Affinage

LSM11

U7 snRNA-associated Sm-like protein LSm11 · UniProt P83369

Length
360 aa
Mass
39.5 kDa
Annotated
2026-06-10
39 papers in source corpus 23 papers cited in narrative 23 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

LSM11 is a U7 snRNP-specific Sm-like protein that constitutes the catalytic engine for endonucleolytic 3'-end cleavage of replication-dependent histone pre-mRNAs (PMID:12975319, PMID:19854135). It replaces SmD2 in the heptameric Sm ring, assembling with Lsm10 onto the noncanonical Sm-binding site of U7 snRNA via a specialized SMN complex; its C-terminal Sm motifs (split by a long spacer) drive ring assembly while its extended N-terminal domain carries the processing function (PMID:12975319). This N-terminal domain docks FLASH, forming a 2:1 FLASH:Lsm11 heterotrimer whose paired N-terminal regions build a platform that recruits the cleavage/polyadenylation machinery—symplekin, CstF64, and the CPSF subunits including the CPSF73 endonuclease—to the U7 snRNP (PMID:23071092, PMID:29020104). A conserved N-terminal helix of Lsm11 directly contacts the metallo-β-lactamase domain of CPSF73 and is required for efficient cleavage, and CPSF73 exonuclease activity on the downstream product depends on Lsm11 (PMID:21245389, PMID:41495886). Assembly and activity of this machinery are governed by additional layers: PRMT5 methylates two arginines in the Lsm11 N-terminus and tethers the Lsm10/Lsm11 heterodimer to the methylosome (PMID:37562960), a SUMO-interacting motif promotes efficient U7 snRNP formation (PMID:40639911), and the particle is recruited to histone pre-mRNA cooperatively with SLBP, FLASH, and ALYREF (PMID:28289156, PMID:30858280). Biallelic LSM11 mutations cause Aicardi-Goutières syndrome by misprocessing histone transcripts, disturbing linker histone stoichiometry, and activating cGAS-STING type I interferon signaling (PMID:33230297).

Mechanistic history

Synthesis pass · year-by-year structured walk · 12 steps
  1. 2003 High

    Established that LSM11 is a U7 snRNP-specific Sm-like protein with a functional division of labor between its domains, answering what distinguishes the histone-processing snRNP from spliceosomal snRNPs.

    Evidence In vitro assembly, IP, GST pulldown, and processing assays with domain truncations; cross-species Co-IP in Drosophila S2 cells

    PMID:12975319 PMID:14624008

    Open questions at the time
    • Mechanism of how the N-terminal domain drives cleavage not defined at this stage
    • Direct cleavage factors recruited by Lsm11 not yet identified
  2. 2005 Medium

    Mapped Lsm11 N-terminal interactions with ZFP100 and the PRMT5/pICln complex, beginning to define how the U7 snRNP recognizes processing partners and is routed through assembly.

    Evidence GST pulldown, scanning mutagenesis, in vitro processing, and Co-IP/methylation assays

    PMID:15824063 PMID:16087681 PMID:16714279

    Open questions at the time
    • ZFP100 interaction later superseded as the key processing tether by FLASH
    • Functional consequence of PRMT5 association on Lsm11 not resolved here
    • Additional N-terminal contacts inferred but partners unidentified
  3. 2007 Medium

    Localized Lsm11 to the histone locus body, linking the protein to the nuclear compartment where histone gene expression is organized.

    Evidence Immunofluorescence and confocal microscopy in Drosophila embryos with histone locus genetic ablation

    PMID:17442888

    Open questions at the time
    • What nucleates HLB assembly independent of the histone locus unknown
    • Role of Lsm11 in HLB formation vs. recruitment not separated
  4. 2009 High

    Identified FLASH as the essential Lsm11-binding factor for processing and showed Lsm11 is required in vivo for U7 snRNP function and viability beyond histone processing.

    Evidence Y2H, GST pulldown, reciprocal Co-IP, in vitro processing, RNAi, and Drosophila null mutant genetics with molecular phenotyping

    PMID:19470752 PMID:19620235 PMID:19854135

    Open questions at the time
    • How FLASH-Lsm11 enables cleavage not yet mechanistic
    • Identity of the essential non-processing Lsm10/Lsm11 function undefined
  5. 2011 High

    Defined the FLASH-Lsm11 interaction at residue resolution and proved by genetic rescue that this protein-protein contact is essential for processing in vivo, while showing Lsm11 (not FLASH) activates the CPSF73 exonuclease mode.

