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    CPSF6 cleavage and polyadenylation specific factor 6 [ Homo sapiens (human) ]

    Gene ID: 11052, updated on 17-Jun-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Downregulation of CPSF6 leads to global mRNA 3' UTR shortening and enhanced antiviral immune responses.

    Downregulation of CPSF6 leads to global mRNA 3' UTR shortening and enhanced antiviral immune responses.
    Ge Y, Huang J, Chen R, Fu Y, Ling T, Ou X, Rong X, Cheng Y, Lin Y, Zhou F, Lu C, Yuan S, Xu A., Free PMC Article

    03/29/2024
    CPSF6 regulates alternative polyadenylation and proliferation of cancer cells through phase separation.

    CPSF6 regulates alternative polyadenylation and proliferation of cancer cells through phase separation.
    Liu S, Wu R, Chen L, Deng K, Ou X, Lu X, Li M, Liu C, Chen S, Fu Y, Xu A.

    11/13/2023
    Alternative polyadenylation factor CPSF6 regulates temperature compensation of the mammalian circadian clock.

    Alternative polyadenylation factor CPSF6 regulates temperature compensation of the mammalian circadian clock.
    Schmal C, Maier B, Ashwal-Fluss R, Bartok O, Finger AM, Bange T, Koutsouli S, Robles MS, Kadener S, Herzel H, Kramer A., Free PMC Article

    07/19/2023
    Formation of nuclear CPSF6/CPSF5 biomolecular condensates upon HIV-1 entry into the nucleus is important for productive infection.

    Formation of nuclear CPSF6/CPSF5 biomolecular condensates upon HIV-1 entry into the nucleus is important for productive infection.
    Luchsinger C, Lee K, Mardones GA, KewalRamani VN, Diaz-Griffero F., Free PMC Article

    07/12/2023
    The roles of CPSF6 in proliferation, apoptosis and tumorigenicity of lung adenocarcinoma.

    The roles of CPSF6 in proliferation, apoptosis and tumorigenicity of lung adenocarcinoma.
    Zu Y, Wang D, Ping W, Sun W., Free PMC Article

    12/17/2022
    Ribonucleic acid-binding protein CPSF6 promotes glycolysis and suppresses apoptosis in hepatocellular carcinoma cells by inhibiting the BTG2 expression.

    Ribonucleic acid-binding protein CPSF6 promotes glycolysis and suppresses apoptosis in hepatocellular carcinoma cells by inhibiting the BTG2 expression.
    Liu Y, Zou H, Xie Q, Zou L, Kong R, Mao B., Free PMC Article

    12/18/2021
    Cleavage and Polyadenylation Specificity Factor 6 Is Required for Efficient HIV-1 Latency Reversal.

    Cleavage and Polyadenylation Specificity Factor 6 Is Required for Efficient HIV-1 Latency Reversal.
    Zheng Y, Schubert HL, Singh PK, Martins LJ, Engelman AN, D'Orso I, Hill CP, Planelles V., Free PMC Article

    11/22/2021
    SAM homeostasis is regulated by CFIm-mediated splicing of MAT2A.

    SAM homeostasis is regulated by CFI(m)-mediated splicing of MAT2A.
    Scarborough AM, Flaherty JN, Hunter OV, Liu K, Kumar A, Xing C, Tu BP, Conrad NK., Free PMC Article

    10/23/2021
    CPSF6 links alternative polyadenylation to metabolism adaption in hepatocellular carcinoma progression.

    CPSF6 links alternative polyadenylation to metabolism adaption in hepatocellular carcinoma progression.
    Tan S, Zhang M, Shi X, Ding K, Zhao Q, Guo Q, Wang H, Wu Z, Kang Y, Zhu T, Sun J, Zhao X., Free PMC Article

    10/23/2021
    Cytoplasmic CPSF6 Regulates HIV-1 Capsid Trafficking and Infection in a Cyclophilin A-Dependent Manner.

    Cytoplasmic CPSF6 Regulates HIV-1 Capsid Trafficking and Infection in a Cyclophilin A-Dependent Manner.
    Zhong Z, Ning J, Boggs EA, Jang S, Wallace C, Telmer C, Bruchez MP, Ahn J, Engelman AN, Zhang P, Watkins SC, Ambrose Z., Free PMC Article

    10/2/2021
    The 4th and 112th Residues of Viral Capsid Cooperatively Modulate Capsid-CPSF6 Interactions of HIV-1.

    The 4th and 112th Residues of Viral Capsid Cooperatively Modulate Capsid-CPSF6 Interactions of HIV-1.
    Saito A, Sultana T, Ode H, Nohata K, Samune Y, Nakayama EE, Iwatani Y, Shioda T., Free PMC Article

    07/3/2021
    MxB impedes the NUP358-mediated HIV-1 pre-integration complex nuclear import and viral replication cooperatively with CPSF6.

    MxB impedes the NUP358-mediated HIV-1 pre-integration complex nuclear import and viral replication cooperatively with CPSF6.
    Xie L, Chen L, Zhong C, Yu T, Ju Z, Wang M, Xiong H, Zeng Y, Wang J, Hu H, Hou W, Feng Y., Free PMC Article

    06/26/2021
    Requirement for cleavage factor IIm in the control of alternative polyadenylation in breast cancer cells.

    Requirement for cleavage factor II(m) in the control of alternative polyadenylation in breast cancer cells.
    Turner RE, Henneken LM, Liem-Weits M, Harrison PF, Swaminathan A, Vary R, Nikolic I, Simpson KJ, Powell DR, Beilharz TH, Dichtl B., Free PMC Article

    10/10/2020
    HIV-1 is more dependent on the K182 capsid residue than HIV-2 for interactions with CPSF6.

