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    SLBP stem-loop histone mRNA binding protein [ Homo sapiens (human) ]

    Gene ID: 7884, updated on 17-Sep-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    DRAIC promotes growth of breast cancer by sponging miR-432-5p to upregulate SLBP.

    DRAIC promotes growth of breast cancer by sponging miR-432-5p to upregulate SLBP.
    Li S, Jia H, Zhang Z, Wu D.

    07/23/2022
    Influenza A virus co-opts ERI1 exonuclease bound to histone mRNA to promote viral transcription.

    Influenza A virus co-opts ERI1 exonuclease bound to histone mRNA to promote viral transcription.
    Declercq M, Biquand E, Karim M, Pietrosemoli N, Jacob Y, Demeret C, Barbezange C, van der Werf S., Free PMC Article

    11/21/2020
    Knocking down miR-384 promotes growth and metastasis of osteosarcoma MG63 cells by targeting SLBP

    Knocking down miR-384 promotes growth and metastasis of osteosarcoma MG63 cells by targeting SLBP.
    Wang Y, Huang H, Li Y.

    08/3/2019
    SLBP is a potentially important cellular regulator of HIV-1, thereby establishing a link between histone metabolism, inflammation, and HIV-1 infection

    Stem-loop binding protein is a multifaceted cellular regulator of HIV-1 replication.
    Li M, Tucker LD, Asara JM, Cheruiyot CK, Lu H, Wu ZJ, Newstein MC, Dooner MS, Friedman J, Lally MA, Ramratnam B., Free PMC Article

    09/30/2017
    showed that inhibiting the SLBP mRNA and protein levels were rescued by epigenetic modifiers suggesting that nickel's effects on SLBP may be mediated via epigenetic mechanisms

    Nickel and cadmium-induced SLBP depletion: A potential pathway to metal mediated cellular transformation.
    Jordan A, Zhang X, Li J, Laulicht-Glick F, Sun H, Costa M., Free PMC Article

    09/9/2017
    Cyclin F-mediated degradation of SLBP limits H2A.X accumulation and apoptosis upon genotoxic stress in G2 cell cycle checkpoint.

    Cyclin F-Mediated Degradation of SLBP Limits H2A.X Accumulation and Apoptosis upon Genotoxic Stress in G2.
    Dankert JF, Rona G, Clijsters L, Geter P, Skaar JR, Bermudez-Hernandez K, Sassani E, Fenyö D, Ueberheide B, Schneider R, Pagano M., Free PMC Article

    09/2/2017
    CRL4(WDR23) is required for efficient histone mRNA 3' end processing to produce mature histone mRNAs for translation. CRL4(WDR23) binds and ubiquitylates SLBP in vitro and in vivo, and this modification activates SLBP function in histone mRNA 3' end processing without affecting its protein levels.

    CRL4(WDR23)-Mediated SLBP Ubiquitylation Ensures Histone Supply during DNA Replication.
    Brodersen MM, Lampert F, Barnes CA, Soste M, Piwko W, Peter M.

    08/19/2017
    FEM1 proteins are ancient regulators of Stem-Loop Binding Protein.

    FEM1 proteins are ancient regulators of SLBP degradation.
    Dankert JF, Pagan JK, Starostina NG, Kipreos ET, Pagano M., Free PMC Article

    06/24/2017
    CRL4-DCAF11 mediates the degradation of SLBP at the end of S phase and this degradation is essential for the viability of cells.

