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Showing TICRR — TRESLIN is a alias.

TICRR

Treslin · UniProt Q7Z2Z1

Length
1910 aa
Mass
210.9 kDa
Annotated
2026-06-10
45 papers in source corpus 21 papers cited in narrative 21 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

TICRR/TRESLIN is an essential metazoan DNA replication initiation factor that acts at the pre-initiation complex (pre-IC) assembly step to load CDC45 onto licensed origins, and its depletion abolishes chromosomal DNA replication (PMID:20116089, PMID:20080954). TRESLIN binds chromatin independently of TopBP1, but its association with the N-terminal BRCT repeats of TopBP1 requires CDK2-cyclin E phosphorylation at conserved CDK consensus sites (S1000/T968 in humans), and this phospho-dependent TRESLIN–TopBP1 interaction is the rate-limiting event for CDC45 loading and origin firing (PMID:20116089, PMID:21700459, PMID:21646402). TRESLIN functions as a stable elongated heterotetramer with MTBP, which contributes a DNA-binding C-terminal domain required for chromatin localization and CDC45 loading; reconstitution requires both proteins together, and the phospho-TRESLIN–MTBP complex is limiting for S-phase duration and origin number (PMID:28877985, PMID:25737283, PMID:34699733). Loading of TRESLIN–MTBP onto phosphorylated MCM2-7 double hexamers is driven by DDK and opposed by RIF1–PP1, an antagonism that defines initiation zones and replication timing, with CDK cooperating with DDK to drive the TopBP1 interaction at the pre-IC step (PMID:41331242, PMID:34699733). TRESLIN abundance and activity are tightly controlled across the cell cycle by CRL4-DTL- and PCNA-dependent proteasomal degradation upon S-phase entry, which moderates active origin number [PMID:34534348, PMID:bio_10.1101_2025.06.10.657920]. The interaction is negatively regulated during replication stress by Chk1, which binds a C-terminal TRESLIN domain (TRCT), directly phosphorylates TRESLIN, and reduces its CDK-site phosphorylation to dissociate TopBP1 and suppress origin firing; loss of Chk1–TRESLIN binding elevates origin firing even in an unperturbed S phase (PMID:25557548, PMID:21700459, PMID:35231445). TRESLIN additionally couples replication initiation to checkpoint signaling by stimulating TopBP1-dependent ATR-mediated Chk1 phosphorylation, and through dynamic, transient action at origins it implements an ATR/Chk1-independent monitoring system that prevents premature G2 entry (PMID:23696651, PMID:36049481).

Mechanistic history

Synthesis pass · year-by-year structured walk · 15 steps
  1. 2010 High

    Established TRESLIN as an essential replication factor acting at the pre-IC step, answering what links origin licensing to helicase activation.

    Evidence Immunodepletion/add-back in Xenopus egg extracts, Co-IP, siRNA knockdown and chromatin fractionation in human/zebrafish cells

    PMID:20080954 PMID:20116089

    Open questions at the time
    • Molecular basis of the TopBP1 interaction not yet defined
    • How CDK activity bridges TRESLIN to TopBP1 unknown
  2. 2011 High

    Identified the CDK2-cyclin E phosphorylation sites on TRESLIN as the molecular switch enabling TopBP1 BRCT binding, explaining how CDK activity licenses initiation.

    Evidence In vitro kinase assay, site-directed mutagenesis of CDK sites, Co-IP and replication rescue in Xenopus and human cells

    PMID:21646402 PMID:21700459

    Open questions at the time
    • Stoichiometry and structure of the phospho-TRESLIN–TopBP1 interface not resolved
    • Whether additional kinases contribute not addressed
  3. 2013 Medium

    Showed TRESLIN is dual-function, stimulating ATR-mediated Chk1 phosphorylation in a TopBP1-dependent manner, linking initiation to checkpoint signaling.