    Evidence Drosophila null-rescue with point mutations, Y2H, Co-IP, scanning mutagenesis, and in vitro processing assays

    PMID:21245389 PMID:21525146

    Open questions at the time
    • The additional processing factor recruited by FLASH/Lsm11 not identified at this point
    • Structural basis of the interaction unresolved
  6. 2012 High

    Revealed that the FLASH and Lsm11 N-termini form a platform recruiting the full polyadenylation machinery including CPSF73, unifying histone-specific and canonical 3'-end processing components.

    Evidence Reciprocal Co-IP, in vitro binding with point mutants, mass spectrometry, and histone pre-mRNA pulldown; independently replicated in Drosophila

    PMID:23071092 PMID:24145821

    Open questions at the time
    • Stoichiometry and architecture of the platform not yet structural
    • How the docked endonuclease is positioned at the cleavage site unknown
  7. 2017 High

    Determined the stoichiometry and architecture of the FLASH-Lsm11 platform and assigned FLASH a second role in U7 recruitment, refining the order of complex assembly.

    Evidence X-ray crystallography, MALS, analytical ultracentrifugation, crosslinking, EMSA, and in vitro processing with SLBP/FLASH truncations

    PMID:28289156 PMID:29020104

    Open questions at the time
    • Full Lsm11-containing U7 snRNP structure not yet solved
    • How the 2:1 platform engages the CPSF endonuclease structurally undefined
  8. 2019 Medium

    Added ALYREF as an Lsm11-interacting factor coupling U7 snRNP recruitment to downstream histone mRNA export.

    Evidence Co-IP, RNA-IP, and siRNA knockdown with processing and export assays

    PMID:30858280

    Open questions at the time
    • Whether ALYREF acts on the same Lsm11 surface as FLASH unclear
    • Single-lab Co-IP without structural mapping
  9. 2020 High

    Connected LSM11 loss-of-function to human disease, showing histone misprocessing activates cGAS-STING interferon signaling in Aicardi-Goutières syndrome.

    Evidence Patient fibroblast studies, RT-PCR, cGAS immunofluorescence, in vitro cGAMP synthesis with reconstituted chromatin, and interferon assays

    PMID:33230297

    Open questions at the time
    • How specific patient mutations impair the molecular steps not dissected
    • Tissue-specific consequences of disturbed linker histone stoichiometry unclear
  10. 2022 High

    Demonstrated in vivo that SMN-dependent Lsm10/Lsm11-mediated U7 snRNP assembly is required for neuromuscular junction integrity, extending Lsm11 function to SMA pathology.

    Evidence Mouse SMA model with AAV Lsm10/Lsm11 co-expression, RT-PCR, NMJ electrophysiology, immunofluorescence, and Agrin Western blot

    PMID:36130491

    Open questions at the time
    • Mechanistic link from histone processing to Agrin loss not fully resolved
    • Why specific muscles are selectively vulnerable unknown
  11. 2023 Medium

    Resolved the structural and regulatory inputs to Lsm11: PRMT5 methylation of N-terminal arginines and a SUMO-interacting motif both govern U7 snRNP assembly.

    Evidence Cryo-EM of the Lsm10/Lsm11-methylosome, in vitro methylation, Co-IP; SUMO2 KO cells with SIM mutagenesis and rescue

    PMID:37562960 PMID:40639911

    Open questions at the time
    • Functional consequence of Lsm11 arginine methylation on processing not fully defined
    • How SUMO interaction integrates with methylosome assembly unclear
  12. 2026 High

    Provided the structural mechanism by which Lsm11 activates cleavage, showing a conserved N-terminal helix contacts the CPSF73 endonuclease domain and is required for catalysis.