    HIV-1 is more dependent on the K182 capsid residue than HIV-2 for interactions with CPSF6.
    Saito A, Ode H, Nohata K, Ohmori H, Nakayama EE, Iwatani Y, Shioda T.

    07/11/2020
    The identification of the direct interaction between viral NP1 and host CPSF6 provides new insights into the mechanism by which a viral small nonstructural protein facilitates the multiple regulation of viral gene expression and replication and reveals a novel target for potent antiviral drug development.

    Cellular Cleavage and Polyadenylation Specificity Factor 6 (CPSF6) Mediates Nuclear Import of Human Bocavirus 1 NP1 Protein and Modulates Viral Capsid Protein Expression.
    Wang X, Xu P, Cheng F, Li Y, Wang Z, Hao S, Wang J, Ning K, Ganaie SS, Engelhardt JF, Yan Z, Qiu J., Free PMC Article

    06/13/2020
    Largely intact HIV-1 capsids dock at the nuclear pore in infected SupT1-R5 cells, with CPSF6 being a facilitator of nucleoplasmic entry in this cell type.

    Analysis of CA Content and CPSF6 Dependence of Early HIV-1 Replication Complexes in SupT1-R5 Cells.
    Zila V, Müller TG, Laketa V, Müller B, Kräusslich HG., Free PMC Article

    05/16/2020
    nuclear entry of HIV-1 subviral complexes in macrophages is mediated by consecutive binding of Nup153 and CPSF6.

    HIV-1 nuclear import in macrophages is regulated by CPSF6-capsid interactions at the nuclear pore complex.
    Bejarano DA, Peng K, Laketa V, Börner K, Jost KL, Lucic B, Glass B, Lusic M, Müller B, Kräusslich HG., Free PMC Article

    04/11/2020
    pol II Chromatin immunoprecipitation-quantitative PCR on a subset of protein coding genes after knocking down CFIm68.

    Effect of CFIm68 knockdown on RNA polymerase II transcription.
    Tellier M, Hardy JG, Norbury CJ, Murphy S., Free PMC Article

    01/25/2020
    The crystal structure of the RSLD-TNPO3 complex revealed potential CPSF6 interaction residues, which were confirmed to mediate TNPO3 binding and CPSF6 nuclear import. Both binding and nuclear import were independent of RSLD phosphorylation, though a hyperphosphorylated mimetic mutant failed to bind TNPO3 and mislocalized to the cell cytoplasm

    Differential role for phosphorylation in alternative polyadenylation function versus nuclear import of SR-like protein CPSF6.
    Jang S, Cook NJ, Pye VE, Bedwell GJ, Dudek AM, Singh PK, Cherepanov P, Engelman AN., Free PMC Article

    11/30/2019
    Study shows that the cellular alternative RNA processing factor CPSF6 plays an important role in the ability of NP1 to suppress internal polyadenylation at (pA)p, in influencing viral mRNA export, and, thus, in modulating gene expression of minute virus of canines, a parvovirus.The cellular RNA processing factor CPSF6 interacted with NP1 in transfected cells and participated with NP1 to modulate its effects.

    Minute Virus of Canines NP1 Protein Interacts with the Cellular Factor CPSF6 To Regulate Viral Alternative RNA Processing.
    Dong Y, Fasina OO, Pintel DJ., Free PMC Article

    10/26/2019
    A novel CPSF6-RARG fusion transcript in acute myeloid leukemia.

    Identification of a novel CPSF6-RARG fusion transcript in acute myeloid leukemia resembling acute promyelocytic leukemia.
    Qin YZ, Huang XJ, Zhu HH.

    06/15/2019
    CPSF6-capsid interactions allow the virus to bypass peripheral heterochromatin and penetrate the nuclear structure for integration.

    Capsid-CPSF6 Interaction Licenses Nuclear HIV-1 Trafficking to Sites of Viral DNA Integration.
    Achuthan V, Perreira JM, Sowd GA, Puray-Chavez M, McDougall WM, Paulucci-Holthauzen A, Wu X, Fadel HJ, Poeschla EM, Multani AS, Hughes SH, Sarafianos SG, Brass AL, Engelman AN., Free PMC Article

    04/6/2019
    The authors demonstrate that CFIm functions as an enhancer-dependent activator of mRNA 3' processing. CFIm regulates global alternative polyadenylation by specifically binding and activating enhancer-containing poly(A) sites.

    Molecular Mechanisms for CFIm-Mediated Regulation of mRNA Alternative Polyadenylation.
    Zhu Y, Wang X, Forouzmand E, Jeong J, Qiao F, Sowd GA, Engelman AN, Xie X, Hertel KJ, Shi Y., Free PMC Article

    12/22/2018
    High CPSF6 expression is associated with HIV infections.

    Truncated CPSF6 Forms Higher-Order Complexes That Bind and Disrupt HIV-1 Capsid.
    Ning J, Zhong Z, Fischer DK, Harris G, Watkins SC, Ambrose Z, Zhang P., Free PMC Article

    08/4/2018
    we found CPSF6 and all core paraspeckles proteins to be overexpressed in human breast cancer cases and their expression to correlate with poor patient outcomes.

    CPSF6 is a Clinically Relevant Breast Cancer Vulnerability Target: Role of CPSF6 in Breast Cancer.
    Binothman N, Hachim IY, Lebrun JJ, Ali S., Free PMC Article

    04/14/2018
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