JMJD5 inhibits lung cancer progression by facilitating EGFR proteasomal degradation. | JMJD5 inhibits lung cancer progression by facilitating EGFR proteasomal degradation. Shen J, Liu G, Qi H, Xiang X, Shao J., Free PMC Article | 11/3/2023 |
Jumonji-C domain-containing protein 5 suppresses proliferation and aerobic glycolysis in pancreatic cancer cells in a c-Myc-dependent manner. | Jumonji-C domain-containing protein 5 suppresses proliferation and aerobic glycolysis in pancreatic cancer cells in a c-Myc-dependent manner. Wang H, Wang J, Liu J, Wang Y, Xia G, Huang X. | 04/30/2022 |
JMJD5 couples with CDK9 to release the paused RNA polymerase II. | JMJD5 couples with CDK9 to release the paused RNA polymerase II. Liu H, Ramachandran S, Fong N, Phang T, Lee S, Parsa P, Liu X, Harmacek L, Danhorn T, Song T, Oh S, Zhang Q, Chen Z, Zhang Q, Tu TH, Happoldt C, O'Conner B, Janknecht R, Li CY, Marrack P, Kappler J, Leach S, Zhang G., Free PMC Article | 10/31/2020 |
Downregulation of Jumonji-C domain-containing protein 5 inhibits proliferation by silibinin in the oral cancer PDTX model. | Downregulation of Jumonji-C domain-containing protein 5 inhibits proliferation by silibinin in the oral cancer PDTX model. Yang CY, Tsao CH, Hsieh CC, Lin CK, Lin CS, Li YH, Chang WC, Cheng JC, Lin GJ, Sytwu HK, Wang YL, Chen YW., Free PMC Article | 09/19/2020 |
Recognition between JMJD5/JMJD7 and histone substrates is specific, which is reflected by the binding data between enzymes and substrates. High structural similarity between JMJD5 and JMJD7 is reflected by the shared common substrates and high binding affinity. | Specific Recognition of Arginine Methylated Histone Tails by JMJD5 and JMJD7. Liu H, Wang C, Lee S, Ning F, Wang Y, Zhang Q, Chen Z, Zang J, Nix J, Dai S, Marrack P, Hagman J, Kappler J, Zhang G., Free PMC Article | 09/28/2019 |
JMJD5 expression is increased in oral squamous cell carcinoma tissue samples and tumor cell lines. | Down-regulation of JMJD5 suppresses metastasis and induces apoptosis in oral squamous cell carcinoma by regulating p53/NF-κB pathway. Yao Y, Zhou WY, He RX. | 04/6/2019 |
KDM8/JMJD5exhibits a novel property as a dual coactivator of AR and PKM2 and as such, it is a potent inducer of castration and therapy resistance.Its oncogenic properties in prostate cancer come from its direct interaction with AR to affect androgen response and with PKM2 to regulate tumor metabolism. | KDM8/JMJD5 as a dual coactivator of AR and PKM2 integrates AR/EZH2 network and tumor metabolism in CRPC. Wang HJ, Pochampalli M, Wang LY, Zou JX, Li PS, Hsu SC, Wang BJ, Huang SH, Yang P, Yang JC, Chu CY, Hsieh CL, Sung SY, Li CF, Tepper CG, Ann DK, Gao AC, Evans CP, Izumiya Y, Chuu CP, Wang WC, Chen HW, Kung HJ., Free PMC Article | 03/16/2019 |
JMJD5 catalyzes stereoselective C-3 hydroxylation of arginine residues in sequences from human RCCD1 and ribosomal protein S6. | JMJD5 is a human arginyl C-3 hydroxylase. Wilkins SE, Islam MS, Gannon JM, Markolovic S, Hopkinson RJ, Ge W, Schofield CJ, Chowdhury R., Free PMC Article | 12/22/2018 |
