre-rRNA transcription and prior tUTP assembly. Sucrose gradient sedimentation, immunoprecipitation, RNAi depletion of tUTP proteins, transcription inhibition Molecular and cellular biology Medium 19332556
2011 The U3 snoRNA hinge region segment VI (forming an 11-bp helix with 5'-ETS) is essential for pre-rRNA processing and cell growth. Compensatory mutations in helix VI restore growth, and specific sequences within segment VI are required for association of Mpp10, Imp4, and Imp3 proteins, placing these proteins at the U3 snoRNA-pre-rRNA interface. Compensatory mutation analysis in vivo, co-immunoprecipitation of Mpp10/Imp4/Imp3 with U3 snoRNA variants Nucleic acids research Medium 21890904
2016 Cryo-EM structure of the Chaetomium thermophilum 90S pre-ribosome identifies the Mpp10-Imp3-Imp4 module as a discrete structural unit within the particle, organized around the 5'-ETS and partially folded 18S rRNA, with the U3 snoRNP positioned centrally. Cryo-EM structural analysis of 90S pre-ribosome Cell High 27419870
2016 Mpp10 is a substrate of the yeast arginine methyltransferase Hmt1, validated by ex vivo methylation assay and MS/MS analysis, establishing Mpp10 as an arginine-methylated protein. Proteome array with anti-methylarginine antibody, ex vivo methylation assay with recombinant Hmt1, MS/MS validation Proteomics Medium 26572822
2017 High-resolution (3.2 Å) cryo-EM structure of the Chaetomium thermophilum 90S preribosome allows atomic model building of the Mpp10 complex. The structure reveals the Mpp10 complex as part of the intertwined assembly factor network that maintains pre-18S RNA domains in an immature state, and identifies the Mpp10 complex in proximity to the unprocessed A1 cleavage site. Cryo-EM at 3.2 Å resolution with atomic model building Nature structural & molecular biology High 28967883
2017 Crystal structure of Imp4 in complex with a short helical element of Mpp10 resolved at 1.88 Å. Additionally, Mpp10 binds Utp3/Sas10 through two conserved motifs in its N-terminal region, and interacts with ribosomal protein S5/uS7 through a short stretch in an acidic loop region, establishing Mpp10 as a multi-protein interaction platform within the 90S pre-ribosome. X-ray crystallography at 1.88 Å, co-immunoprecipitation, binding assays for novel interactions PloS one High 28813493
2019 Sas10/Utp3 stabilizes Mpp10 from Capn3-mediated cleavage by masking the Capn3-recognition site on Mpp10. Def interacts with Sas10 to form the Def-Sas10-Mpp10 complex, which facilitates Capn3-mediated cleavage of Mpp10. Sas10 is required for nucleolar localization of the Mpp10-Imp3-Imp4 complex, establishing Sas10 as both a chaperone/protector and delivery factor for the Mpp10 complex. In vivo protein interaction assays (Co-IP), genetic depletion/knockdown in zebrafish, subcellular localization analysis, protein stability assays Nucleic acids research High 30773582
2021 Mpp10 is a substrate of the nucleolus-localized Def-CAPN3 protein degradation pathway. CAPN3 (Calpain3), recruited to the nucleolus by Def, proteolytically cleaves Mpp10 via a recognition motif on Mpp10. Def depletion leads to accumulation of Mpp10 in the nucleolus and rRNA processing abnormality, establishing Mpp10 turnover as part of cell-cycle control and ribosome biogenesis regulation. Genetic depletion of Def, subcellular fractionation, protein degradation assays, rRNA processing analysis Journal of genetics and genomics Medium 34452850
2022 An 86-amino acid motif (430-515 aa) in human CAPN3 is essential for its interaction with human Def, and the corresponding region is conserved in zebrafish Capn3b. The 2/3 C-terminus of human Def mediates the Def-CAPN3 interaction. This Def-CAPN3 complex mediates degradation of Mpp10 in the nucleolus. Truncation and internal deletion analysis of CAPN3, co-immunoprecipitation of Def-CAPN3 variants Biochemical and biophysical research communications Medium 35878425
2023 UTP11 binds directly to MPP10 (pre-rRNA processing factor) and is required for 18S rRNA biosynthesis; depletion of UTP11 impedes 18S rRNA production to trigger nucleolar stress. Co-immunoprecipitation/binding assay between UTP11 and MPP10, rRNA processing analysis upon UTP11 depletion Redox biology Low 37087976
2024 UTP3/SAS10 assists the nucleolar localization of MPP10 (along with UTP25, EMG1, UTP12, and UTP13) through its interaction with nuclear importin α. Knockdown of human UTP3 impairs MPP10 nucleolar localization and cleavage at the pre-rRNA A0-site, establishing a UTP3-dependent nucleolar translocation pathway for MPP10. Systematic localization screen of 50 SSU processome components by fluorescence microscopy, siRNA knockdown, importin α interaction assay, rRNA processing analysis Nucleic acids research Medium 39036955