    Evidence Cryo-EM of reconstituted U7 snRNP on noncleavable pre-mRNA, helix mutagenesis, and in vitro cleavage assays

    PMID:41495886

    Open questions at the time
    • How CPSF73 conformational activation is triggered in the productive cycle not fully resolved
    • Coordination of cleavage-site selection with the molecular ruler not structurally integrated

Open questions

Synthesis pass · forward-looking unresolved questions
  • How the multiple regulatory inputs to Lsm11 (PRMT5 methylation, SUMOylation, NPAT competition for FLASH) are integrated to control histone gene output across the cell cycle remains open.
  • No unified model coupling Lsm11 modifications to cleavage timing
  • Physiological role of Lsm11-NPAT competition for FLASH untested in vivo

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003723 RNA binding 3 GO:0060090 molecular adaptor activity 3 GO:0005198 structural molecule activity 2 GO:0140098 catalytic activity, acting on RNA 2
Localization
GO:0005634 nucleus 2 GO:0005654 nucleoplasm 2
Pathway
R-HSA-8953854 Metabolism of RNA 3 R-HSA-1643685 Disease 2 R-HSA-74160 Gene expression (Transcription) 2
Partners
ALYREFCPSF73FLASHLSM10PRMT5SLBPSMNZFP100
Complex memberships
FLASH-Lsm11 platformPRMT5/MEP50/pICln methylosomeU7 snRNPhistone cleavage complex (CPSF/CstF/symplekin)

