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    TP53INP2 tumor protein p53 inducible nuclear protein 2 [ Homo sapiens (human) ]

    Gene ID: 58476, updated on 2-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    TP53INP2-dependent activation of muscle autophagy ameliorates sarcopenia and promotes healthy aging.

    TP53INP2-dependent activation of muscle autophagy ameliorates sarcopenia and promotes healthy aging.
    Sebastián D, Beltrà M, Irazoki A, Sala D, Aparicio P, Aris C, Alibakhshi E, Rubio-Valera M, Palacín M, Castellanos J, Lores L, Zorzano A., Free PMC Article

    08/20/2024
    TP53INP2 modulates the malignant progression of colorectal cancer by reducing the inactive form of beta-catenin.

    TP53INP2 modulates the malignant progression of colorectal cancer by reducing the inactive form of β-catenin.
    Shi K, Shan Y, Sun X, Chen K, Luo Q, Xu Q.

    01/5/2024
    Cytoplasmic Expression of TP53INP2 Modulated by Demethylase FTO and Mutant NPM1 Promotes Autophagy in Leukemia Cells.

    Cytoplasmic Expression of TP53INP2 Modulated by Demethylase FTO and Mutant NPM1 Promotes Autophagy in Leukemia Cells.
    Huang J, Sun M, Tao Y, Ren J, Peng M, Jing Y, Xiao Q, Yang J, Lin C, Lei L, Yang Z, Zhang L., Free PMC Article

    02/4/2023
    Inactivation of ZSCAN18 by promoter hypermethylation drives the proliferation via attenuating TP53INP2-mediated autophagy in gastric cancer cells.

    Inactivation of ZSCAN18 by promoter hypermethylation drives the proliferation via attenuating TP53INP2-mediated autophagy in gastric cancer cells.
    Li B, Ren B, Ma G, Cai F, Wang P, Zeng Y, Liu Y, Zhang L, Yang Y, Liang H, Zhang R, Deng J., Free PMC Article

    01/21/2023
    TP53INP2 Contributes to TGF-beta2-Induced Autophagy during the Epithelial-Mesenchymal Transition in Posterior Capsular Opacification Development.

    TP53INP2 Contributes to TGF-β2-Induced Autophagy during the Epithelial-Mesenchymal Transition in Posterior Capsular Opacification Development.
    Cui Y, Yang H, Shi S, Ping X, Zheng S, Tang X, Yu X, Shentu X., Free PMC Article

    08/20/2022
    Overexpression of TP53INP2 Promotes Apoptosis in Clear Cell Renal Cell Cancer via Caspase-8/TRAF6 Signaling Pathway.

    Overexpression of TP53INP2 Promotes Apoptosis in Clear Cell Renal Cell Cancer via Caspase-8/TRAF6 Signaling Pathway.
    Li X, Hu D, Li Y, Luo Y, Liang B, Yu K, Xiong W, Zuo D., Free PMC Article

    06/18/2022
    Dysregulation in the expression of (lncRNA-TSIX, TP53INP2 mRNA, miRNA-1283) in spinal cord injury.

    Dysregulation in the expression of (lncRNA-TSIX, TP53INP2 mRNA, miRNA-1283) in spinal cord injury.
    Salah SMM, Matboli M, Nasser HE, Abdelnaiem IA, Shafei AE, El-Asmer MF.

    08/21/2021
    The bifunctional role of TP53INP2 in transcription and autophagy.

    The bifunctional role of TP53INP2 in transcription and autophagy.
    Xu Y, Wan W., Free PMC Article

    07/31/2021
    TP53INP2 interacted directly with ATG7 to form a LC3B-TP53INP2-ATG7 complex in the cytoplasm.

    TP53INP2 contributes to autophagosome formation by promoting LC3-ATG7 interaction.
    You Z, Xu Y, Wan W, Zhou L, Li J, Zhou T, Shi Y, Liu W., Free PMC Article

    07/11/2020
    Results showed that TP53INP2 interacts with ubiquitin and ubiquitinated proteins through the ubiquitin-interacting motif (UIM). Moreover, overexpression of TP53INP2 lacking the UIM in cells leads to massive accumulation of ubiquitinated proteins and sensitizes the cells to apoptosis under stressed conditions.

    TP53INP2 mediates autophagic degradation of ubiquitinated proteins through its ubiquitin-interacting motif.
    Xu Y, Wan W.

    06/6/2020
    A screen of cancer cell lines showed that those with higher protein levels of TP53INP2 are more prone to TRAIL-induced apoptosis, making TP53INP2 a potential predictive marker of cancer cell responsiveness to TRAIL treatment. These findings uncover a novel mechanism for the regulation of caspase-8 ubiquitination and reveal TP53INP2 as an important regulator of the death receptor pathway.