    DDB1 and CUL4 associated factor 11 (DCAF11) mediates degradation of Stem-loop binding protein at the end of S phase.
    Djakbarova U, Marzluff WF, Köseoğlu MM., Free PMC Article

    06/24/2017
    arsenic, a carcinogenic metal, decreases cellular levels of SLBP by inducing its proteasomal degradation and inhibiting SLBP transcription via epigenetic mechanisms

    Arsenic induces polyadenylation of canonical histone mRNA by down-regulating stem-loop-binding protein gene expression.
    Brocato J, Fang L, Chervona Y, Chen D, Kiok K, Sun H, Tseng HC, Xu D, Shamy M, Jin C, Costa M., Free PMC Article

    01/24/2015
    the S/G2 stable mutant form of SLBP is degraded by proteasome in G1, indicating that indicating that the SLBP degradation in G1 is independent of the previously identified SLBP degradation at S/G2

    Translation regulation and proteasome mediated degradation cooperate to keep stem-loop binding protein low in G1-phase.
    Djakbarova U, Marzluff WF, Köseoğlu MM., Free PMC Article

    10/25/2014
    Although the C-terminal tail of dSLBP does not contact the RNA, phosphorylation of the tail promotes SLBP conformations competent for RNA binding and thereby appears to reduce the entropic penalty for the association.

    Molecular mechanisms for the regulation of histone mRNA stem-loop-binding protein by phosphorylation.
    Zhang J, Tan D, DeRose EF, Perera L, Dominski Z, Marzluff WF, Tong L, Hall TM., Free PMC Article

    10/4/2014
    Alternative splicing allows the synthesis of HBP/SLBP isoforms with different properties that may be important for regulating HBP/SLBP functions during replication stress.

    Replication stress-induced alternative mRNA splicing alters properties of the histone RNA-binding protein HBP/SLBP: a key factor in the control of histone gene expression.
    Rattray AM, Nicholson P, Müller B., Free PMC Article

    09/6/2014
    C-terminal extension of Lsm4 interacts directly with the histone mRNP, contacting both SLBP and 3'hExo.

    The C-terminal extension of Lsm4 interacts directly with the 3' end of the histone mRNP and is required for efficient histone mRNA degradation.
    Lyons SM, Ricciardi AS, Guo AY, Kambach C, Marzluff WF., Free PMC Article

    03/1/2014
    Data suggest that oligomerization and SLBP phosphorylation regulate SLBP-SLIP1-histone-mRNA complex formation/disassociation; sequential and ordered assembly is required.

    Assembly of the SLIP1-SLBP complex on histone mRNA requires heterodimerization and sequential binding of SLBP followed by SLIP1.
    Bansal N, Zhang M, Bhaskar A, Itotia P, Lee E, Shlyakhtenko LS, Lam TT, Fritz A, Berezney R, Lyubchenko YL, Stafford WF, Thapar R, Bansal N, Zhang M, Bhaskar A, Itotia P, Lee E, Shlyakhtenko LS, Lam TT, Fritz A, Berezney R, Lyubchenko YL, Stafford WF, Thapar R., Free PMC Articles: PMC3580866, PMC3580866

    03/16/2013
    Using yeast two-hybrid screening, the authors identify CT initiation factor-interacting protein (CTIF) as a protein that binds directly to SLBP. SLBP preferentially associates with the CT complex of histone mRNAs consisting of CBP80/CBP20, but not with the eIF4E/eIF4G (ET) complex, as has been proposed. Rapid degradation of histone mRNA on the inhibition of DNA replication requires association of SLBP with CTIF.

    Rapid degradation of replication-dependent histone mRNAs largely occurs on mRNAs bound by nuclear cap-binding proteins 80 and 20.
    Choe J, Kim KM, Park S, Lee YK, Song OK, Kim MK, Lee BG, Song HK, Kim YK., Free PMC Article

    03/1/2013
    This paper shows that SLBP is a substrate for the prolyl isomerase Pin1. Pin1, along with PP2A, facilitates dissociation of the SLBP-histone mRNA complex at the end of S-phase, thereby promoting histone mRNA decay and SLBP ubiquitination.