    Evidence In vitro ATR kinase assay, cell-based checkpoint assays, phospho-site mutagenesis

    PMID:23696651

    Open questions at the time
    • Single lab, not independently confirmed
    • Mechanism by which Ser-1000 status modulates ATR signaling unclear
  4. 2014 High

    Defined how Chk1 docks onto TRESLIN to restrain origin firing in unperturbed S phase, revealing a built-in negative regulator of CDC45 loading.

    Evidence Co-IP, TRCT domain mutagenesis abolishing binding, EdU and CDC45 chromatin-loading assays

    PMID:25557548

    Open questions at the time
    • Which TRESLIN residues Chk1 phosphorylates not yet mapped here
    • Relationship to CDK-site phosphorylation not resolved
  5. 2017 High

    Established MTBP as the obligate TRESLIN partner and DNA-binding module required for chromatin loading and CDC45 recruitment.

    Evidence Immunodepletion/add-back reconstitution in Xenopus extracts, DNA-binding assays, CTM domain mutagenesis, human S-phase assays

    PMID:28877985

    Open questions at the time
    • Structural basis of TRESLIN–MTBP assembly not defined
    • DNA sequence preference of CTM in vivo not established
  6. 2017 Medium

    Demonstrated multiple layers controlling TRESLIN abundance and CDK-driven activity (Gwl/Ensa/PP2A-B55 degradation, CKS-enhanced phosphorylation, and mutant-p53 bypass), framing TRESLIN as a tightly tuned limiting factor.

    Evidence siRNA knockdown with rescue, proteasome inhibition, in vitro kinase assays with CKS, Co-IP and BrdU assays with p53 mutants and CDK2 inhibitor

    PMID:28439015 PMID:28739856 PMID:28785014

    Open questions at the time
    • Each mechanism from a single lab
    • How these regulatory inputs are integrated in vivo unclear
  7. 2015 Medium

    Showed that phosphomimetic TRESLIN shortens S phase by increasing initiation in an MTBP-interaction-dependent manner, establishing phospho-TRESLIN as rate-limiting for S-phase progression.

    Evidence Phosphomimetic TICRR-TESE overexpression, EdU incorporation, DNA fiber and replication cluster analysis in human cells

    PMID:25737283

    Open questions at the time
    • Single lab
    • Whether endogenous phospho-occupancy is limiting not directly measured
  8. 2020 Medium

    Mapped genome-wide TRESLIN-MTBP occupancy, linking the complex to open chromatin and regulatory elements rather than random origins.

    Evidence MTBP ChIP-seq with chromatin accessibility and histone modification correlation in human cells

    PMID:32966791

    Open questions at the time
    • Whether all binding sites correspond to firing origins unknown
    • Functional consequence of regulatory-element binding not established
  9. 2021 Medium

    Resolved complex stoichiometry (2:2 tetramer) and established that DDK strengthens TRESLIN-MTBP chromatin loading and cooperates with CDK for TopBP1 engagement.

    Evidence Immunodepletion/add-back in Xenopus extracts, biochemical stoichiometry, kinase inhibitor treatments

    PMID:34699733

    Open questions at the time
    • High-resolution structure of the tetramer not determined
    • DDK substrate site driving loading not mapped here
  10. 2021 Medium

    Identified CRL4-DTL-dependent S-phase degradation of TICRR as a mechanism limiting active origin number.

    Evidence Cell-cycle synchronization, immunoblotting, siRNA screen of E3 components, proteasome inhibition

    PMID:34534348

    Open questions at the time
    • Degron and ubiquitination sites not mapped
    • Single lab
  11. 2022 Medium

    Detailed how Chk1 dissociates TopBP1 from TRESLIN during stress via combined CDK-activity reduction (T968) and direct phosphorylation (S1114), refining the negative-regulatory mechanism.

    Evidence Phospho-specific antibodies, CDK/Chk1 inhibitors, mutagenesis, origin firing assays in cancer cells

    PMID:35231445

    Open questions at the time
    • Relative contribution of each phospho-event in vivo not quantified
    • Single lab
  12. 2022 Medium

    Revealed TRESLIN-MTBP acts transiently at origins and operates an ATR/CHK1-independent surveillance of origin-firing dynamics that governs the S/G2 transition.