Evidence

Reading pass · 23 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2003 Lsm11 is a novel Sm-like protein that replaces SmD2 in the U7 snRNP Sm ring. Its long N-terminal domain mediates an important step in histone mRNA 3'-end cleavage, while its C-terminal Sm motifs (interrupted by an unusually long spacer) are sufficient for assembly with U7 snRNA. Assembly of the U7-specific Sm core depends on the noncanonical Sm-binding site of U7 snRNA and is facilitated by a specialized SMN complex containing Lsm10 and Lsm11 but lacking SmD1/D2. In vitro assembly assays, immunoprecipitation, GST pulldown, in vitro processing assays, domain deletion/truncation analysis Genes & development High 12975319
2003 Drosophila Lsm11 (dLsm11) associates with dLsm10, SmB (but not SmD1/D2), and the Drosophila U7 snRNA, and indirectly with histone H3 pre-mRNA; dLsm10 and dLsm11 can assemble into U7 snRNPs in mammalian cells, demonstrating evolutionary conservation of the unique U7 snRNP composition. Immunoprecipitation in Drosophila S2 cells, cross-species complementation assay RNA (New York, N.Y.) Medium 14624008
2005 Lsm11 undergoes two distinct interactions with ZFP100: one between the Lsm11 N-terminus and the zinc finger repeats of ZFP100, and a second between the N-terminus of ZFP100 and the Sm domain of Lsm11. The second interaction is sufficient for specific recognition of U7 snRNP by ZFP100 in cell extracts. Clustered point mutations in three conserved regions of the Lsm11 N-terminus impair histone RNA processing independently of ZFP100 binding, indicating additional roles (e.g., contacting the pre-mRNA or other factors). GST pulldown (in vitro and in cell extracts), scanning mutagenesis, in vitro processing assays Nucleic acids research Medium 15824063
2005 Lsm10 and Lsm11 associate with the pICln subunit of the PRMT5 complex in vitro and in vivo without receiving symmetrical dimethylarginine (sDMA) modifications, implicating the PRMT5 complex in an early stage of U7 snRNP assembly independent of methylation. Binding of Lsm10 and Lsm11 to SMN is independent of methylation, and two separate binding sites exist in SMN: one recognizing Sm domains and one recognizing sDMA-modified RG-tails. Co-immunoprecipitation, GST pulldown, in vitro binding assays, methylation assays The Journal of biological chemistry Medium 16087681
2006 ZFP100 zinc fingers 5–10 are required for binding to a 20-amino-acid region of Lsm11, and the domain sufficient for Cajal body localization and Lsm11 binding is also sufficient to stimulate histone pre-mRNA processing in vivo, linking the ZFP100–Lsm11 interaction to processing activity. Co-immunoprecipitation, domain truncation, in vivo reporter assay, photobleaching (FRAP) RNA (New York, N.Y.) Medium 16714279
2007 Lsm11 localizes to the histone locus body (HLB) in Drosophila embryos; using anti-Lsm11 antibodies, the HLB is shown to form at nuclear cycle 11 coincident with zygotic histone transcription. Lsm11 foci are present even in histone locus deletion embryos, indicating HLB assembly is not strictly dependent on the histone locus itself. Immunofluorescence, confocal microscopy, genetic ablation of histone locus in embryos Molecular biology of the cell Medium 17442888
2009 FLASH directly interacts with Lsm11 in vitro and in vivo (by yeast two-hybrid and immunoprecipitation), stimulates 3'-end processing of histone pre-mRNA in mammalian nuclear extracts, and is essential for U7-dependent processing in both vertebrates (human) and invertebrates (Drosophila), with FLASH depletion leading to polyadenylation of histone mRNAs. Yeast two-hybrid, GST pulldown (in vitro), co-immunoprecipitation (in vivo), in vitro processing assay (mammalian nuclear extracts), RNAi knockdown in Drosophila cells Molecular cell High 19854135
2009 Three components of the U7-specific Sm ring—SmB, SmD3, and Lsm10—contact the region between the cleavage site and U7-binding site in histone pre-mRNA and likely function as a molecular ruler determining the cleavage site. Lsm11 and SmB were identified as stable components of the 3'-end processing complex assembled on histone pre-mRNA. Biotin-affinity pulldown of processing complex from nuclear extracts, UV cross-linking, mass spectrometry identification Molecular and cellular biology Medium 19470752