    Regulation of death receptor signaling by the autophagy protein TP53INP2.
    Ivanova S, Polajnar M, Narbona-Perez AJ, Hernandez-Alvarez MI, Frager P, Slobodnyuk K, Plana N, Nebreda AR, Palacin M, Gomis RR, Behrends C, Zorzano A., Free PMC Article

    01/11/2020
    Tp53inp2 is an atypical mRNA that regulates axon growth by enhancing NGF-TrkA signaling in a translation-independent manner.

    Regulation of NGF Signaling by an Axonal Untranslated mRNA.
    Crerar H, Scott-Solomon E, Bodkin-Clarke C, Andreassi C, Hazbon M, Logie E, Cano-Jaimez M, Gaspari M, Kuruvilla R, Riccio A., Free PMC Article

    11/16/2019
    TP53INP2 modulates adipogenesis through autophagy-dependent sequestration of GSK3beta into late endosomes and beta catenin activation, regulating adiposity.

    TP53INP2 regulates adiposity by activating β-catenin through autophagy-dependent sequestration of GSK3β.
    Romero M, Sabaté-Pérez A, Francis VA, Castrillón-Rodriguez I, Díaz-Ramos Á, Sánchez-Feutrie M, Durán X, Palacín M, Moreno-Navarrete JM, Gustafson B, Hammarstedt A, Fernández-Real JM, Vendrell J, Smith U, Zorzano A.

    04/20/2019
    TP53INP2 promotes ribosome biogenesis through facilitating rRNA synthesis at the nucleolus

    TP53INP2/DOR, a mediator of cell autophagy, promotes rDNA transcription via facilitating the assembly of the POLR1/RNA polymerase I preinitiation complex at rDNA promoters.
    Xu Y, Wan W, Shou X, Huang R, You Z, Shou Y, Wang L, Zhou T, Liu W., Free PMC Article

    01/20/2018
    We conducted a replication study using a dataset outside of the Challenge, and found the association between TP53INP2 and ER-negative breast cancer was significant (p = 5.07x10-3). Expression of HP (16q22.2) showed a suggestive association with ER-negative breast cancer in the discovery phase (Z = 4.30, p = 1.70x10-5) although the association was not significant after Bonferroni adjustment.

    Trans-ethnic predicted expression genome-wide association analysis identifies a gene for estrogen receptor-negative breast cancer.
    Gao G, Pierce BL, Olopade OI, Im HK, Huo D., Free PMC Article

    10/14/2017
    The results reveal the association of TP53INP2-related basal autophagy with cell growth and malignant progression of human liposarcoma.

    TP53INP2-related basal autophagy is involved in the growth and malignant progression in human liposarcoma cells.
    Hu Y, Li X, Xue W, Pang J, Meng Y, Shen Y, Xu Q.

    04/1/2017
    nucleolus integrity is not essential for both DOR nucleo-cytoplasmic shuttling and DOR function on basal autophagy

    DOR undergoes nucleo-cytoplasmic shuttling, which involves passage through the nucleolus.
    Mauvezin C, Sancho A, Ivanova S, Palacin M, Zorzano A.

    12/8/2012
    Mutation of conserved hydrophobic residues in region 1 of TP53inp2 reduces transcriptional activity, and blocks nuclear exit and autophagic activity under autophagy-activated conditions.

    DOR/Tp53inp2 and Tp53inp1 constitute a metazoan gene family encoding dual regulators of autophagy and transcription.
    Sancho A, Duran J, García-España A, Mauvezin C, Alemu EA, Lamark T, Macias MJ, DeSalle R, Royo M, Sala D, Chicote JU, Palacín M, Johansen T, Zorzano A., Free PMC Article

    08/4/2012
    DOR plays an important role in thyroid hormone-mediated osteoblast differentiation, and a DOR SNP associates with plasma osteocalcin in men.

    Role of diabetes- and obesity-related protein in the regulation of osteoblast differentiation.
    Linares GR, Xing W, Burghardt H, Baumgartner B, Chen ST, Ricart W, Fernández-Real JM, Zorzano A, Mohan S., Free PMC Article

    09/10/2011
    Alternative splicing of an exon in the 5' untranslated region of a gene termed TP53INP2 is a key event downstream of hnRNP A2 that is necessary for cells to invade the extracellular matrix.

    hnRNP A2 regulates alternative mRNA splicing of TP53INP2 to control invasive cell migration.
    Moran-Jones K, Grindlay J, Jones M, Smith R, Norman JC., Free PMC Article

    01/21/2010
    TP53INP2 is a novel gene involved in the autophagy of mammalian cells.

    The TP53INP2 protein is required for autophagy in mammalian cells.
    Nowak J, Archange C, Tardivel-Lacombe J, Pontarotti P, Pébusque MJ, Vaccaro MI, Velasco G, Dagorn JC, Iovanna JL., Free PMC Article

    01/21/2010
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