    Evidence Live-cell imaging, chromatin fractionation, ATR/CHK1 inhibitors, knockdowns in human cells

    PMID:36049481

    Open questions at the time
    • Molecular sensor mechanism not defined
    • Single lab
  13. 2022 Low

    Provided a domain architecture for TRESLIN, assigning a Sld3-homologous core (Ku70-like M domain, Sld3-Treslin domain, TopBP1-interaction domain) required for origin firing.

    Evidence Sequence analysis, structural homology modeling, domain mutant expression with replication assays in human cells

    PMID:35091422

    Open questions at the time
    • Structural assignment is computational, not experimentally solved
    • Single lab
  14. 2025 Medium

    Established that DDK vs RIF1-PP1 phosphorylation of MCM-DH controls TRESLIN-MTBP loading to set initiation zones and replication timing, and that G1 chromatin binding is licensing-independent with distinct G1 vs S binding modes.

    Evidence Genome-wide TRESLIN-MTBP and MCM mapping, kinase/phosphatase inhibitors, Cut&Run, Geminin-based MCM depletion, siRNA in human cells

    PMID:40624716 PMID:41331242

    Open questions at the time
    • Function of licensing-independent G1 binding unknown
    • Structural basis of phospho-MCM recognition not defined
  15. 2025 Medium

    Linked CDK-sensitive, PCNA-dependent TRESLIN degradation to dormant origin firing under WEE1 inhibition, identifying a conserved degron-like sequence governing this control.

    Evidence WEE1/CDK inhibitor epistasis, PCNA dependency assays, chromatin fractionation, DNA fiber analysis, domain mutagenesis (preprint)

    PMID:bio_10.1101_2025.06.10.657920

    Open questions at the time
    • Preprint, not peer-reviewed
    • Precise degron residues and ubiquitin ligase coupling to PCNA unresolved

Open questions

Synthesis pass · forward-looking unresolved questions
  • How TRESLIN-MTBP physically recognizes the phosphorylated MCM2-7 double hexamer and assembles CDC45 at atomic resolution, and how its multiple regulatory inputs are integrated to select specific origins, remain unresolved.
  • No experimental high-resolution structure of TRESLIN-MTBP or its origin complexes
  • Mechanism of origin-site selection from genome-wide binding not fully defined
  • Integration of degradation, checkpoint, and kinase inputs into a single quantitative model lacking

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 4 GO:0003677 DNA binding 2
Localization
GO:0005694 chromosome 4 GO:0005634 nucleus 2
Pathway
R-HSA-69306 DNA Replication 5 R-HSA-1640170 Cell Cycle 3 R-HSA-8953897 Cellular responses to stimuli 3
Partners
CDK2CHEK1CKS1BDTLDUE-B/UBE2V2MTBPTOPBP1TP53
Complex memberships
TRESLIN-MTBP complex