2009 Mutations in Drosophila Lsm11 disrupt histone pre-mRNA processing (causing polyadenylated histone mRNA). Lsm10 protein fails to accumulate in Lsm11 mutants, suggesting Lsm10–Lsm11 dimers are precursors for U7 snRNP assembly. Lsm11 is required for U7 snRNA localization to the histone locus body, even though U7 snRNA can still assemble into a trimethylguanosine-capped particle in the absence of Lsm11. Lsm10 and Lsm11 mutants, unlike U7 snRNA null mutants, are lethal, indicating an essential Lsm10/Lsm11 function beyond histone pre-mRNA processing. Drosophila genetics (null mutants), RT-PCR, immunofluorescence, anti-TMG immunoprecipitation RNA (New York, N.Y.) High 19620235
2010 CF Im68, a cleavage/polyadenylation factor, associates with highly purified U7 snRNP and this interaction depends on the N-terminus of Lsm11. Both depletion and overexpression of CF Im68 reduce histone RNA processing efficiency in vivo. The small CF Im subunit CF Im25 does not participate in histone RNA processing. Biochemical purification of U7 snRNP, immunoprecipitation, siRNA knockdown, in vitro processing assay Nucleic acids research Medium 20634199
2011 Amino acids 105–154 of Drosophila FLASH bind to amino acids 1–78 of dLsm11 (N-terminal domain). A two-amino-acid mutation in dLsm11 that abolishes dFLASH binding, without affecting U7 snRNP localization to the HLB, fails to rescue lethality or processing defects caused by Lsm11 null mutation, demonstrating that the FLASH–Lsm11 protein–protein interaction is essential for histone pre-mRNA processing in vivo. Drosophila genetic rescue assay (null mutation complementation), yeast two-hybrid, co-immunoprecipitation, site-directed mutagenesis, immunofluorescence RNA (New York, N.Y.) High 21525146
2011 Scanning mutagenesis identified critical residues in human Lsm11 that mediate its interaction with FLASH. Mutations in FLASH between residues 50–99 that do not affect Lsm11 binding convert FLASH into an inhibitory dominant negative, suggesting this FLASH region plus Lsm11 recruits an additional unknown processing factor. After endonucleolytic cleavage, the 5'→3' exonuclease activity of CPSF73 on the downstream cleavage product depends on Lsm11 but not on FLASH, indicating FLASH is dispensable for activating the exonuclease mode. Scanning mutagenesis, GST pulldown, in vitro processing assay with mammalian nuclear extracts, antibody inhibition Molecular and cellular biology Medium 21245389
2012 The N-terminal regions of FLASH and Lsm11 form a platform that recruits a specific set of polyadenylation factors—symplekin, CstF64, and all CPSF subunits including the CPSF73 endonuclease—to the U7 snRNP. Point mutations in FLASH that abolish processing also inhibit this interaction. The same polyadenylation factors associate with endogenous U7 snRNP and are recruited to histone pre-mRNA in a U7-dependent manner. Co-immunoprecipitation (reciprocal), in vitro binding assays, point mutagenesis, mass spectrometry, histone pre-mRNA pull-down Molecular and cellular biology High 23071092
2013 The Drosophila U7 snRNP contains FLASH and at least six polyadenylation factors (symplekin, CPSF73, CPSF100, CPSF160, WDR33, CstF64) as stable stoichiometric components, and this composite particle is recruited to histone pre-mRNA for processing. A motif in Drosophila FLASH is essential for recruiting the polyadenylation complex to U7 snRNP via Lsm11. Biochemical purification from Drosophila nuclear extracts, mass spectrometry, RNAi knockdown, in vitro processing assay RNA (New York, N.Y.) High 24145821
2017 SLBP stabilizes U7 snRNP binding to histone pre-mRNA via two regions (helix B of its RNA-binding domain and C-terminal region), and this stabilization requires FLASH but not the downstream polyadenylation factors, assigning FLASH a second role: cooperating with SLBP to recruit U7 snRNP to histone pre-mRNA, distinct from its role in forming the polyadenylation factor docking platform with Lsm11. EMSA (gel shift), in vitro processing assay, domain truncation of SLBP/FLASH, UV cross-linking RNA (New York, N.Y.) Medium 28289156
2017 Crystal structures of the FLASH N-terminal domain reveal it forms a coiled-coil dimer. Solution light scattering, analytical ultracentrifugation, and crosslinking show the FLASH NTD–Lsm11 NTD complex is a 2:1 heterotrimer (two FLASH NTD molecules per one Lsm11 NTD). X-ray crystallography, multi-angle light scattering, analytical ultracentrifugation, chemical crosslinking PloS one High 29020104