Source papers

Stage 0 corpus · 38 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2016 Architecture of the 90S Pre-ribosome: A Structural View on the Birth of the Eukaryotic Ribosome. Cell 181 27419870
1996 Identification of novel M phase phosphoproteins by expression cloning. Molecular biology of the cell 170 8885239
2007 The 90S preribosome is a multimodular structure that is assembled through a hierarchical mechanism. Molecular and cellular biology 144 17515605
2004 The small-subunit processome is a ribosome assembly intermediate. Eukaryotic cell 142 15590835
1999 Imp3p and Imp4p, two specific components of the U3 small nucleolar ribonucleoprotein that are essential for pre-18S rRNA processing. Molecular and cellular biology 122 10409734
1997 Mpp10p, a U3 small nucleolar ribonucleoprotein component required for pre-18S rRNA processing in yeast. Molecular and cellular biology 105 9315638
2017 3.2-Å-resolution structure of the 90S preribosome before A1 pre-rRNA cleavage. Nature structural & molecular biology 90 28967883
2009 A novel small-subunit processome assembly intermediate that contains the U3 snoRNP, nucleolin, RRP5, and DBP4. Molecular and cellular biology 59 19332556
2011 A second base pair interaction between U3 small nucleolar RNA and the 5'-ETS region is required for early cleavage of the yeast pre-ribosomal RNA. Nucleic acids research 54 21890904
2002 Components of an interdependent unit within the SSU processome regulate and mediate its activity. Molecular and cellular biology 53 12242301
1998 M phase phosphoprotein 10 is a human U3 small nucleolar ribonucleoprotein component. Molecular biology of the cell 50 9450966
2010 The DEAD-box RNA helicase-like Utp25 is an SSU processome component. RNA (New York, N.Y.) 44 20884785
1997 Functional separation of pre-rRNA processing steps revealed by truncation of the U3 small nucleolar ribonucleoprotein component, Mpp10. Proceedings of the National Academy of Sciences of the United States of America 43 9391061
2017 Genetics of early-onset Parkinson's disease in Finland: exome sequencing and genome-wide association study. Neurobiology of aging 41 28256260
2004 Role of pre-rRNA base pairing and 80S complex formation in subnucleolar localization of the U3 snoRNP. Molecular and cellular biology 38 15367679
2003 Human scleroderma sera contain autoantibodies to protein components specific to the U3 small nucleolar RNP complex. Arthritis and rheumatism 37 12528121
2004 Imp3p and Imp4p mediate formation of essential U3-precursor rRNA (pre-rRNA) duplexes, possibly to recruit the small subunit processome to the pre-rRNA. Proceedings of the National Academy of Sciences of the United States of America 35 15489263
2019 Sas10 controls ribosome biogenesis by stabilizing Mpp10 and delivering the Mpp10-Imp3-Imp4 complex to nucleolus. Nucleic acids research 28 30773582
2010 Utp25p, a nucleolar Saccharomyces cerevisiae protein, interacts with U3 snoRNP subunits and affects processing of the 35S pre-rRNA. The FEBS journal 26 20528918
2013 Nucleolar proteins Bfr2 and Enp2 interact with DEAD-box RNA helicase Dbp4 in two different complexes. Nucleic acids research 23 24357410
2023 UTP11 deficiency suppresses cancer development via nucleolar stress and ferroptosis. Redox biology 21 37087976
2001 An unexpected, conserved element of the U3 snoRNA is required for Mpp10p association. RNA (New York, N.Y.) 21 11421365
2014 DEAD-box RNA helicase Dbp4 is required for small-subunit processome formation and function. Molecular and cellular biology 19 25535329
2008 Mrd1p binds to pre-rRNA early during transcription independent of U3 snoRNA and is required for compaction of the pre-rRNA into small subunit processomes. Nucleic acids research 19 18586827
2004 Two-hybrid Mpp10p interaction-defective Imp4 proteins are not interaction defective in vivo but do confer specific pre-rRNA processing defects in Saccharomyces cerevisiae. Nucleic acids research 17 14990745
2017 Mpp10 represents a platform for the interaction of multiple factors within the 90S pre-ribosome. PloS one 15 28813493
2010 Adjacent gene pairing plays a role in the coordinated expression of ribosome biogenesis genes MPP10 and YJR003C in Saccharomyces cerevisiae. Eukaryotic cell 14 21115740
2014 Dissecting the cis and trans elements that regulate adjacent-gene coregulation in Saccharomyces cerevisiae. Eukaryotic cell 13 24706020
2021 Nucleolus-localized Def-CAPN3 protein degradation pathway and its role in cell cycle control and ribosome biogenesis. Journal of genetics and genomics = Yi chuan xue bao 9 34452850
2016 Protein substrates of the arginine methyltransferase Hmt1 identified by proteome arrays. Proteomics 9 26572822
2014 Purification, crystallization and preliminary X-ray diffraction analysis of Imp3 in complex with an Mpp10 peptide involved in yeast ribosome biogenesis. Acta crystallographica. Section F, Structural biology communications 9 25005089
1997 Mpp10p, a new protein component of the U3 snoRNP required for processing of 18S rRNA precursors. Nucleic acids symposium series 9 9478208
2019 Proteins and RNA sequences required for the transition of the t-Utp complex into the SSU processome. FEMS yeast research 8 30445532
2007 Panax ginseng increases hypoxia-induced down-regulated cellular response related genes in human neuroblastoma cells, SK-N-MC. Neurological research 7 17359646
2024 A transcriptome-wide association study identified susceptibility genes for hepatocellular carcinoma in East Asia. Gastroenterology report 4 38846986
2020 Anti-infective nitazoxanide disrupts transcription of ribosome biogenesis-related genes in yeast. Genes & genomics 4 32524281
2024 A UTP3-dependent nucleolar translocation pathway facilitates pre-rRNA 5'ETS processing. Nucleic acids research 3 39036955
2022 An 86 amino acids motif in CAPN3 is essential for formation of the nucleolus-localized Def-CAPN3 complex. Biochemical and biophysical research communications 2 35878425

Missed literature

Know a paper Affinage missed for MPHOSPH10? Flag it for the maintainers and the community.

No submissions yet.