Evidence

Reading pass · 21 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2010 Treslin (TICRR) associates with TopBP1 in Xenopus egg extracts and human cells, and is required for loading of Cdc45 onto chromatin. Depletion of Treslin strongly inhibits chromosomal DNA replication. Treslin binds chromatin independently of TopBP1, but Treslin-TopBP1 association requires Cdk2 activity and is necessary for Cdc45 loading. Immunodepletion from Xenopus egg extracts, co-immunoprecipitation, siRNA knockdown in human cells, chromatin fractionation Cell High 20116089
2010 TICRR (ticrr) associates with TopBP1 via BRCT motifs essential for TopBP1's replication and checkpoint functions, and ticrr deficiency disrupts chromatin binding of pre-initiation complex (pre-IC) components without affecting pre-replication complex (pre-RC) loading, placing TICRR at the pre-IC assembly step. Zebrafish genetic screen, co-immunoprecipitation, chromatin fractionation, morpholino knockdown Genes & development High 20080954
2011 Treslin/TICRR contains two conserved CDK phosphorylation sites (orthologous to yeast Sld3 CDK sites) that are essential for DNA replication. Phosphorylation of these sites mediates interaction with the N-terminal pair of BRCT repeats in TopBP1 (ortholog of yeast Dpb11). Replication stress prevents this interaction via the Chk1 checkpoint kinase. Mutagenesis of CDK sites, co-immunoprecipitation, siRNA knockdown with replication assays, sequence conservation analysis Current biology : CB High 21700459
2011 Treslin is phosphorylated by Cdk2-cyclin E at a conserved CDK consensus site (S976 in Xenopus, S1000 in humans). This phosphorylation is required for effective association with TopBP1 and for DNA replication. A non-phosphorylatable mutant shows severely diminished TopBP1 binding and replication deficiency. In vitro kinase assay with recombinant Cdk2-cyclin E, site-directed mutagenesis, co-immunoprecipitation, human cell replication assays The Journal of cell biology High 21646402
2014 Chk1 associates specifically with a C-terminal domain of Treslin (TRCT domain). This interaction enables Chk1-catalyzed phosphorylation of Treslin. Abolishing the Treslin-Chk1 interaction results in elevated replication initiation during an unperturbed S phase due to enhanced Cdc45 loading, revealing a Chk1 role in suppressing origin firing during normal S phase. Co-immunoprecipitation, TRCT domain mutagenesis, EdU incorporation assays, Cdc45 chromatin loading analysis Molecular cell High 25557548
2013 Treslin stimulates ATR-mediated phosphorylation of Chk1 both in vitro and in vivo in a TopBP1-dependent manner, and the phosphorylation state of Treslin at Ser-1000 is important for this checkpoint activity, indicating Treslin is a dual replication/checkpoint protein. In vitro ATR kinase assay, cell-based checkpoint assays, phosphorylation site mutagenesis The Journal of biological chemistry Medium 23696651
2015 Overexpression of a phosphomimetic TICRR mutant (TICRR-TESE, mimicking CDK phosphorylation at two key residues) shortens S phase by increasing replication initiation. This effect requires the TICRR region necessary for interaction with MTBP (Mdm2-binding protein), demonstrating that phosphorylated TICRR is limiting for S-phase progression. Phosphomimetic mutant overexpression, EdU incorporation, DNA fiber analysis, replication cluster analysis in human cells Genes & development Medium 25737283
2017 MTBP (Mdm2-binding protein) is a binding partner of Treslin. Depletion of MTBP from Xenopus egg extracts co-depletes Treslin and abolishes DNA replication, which can only be rescued by recombinant Treslin-MTBP together, not either protein alone. MTBP contains a C-terminal domain (CTM) that binds double-stranded and G-quadruplex DNA, and CTM mutants are defective for chromatin localization and Cdc45 loading. Immunodepletion and add-back in Xenopus egg extracts, DNA-binding assays, chromatin fractionation, human cell S-phase assays, domain mutagenesis Molecular biology of the cell High 28877985
2017 Ensa (a substrate of Greatwall kinase) controls Treslin protein levels via the ubiquitin-proteasome pathway. Ensa knockdown reduces Treslin levels and extends S phase; this phenotype is rescued by Treslin overexpression. The Gwl/Ensa/PP2A-B55 pathway thus regulates S-phase duration by controlling Treslin degradation. siRNA knockdown, proteasome inhibitor treatment, rescue experiments with Treslin overexpression, flow cytometry Nature communications Medium 28785014
2017 Mutant p53 (contact-type, e.g. R273H) enhances the interaction between TopBP1 and Treslin and promotes DNA replication even when Cdk2 is inhibited, bypassing the normal CDK requirement for Treslin-TopBP1 interaction. Co-immunoprecipitation, BrdU incorporation assays, CDK2 inhibitor treatment, expression of specific p53 mutants Proceedings of the National Academy of Sciences of the United States of America Medium 28439015
2021 MTBP forms an elongated tetramer with Treslin containing two molecules of each protein. Treslin-MTBP is rate-limiting for replication initiation. DDK activity both increases and strengthens the interaction of Treslin-MTBP with licensed chromatin, and cooperates with CDK to drive Treslin-MTBP interaction with TopBP1 at the pre-IC formation step. Immunodepletion and add-back in Xenopus egg extracts, biochemical characterization of complex stoichiometry, kinase inhibitor treatments Open biology Medium 34699733