2019 ALYREF physically interacts with Lsm11 (U7-snRNP-specific component) and promotes histone pre-mRNA 3'-end processing by facilitating U7-snRNP recruitment to histone pre-mRNA. ALYREF also enhances nuclear export of processed histone mRNAs as part of the TREX complex. Co-immunoprecipitation, RNA-immunoprecipitation, siRNA knockdown with processing and export assays The EMBO journal Medium 30858280
2020 Biallelic mutations in LSM11 (encoding a component of the U7 snRNP histone pre-mRNA processing complex) cause misprocessing of canonical histone transcripts, disturb linker histone stoichiometry, alter nuclear cGAS distribution, and enhance cGAS-STING-mediated type I interferon signaling, establishing LSM11 as an Aicardi-Goutières syndrome gene. Chromatin lacking linker histone stimulates cGAMP production more efficiently in vitro, linking histone processing defects to innate immune activation. Patient-derived fibroblast studies, RT-PCR (histone mRNA processing), cGAS localization (immunofluorescence), cGAS in vitro cGAMP synthesis assay with reconstituted chromatin, interferon signaling assays Nature genetics High 33230297
2022 SMN-mediated assembly of U7 snRNP (requiring Lsm10 and Lsm11) is necessary for neuromuscular junction (NMJ) integrity; co-expression of Lsm10 and Lsm11 selectively enhances U7 snRNP assembly, corrects histone mRNA processing defects, and rescues NMJ denervation, synaptic transmission defects, and skeletal muscle atrophy in SMA mice. U7 snRNP dysfunction also drives selective loss of the synaptic organizer Agrin at NMJs in vulnerable muscles. Mouse SMA model (in vivo), AAV-mediated co-expression of Lsm10/Lsm11, RT-PCR (histone mRNA processing), electrophysiology (NMJ transmission), immunofluorescence (NMJ morphology), Western blot (Agrin levels) Cell reports High 36130491
2023 A heterodimer of Lsm10 and Lsm11 tightly interacts with the PRMT5/MEP50/pICln methylosome. Cryo-EM structural studies and biochemical assays show the interaction is mediated by PRMT5, which binds and methylates two arginine residues in the N-terminal region of Lsm11. PRMT5 also methylates an N-terminal arginine in SmE specifically in the U7 context (SmE is not methylated during spliceosomal Sm ring biogenesis). Cryo-EM structure determination, in vitro methylation assay, co-immunoprecipitation, biochemical binding assays RNA (New York, N.Y.) High 37562960
2023 A SUMO-interacting motif (SIM) in the N-terminus of Lsm11 is required for efficient formation of U7 snRNP; in SUMO2 knockout cells, U7 snRNP levels are reduced and histone pre-mRNA 3'-end cleavage is defective with increased histone mRNA polyadenylation. Overexpression of Lsm11 and U7 snRNA rescues U7 snRNP levels and processing defects in SUMO2 KO cells. SUMO2 knockout cell line, rescue by Lsm11/U7 snRNA overexpression, RT-PCR (histone mRNA processing), immunofluorescence (HLB dynamics), SIM deletion mutagenesis Genes & development Medium 40639911
2026 A conserved N-terminal helix of Lsm11 contacts the metallo-β-lactamase domain of the CPSF73 endonuclease within U7 snRNP; mutating or deleting this helix substantially reduces cleavage activity toward histone pre-mRNA. Cryo-EM of reconstituted wild-type U7 snRNP on a noncleavable pre-mRNA shows CPSF73 can adopt an open, active conformation independent of RNA binding at its active site. The CstF77 C-terminus contacts the CPSF100 subunit at a newly identified binding site that modestly contributes to cleavage activity. Cryo-EM structure determination, site-directed mutagenesis (helix deletion/point mutants), in vitro cleavage assay, reconstitution of U7 snRNP with pre-mRNA Nucleic acids research High 41495886
2016 Hydrogen/deuterium exchange mass spectrometry shows the FLASH-interacting domain in Lsm11 is highly dynamic, while a downstream region required for recruiting the histone cleavage complex (HCC) folds into a stable structure. In vitro binding assays reveal Lsm11 also contacts the C-terminal SANT/Myb-like domain of FLASH (the same region that binds NPAT), and this binding partially relaxes (destabilizes) that domain, suggesting competition between Lsm11 and NPAT for FLASH that may regulate histone gene expression. Hydrogen/deuterium exchange mass spectrometry, in vitro GST pulldown binding assays Journal of molecular biology Medium 26860583