    The prolyl isomerase Pin1 targets stem-loop binding protein (SLBP) to dissociate the SLBP-histone mRNA complex linking histone mRNA decay with SLBP ubiquitination.
    Krishnan N, Lam TT, Fritz A, Rempinski D, O'Loughlin K, Minderman H, Berezney R, Marzluff WF, Thapar R., Free PMC Article

    01/30/2013
    This paper describes the biophysical characterization of human SLBP and the SLBP-SLIP1 complex. Human SLBP is an intrinsically disordered protein that is phosphorylated at 23 Ser/Thr sites when expressed in a eukaryotic expression system such as baculovirus. Unphosphorylated human SLBP forms a high affinity heterotetramer with SLIP1 and the SLBP-SLIP1 complex is regulated by SLBP phosphorylation.

    Assembly of the SLIP1-SLBP complex on histone mRNA requires heterodimerization and sequential binding of SLBP followed by SLIP1.
    Bansal N, Zhang M, Bhaskar A, Itotia P, Lee E, Shlyakhtenko LS, Lam TT, Fritz A, Berezney R, Lyubchenko YL, Stafford WF, Thapar R, Bansal N, Zhang M, Bhaskar A, Itotia P, Lee E, Shlyakhtenko LS, Lam TT, Fritz A, Berezney R, Lyubchenko YL, Stafford WF, Thapar R., Free PMC Articles: PMC3580866, PMC3580866

    01/30/2013
    the crystal structure of a ternary complex of human SLBP RNA binding domain, human 3'hExo, and a 26-nucleotide stem-loop RNA is reported.

    Structure of histone mRNA stem-loop, human stem-loop binding protein, and 3'hExo ternary complex.
    Tan D, Marzluff WF, Dominski Z, Tong L., Free PMC Article

    01/26/2013
    haploinsufficiency of SLBP and/or WHSC2 (NELF-A) contributes to several novel cellular phenotypes of WHS.

    Characterizing the functional consequences of haploinsufficiency of NELF-A (WHSC2) and SLBP identifies novel cellular phenotypes in Wolf-Hirschhorn syndrome.
    Kerzendorfer C, Hannes F, Colnaghi R, Abramowicz I, Carpenter G, Vermeesch JR, O'Driscoll M.

    09/15/2012
    The nuclear magnetic resonance and kinetic studies presented here provide a framework for understanding how SLBP recognizes histone mRNA and highlight possible structural roles of phosphorylation and proline isomerization in RNA binding proteins

    Interaction of the histone mRNA hairpin with stem-loop binding protein (SLBP) and regulation of the SLBP-RNA complex by phosphorylation and proline isomerization.
    Zhang M, Lam TT, Tonelli M, Marzluff WF, Thapar R., Free PMC Article

    06/16/2012
    These results suggest a previously undescribed role for SLBP in histone mRNA export.

    Knockdown of SLBP results in nuclear retention of histone mRNA.
    Sullivan KD, Mullen TE, Marzluff WF, Wagner EJ., Free PMC Article

    01/21/2010
    Study concludes that the increase in cyclin A/Cdk1 activity at the end of S phase triggers degradation of SLBP at S/G(2).

    Phosphorylation of threonine 61 by cyclin a/Cdk1 triggers degradation of stem-loop binding protein at the end of S phase.
    Koseoglu MM, Graves LM, Marzluff WF., Free PMC Article

    01/21/2010
    identified five conserved residues in a 15-amino-acid region in the amino-terminal portion of SLBP, each of which is required for translation.

    SLIP1, a factor required for activation of histone mRNA translation by the stem-loop binding protein.
    Cakmakci NG, Lerner RS, Wagner EJ, Zheng L, Marzluff WF., Free PMC Article

    01/21/2010
    Removal of the phosphoryl group from T230 by either dephosphorylation or mutation results in a 7-fold reduction in the affinity of SLBP for the stem-loop RNA

    Combined top-down and bottom-up proteomics identifies a phosphorylation site in stem-loop-binding proteins that contributes to high-affinity RNA binding.
    Borchers CH, Thapar R, Petrotchenko EV, Torres MP, Speir JP, Easterling M, Dominski Z, Marzluff WF., Free PMC Article

    01/21/2010
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