2021 TICRR/TRESLIN protein levels are high in G1 and decrease upon S-phase entry via CRL4-DTL E3 ubiquitin ligase-dependent proteasomal degradation. This mechanism moderates TICRR levels to control the number of active origins during S phase. Cell cycle synchronization, immunoblotting, siRNA screens targeting E3 ligase components, proteasome inhibitor treatment Nucleic acids research Medium 34534348
2020 MTBP (and hence the Treslin-MTBP complex) binds to at least 30,000 sites in the human genome, preferentially at regions of open chromatin containing transcriptional-regulatory elements (promoters, enhancers, super-enhancers) with nucleosome-free DNA (G-quadruplex or AP-1 motifs) and H3K4me2-marked nucleosomes. ChIP-seq genome-wide mapping of MTBP in human cells, correlation with chromatin accessibility and histone modification datasets Cell reports Medium 32966791
2022 TRESLIN-MTBP acts transiently at pre-replication complexes to initiate origin firing and is released after CDC45 recruitment. The dynamic behavior of TRESLIN-MTBP implements a monitoring system that senses the rate of origin firing and the decline of active origins in late S phase, preventing premature entry into G2 independently of ATR/CHK1 kinases. Live-cell imaging, chromatin fractionation, cell cycle analysis, ATR/CHK1 inhibitor treatments, knockdown experiments Molecular cell Medium 36049481
2022 Chk1 regulates the Treslin-TopBP1 interaction through multiple mechanisms during replication stress: (1) Chk1-dependent decrease in CDK activity reduces phosphorylation of Treslin T968 (but not S1000), and (2) Chk1 directly phosphorylates additional sites on Treslin including S1114, both contributing to dissociation of TopBP1 from Treslin and suppression of origin firing. Phospho-specific antibodies, CDK inhibitor and Chk1 inhibitor treatments, mutagenesis, replication origin firing assays in cancer cell lines The Journal of biological chemistry Medium 35231445
2018 DUE-B interacts with Treslin in HeLa cells in a cell-cycle-regulated manner (peaking as cells exit G1). The conserved C-terminal domain of DUE-B is required for its binding to TopBP1, Treslin, Cdc45, and MCM2-7, and for efficient chromatin loading of Treslin, Cdc45, and TopBP1. The DUE-B-Treslin interaction is required for Cdc45 loading onto chromatin. Co-immunoprecipitation, domain mutagenesis, chromatin fractionation, cell cycle synchronization The Journal of biological chemistry Medium 30037903
2017 CKS proteins (Cks1, Cks2) enhance the ability of Cdk2 to phosphorylate Treslin in vitro, promoting replication checkpoint recovery. CKS binding-defective mutants retain the ability to stimulate Treslin phosphorylation. Silencing of Cks1/Cks2 decreases Treslin phosphorylation in vivo, and CKS overexpression prevents checkpoint-dependent dephosphorylation of Treslin. In vitro kinase assay, siRNA knockdown, CKS mutant overexpression, phospho-Treslin immunoblotting Molecular and cellular biology Medium 28739856
2025 TRESLIN-MTBP is a key limiting firing factor for replication initiation in human cells. Its loading onto phosphorylated MCM2-7 double hexamer (MCM-DH) is controlled by opposing phosphorylation events on MCM-DH by DDK (promoting TRESLIN-MTBP loading) and RIF1-Protein Phosphatase 1 (opposing loading), which determines initiation zones and establishes replication timing. Genome-wide mapping of TRESLIN-MTBP and MCM, kinase/phosphatase inhibitor treatments, chromatin fractionation in human cells Nature communications Medium 41331242
2025 During G1, MTBP depends on TRESLIN for proper chromatin association, but not during S phase, suggesting two distinct modes of TRESLIN-MTBP chromatin binding. Neither TRESLIN nor MTBP binding to chromatin during G1 requires licensed MCM origins. Cut&Run genomic binding mapping, cell cycle synchronization, Geminin-based MCM depletion, siRNA knockdown of TRESLIN/MTBP Genome biology Medium 40624716
2022 Sequence analysis and structural homology modeling revealed that Treslin/TICRR contains a conserved Ku70-homologous β-barrel fold in its middle domain (M domain), and a von Willebrand factor type A domain in the CIT region. The M domain, Sld3-Treslin domain, and TopBP1/Dpb11 interaction domain together constitute the Sld3-homologous core. Domain mutants expressed in human cells indicate all three Sld3-core domains plus non-conserved terminal domains are required for proper origin firing. Protein sequence analysis, structural homology modeling, domain mutant expression in human cells with replication assays Life science alliance Low 35091422
2025 WEE1 kinase inhibition during S phase increases CDK activity, which blocks PCNA-dependent proteasomal degradation of TRESLIN and enhances chromatin association of TRESLIN and MTBP, leading to elevated helicase recruitment and dormant origin firing. A conserved sequence within TRESLIN is required for this CDK-sensitive degradation. WEE1 inhibitor treatment, CDK inhibitor reversal, PCNA dependency assays, chromatin fractionation, DNA fiber analysis in human cells, domain mutagenesis bioRxivpreprint Medium bio_10.1101_2025.06.10.657920