Source papers

Stage 0 corpus · 39 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2003 Unique Sm core structure of U7 snRNPs: assembly by a specialized SMN complex and the role of a new component, Lsm11, in histone RNA processing. Genes & development 182 12975319
2020 cGAS-mediated induction of type I interferon due to inborn errors of histone pre-mRNA processing. Nature genetics 165 33230297
2009 FLASH, a proapoptotic protein involved in activation of caspase-8, is essential for 3' end processing of histone pre-mRNAs. Molecular cell 122 19854135
2004 The special Sm core structure of the U7 snRNP: far-reaching significance of a small nuclear ribonucleoprotein. Cellular and molecular life sciences : CMLS 120 15526162
2012 A complex containing the CPSF73 endonuclease and other polyadenylation factors associates with U7 snRNP and is recruited to histone pre-mRNA for 3'-end processing. Molecular and cellular biology 71 23071092
2007 Developmental and cell cycle regulation of the Drosophila histone locus body. Molecular biology of the cell 70 17442888
2019 ALYREF links 3'-end processing to nuclear export of non-polyadenylated mRNAs. The EMBO journal 46 30858280
2010 Muscle wasted: a novel component of the Drosophila histone locus body required for muscle integrity. Journal of cell science 46 20647374
2013 3'-End processing of histone pre-mRNAs in Drosophila: U7 snRNP is associated with FLASH and polyadenylation factors. RNA (New York, N.Y.) 45 24145821
2011 Interaction between FLASH and Lsm11 is essential for histone pre-mRNA processing in vivo in Drosophila. RNA (New York, N.Y.) 41 21525146
2005 Toward an assembly line for U7 snRNPs: interactions of U7-specific Lsm proteins with PRMT5 and SMN complexes. The Journal of biological chemistry 37 16087681
2014 CstF64: cell cycle regulation and functional role in 3' end processing of replication-dependent histone mRNAs. Molecular and cellular biology 34 25266659
2011 FLASH is required for the endonucleolytic cleavage of histone pre-mRNAs but is dispensable for the 5' exonucleolytic degradation of the downstream cleavage product. Molecular and cellular biology 33 21245389
2023 Cyclin E/CDK2 and feedback from soluble histone protein regulate the S phase burst of histone biosynthesis. Cell reports 32 37428633
2009 The Drosophila U7 snRNP proteins Lsm10 and Lsm11 are required for histone pre-mRNA processing and play an essential role in development. RNA (New York, N.Y.) 30 19620235
2017 U7 snRNP is recruited to histone pre-mRNA in a FLASH-dependent manner by two separate regions of the stem-loop binding protein. RNA (New York, N.Y.) 29 28289156
2022 SMN controls neuromuscular junction integrity through U7 snRNP. Cell reports 27 36130491
2006 ZFP100, a component of the active U7 snRNP limiting for histone pre-mRNA processing, is required for entry into S phase. Molecular and cellular biology 27 16914750
2005 U7 snRNP-specific Lsm11 protein: dual binding contacts with the 100 kDa zinc finger processing factor (ZFP100) and a ZFP100-independent function in histone RNA 3' end processing. Nucleic acids research 25 15824063
2021 Identification and validation of RNA-binding protein-related gene signature revealed potential associations with immunosuppression and drug sensitivity in glioma. Cancer medicine 23 34482648
2003 Evolutionary conservation of the U7 small nuclear ribonucleoprotein in Drosophila melanogaster. RNA (New York, N.Y.) 23 14624008
2009 Three proteins of the U7-specific Sm ring function as the molecular ruler to determine the site of 3'-end processing in mammalian histone pre-mRNA. Molecular and cellular biology 21 19470752
2022 Mutations in RNU7-1 Weaken Secondary RNA Structure, Induce MCP-1 and CXCL10 in CSF, and Result in Aicardi-Goutières Syndrome with Severe End-Organ Involvement. Journal of clinical immunology 19 35320431
2010 The 68 kDa subunit of mammalian cleavage factor I interacts with the U7 small nuclear ribonucleoprotein and participates in 3'-end processing of animal histone mRNAs. Nucleic acids research 19 20634199
2019 Composition of the Survival Motor Neuron (SMN) Complex in Drosophila melanogaster. G3 (Bethesda, Md.) 17 30563832
2006 Conserved zinc fingers mediate multiple functions of ZFP100, a U7snRNP associated protein. RNA (New York, N.Y.) 17 16714279
2017 The N-terminal domains of FLASH and Lsm11 form a 2:1 heterotrimer for histone pre-mRNA 3'-end processing. PloS one 14 29020104
2016 Mapping the Interaction Network of Key Proteins Involved in Histone mRNA Generation: A Hydrogen/Deuterium Exchange Study. Journal of molecular biology 11 26860583
2011 Myc localizes to histone locus bodies during replication in Drosophila. PloS one 11 21886841
2021 Aicardi-Goutières Syndrome due to a SAMHD1 Mutation Presenting with Deep White Matter Cysts. Molecular syndromology 6 35418820
2023 CRISPR-Cas9 knockout screen identifies novel treatment targets in childhood high-grade glioma. Clinical epigenetics 5 37161535
2023 In vitro methylation of the U7 snRNP subunits Lsm11 and SmE by the PRMT5/MEP50/pICln methylosome. RNA (New York, N.Y.) 5 37562960
2022 Downregulated miRNAs associated with auditory deafferentation and compensatory neural plastic changes following single-sided deafness in the inferior colliculi of rats. Gene 4 35995115
2023 MiR146a modulates chondrogenesis of bone marrow mesenchymal stem cells by modulating Lsm11 expression. American journal of physiology. Cell physiology 3 36939200
2025 The c.529G>A (p.Ala177Thr) RNASEH2B Gene Pathogenic Variant as a First-Line Genetic Test for Aicardi-Goutières Syndrome: A Case Series of Four Moroccan Families. American journal of medical genetics. Part A 2 39890436
2026 An N-terminal helix of Lsm11 stabilizes CPSF73 in U7 snRNP for histone pre-mRNA 3'-end processing. Nucleic acids research 0 41495886
2025 Proteins that recognize unique features of U7 snRNA and may substitute for Gemin5 in the assembly of U7-specific Sm ring. RNA (New York, N.Y.) 0 40592581
2025 SUMO2 promotes histone pre-mRNA processing by stabilizing histone locus body interactions and facilitating U7 snRNP assembly. Genes & development 0 40639911
2023 In vitro methylation of the U7 snRNP subunits Lsm11 and SmE by the PRMT5/MEP50/pICln methylosome. bioRxiv : the preprint server for biology 0 37215023

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