Source papers

Stage 0 corpus · 45 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2006 Phosphorylation of Sld2 and Sld3 by cyclin-dependent kinases promotes DNA replication in budding yeast. Nature 390 17167417
2006 CDK-dependent phosphorylation of Sld2 and Sld3 initiates DNA replication in budding yeast. Nature 374 17167415
2010 Checkpoint-dependent inhibition of DNA replication initiation by Sld3 and Dbf4 phosphorylation. Nature 227 20835227
2010 Treslin collaborates with TopBP1 in triggering the initiation of DNA replication. Cell 208 20116089
2011 Origin association of Sld3, Sld7, and Cdc45 proteins is a key step for determination of origin-firing timing. Current biology : CB 202 22169533
2001 Sld3, which interacts with Cdc45 (Sld4), functions for chromosomal DNA replication in Saccharomyces cerevisiae. The EMBO journal 186 11296242
2010 Damage-induced phosphorylation of Sld3 is important to block late origin firing. Nature 154 20865002
2011 Regulation of DNA replication through Sld3-Dpb11 interaction is conserved from yeast to humans. Current biology : CB 115 21700459
2016 Phosphopeptide binding by Sld3 links Dbf4-dependent kinase to MCM replicative helicase activation. The EMBO journal 108 26912723
2010 A vertebrate gene, ticrr, is an essential checkpoint and replication regulator. Genes & development 106 20080954
2011 Direct regulation of Treslin by cyclin-dependent kinase is essential for the onset of DNA replication. The Journal of cell biology 105 21646402
2006 Distinct roles for Sld3 and GINS during establishment and progression of eukaryotic DNA replication forks. The EMBO journal 105 16601689
2014 Interaction of Chk1 with Treslin negatively regulates the initiation of chromosomal DNA replication. Molecular cell 78 25557548
2006 Ordered assembly of Sld3, GINS and Cdc45 is distinctly regulated by DDK and CDK for activation of replication origins. The EMBO journal 72 16990792
2011 Sld7, an Sld3-associated protein required for efficient chromosomal DNA replication in budding yeast. The EMBO journal 53 21487389
2015 Cyclin-dependent kinase regulates the length of S phase through TICRR/TRESLIN phosphorylation. Genes & development 51 25737283
2017 Ensa controls S-phase length by modulating Treslin levels. Nature communications 47 28785014
2017 MTBP, the partner of Treslin, contains a novel DNA-binding domain that is essential for proper initiation of DNA replication. Molecular biology of the cell 39 28877985
2017 Mutant p53 perturbs DNA replication checkpoint control through TopBP1 and Treslin. Proceedings of the National Academy of Sciences of the United States of America 36 28439015
2011 CDK promotes interactions of Sld3 and Drc1 with Cut5 for initiation of DNA replication in fission yeast. Molecular biology of the cell 30 21593208
2015 The quaternary structure of the eukaryotic DNA replication proteins Sld7 and Sld3. Acta crystallographica. Section D, Biological crystallography 29 26249346
2016 Concerted activities of Mcm4, Sld3, and Dbf4 in control of origin activation and DNA replication fork progression. Genome research 27 26733669
2011 Origin single-stranded DNA releases Sld3 protein from the Mcm2-7 complex, allowing the GINS tetramer to bind the Mcm2-7 complex. The Journal of biological chemistry 27 21460226
2014 Crystal structure of the homology domain of the eukaryotic DNA replication proteins Sld3/Treslin. Structure (London, England : 1993) 24 25126958
2011 GINS and Sld3 compete with one another for Mcm2-7 and Cdc45 binding. The Journal of biological chemistry 24 21362622
2021 The role of DDK and Treslin-MTBP in coordinating replication licensing and pre-initiation complex formation. Open biology 23 34699733
2020 Binding of the Treslin-MTBP Complex to Specific Regions of the Human Genome Promotes the Initiation of DNA Replication. Cell reports 22 32966791
2019 TICRR Contributes to Tumorigenesis Through Accelerating DNA Replication in Cancers. Frontiers in oncology 20 31275851
2022 The TRESLIN-MTBP complex couples completion of DNA replication with S/G2 transition. Molecular cell 19 36049481
2013 Direct role for the replication protein treslin (Ticrr) in the ATR kinase-mediated checkpoint response. The Journal of biological chemistry 17 23696651
2021 The CRL4DTL E3 ligase induces degradation of the DNA replication initiation factor TICRR/TRESLIN specifically during S phase. Nucleic acids research 16 34534348
2011 DNA replication: mammalian Treslin-TopBP1 interaction mirrors yeast Sld3-Dpb11. Current biology : CB 16 21855008
2016 Sld3-MCM Interaction Facilitated by Dbf4-Dependent Kinase Defines an Essential Step in Eukaryotic DNA Replication Initiation. Frontiers in microbiology 15 27375603
2015 The Replication Initiation Protein Sld3/Treslin Orchestrates the Assembly of the Replication Fork Helicase during S Phase. The Journal of biological chemistry 13 26405041
2022 Refining the domain architecture model of the replication origin firing factor Treslin/TICRR. Life science alliance 8 35091422
2010 DNA replication: metazoan Sld3 steps forward. Current biology : CB 7 20620904
2025 Cell cycle-dependent TICRR/TRESLIN and MTBP chromatin binding mechanisms and patterns. Genome biology 6 40624716
2025 Regulated TRESLIN-MTBP loading governs initiation zones and replication timing in human DNA replication. Nature communications 5 41331242
2017 CKS Proteins Promote Checkpoint Recovery by Stimulating Phosphorylation of Treslin. Molecular and cellular biology 5 28739856
2024 Cell Cycle-Dependent TICRR/TRESLIN and MTBP Chromatin Binding Mechanisms and Patterns. bioRxiv : the preprint server for biology 4 38370757
2018 Interaction between DUE-B and Treslin is required to load Cdc45 on chromatin in human cells. The Journal of biological chemistry 4 30037903
2021 Interaction of replication factor Sld3 and histone acetyl transferase Esa1 alleviates gene silencing and promotes the activation of late and dormant replication origins. Genetics 3 33683348
2012 Treslin, DUE-B, and GEMC1 cannot complement Sld3 mutants in fission yeast. FEMS yeast research 3 22380713
2022 Intra-S phase checkpoint kinase Chk1 dissociates replication proteins Treslin and TopBP1 through multiple mechanisms during replication stress. The Journal of biological chemistry 2 35231445
2025 Deciphering TICRR's oncogenic landscape in pancreatic adenocarcinoma: molecular insights and clinical implications. Discover oncology 0 41105363

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