Here, we report that JMJD5, a Jumonji C (JmjC) domain-containing protein, is a Cathepsin L-type protease that mediates histone H3 N-tail proteolytic cleavage under stress conditions that cause a DNA damage response. | JMJD5 cleaves monomethylated histone H3 N-tail under DNA damaging stress. Shen J, Xiang X, Chen L, Wang H, Wu L, Sun Y, Ma L, Gu X, Liu H, Wang L, Yu YN, Shao J, Huang C, Chin YE., Free PMC Article | 08/4/2018 |
The protease activities of JMJD5 and JMJD7 represent a mechanism for removal of histone tails bearing methylated arginine residues and define a potential mechanism of transcription regulation. | Clipping of arginine-methylated histone tails by JMJD5 and JMJD7. Liu H, Wang C, Lee S, Deng Y, Wither M, Oh S, Ning F, Dege C, Zhang Q, Liu X, Johnson AM, Zang J, Chen Z, Janknecht R, Hansen K, Marrack P, Li CY, Kappler JW, Hagman J, Zhang G., Free PMC Article | 06/30/2018 |
JMJD5 depletion increases the susceptibility of cancer cells to microtubule-destabilizing agents. | Depletion of JMJD5 sensitizes tumor cells to microtubule-destabilizing agents by altering microtubule stability. Wu J, He Z, Wang DL, Sun FL., Free PMC Article | 06/24/2017 |
JMJD5 is a tumor suppressor gene in HCC pathogenesis, and the epigenetic silencing of JMJD5 promotes HCC cell proliferation by directly down-regulating CDKN1A transcription. | Epigenetic silencing of JMJD5 promotes the proliferation of hepatocellular carcinoma cells by down-regulating the transcription of CDKN1A 686. Wu BH, Chen H, Cai CM, Fang JZ, Wu CC, Huang LY, Wang L, Han ZG., Free PMC Article | 01/28/2017 |
Data suggest that JMJD5 partially accumulates on mitotic spindles during mitosis; depletion of JMJD5 results in significant mitotic arrest, spindle assembly defects, and sustained activation of spindle assembly checkpoint. | JMJD5 (Jumonji Domain-containing 5) Associates with Spindle Microtubules and Is Required for Proper Mitosis. He Z, Wu J, Su X, Zhang Y, Pan L, Wei H, Fang Q, Li H, Wang DL, Sun FL., Free PMC Article | 08/6/2016 |
These results suggest that direct interaction of JMJD5 with HBx facilitates hepatitis B virus replication through the hydroxylase activity of JMJD5. | Hepatocyte Factor JMJD5 Regulates Hepatitis B Virus Replication through Interaction with HBx. Kouwaki T, Okamoto T, Ito A, Sugiyama Y, Yamashita K, Suzuki T, Kusakabe S, Hirano J, Fukuhara T, Yamashita A, Saito K, Okuzaki D, Watashi K, Sugiyama M, Yoshio S, Standley DM, Kanto T, Mizokami M, Moriishi K, Matsuura Y., Free PMC Article | 07/30/2016 |
Suggest JMJD5 as a potential oncogene in colon carcinogenesis. | JMJD5 is a potential oncogene for colon carcinogenesis. Zhang R, Huang Q, Li Y, Song Y, Li Y., Free PMC Article | 05/21/2016 |
results reveal that JMJD5 is a novel binding partner of p53 and it functions as a positive modulator of cell cycle and cell proliferation mainly through the repression of p53 pathway. | JMJD5 interacts with p53 and negatively regulates p53 function in control of cell cycle and proliferation. Huang X, Zhang S, Qi H, Wang Z, Chen HW, Shao J, Shen J. | 12/5/2015 |
we provide genetic and biochemical evidence that the JMJD5/CDKN1A (p21) axis is essential to maintaining the short G1 phase which is critical for pluripotency in human embryonic stem cells | JMJD5 regulates cell cycle and pluripotency in human embryonic stem cells. Zhu H, Hu S, Baker J. | 10/10/2015 |
RCCD1 and KDM8 form a histone demethylase complex. | Human-chromatin-related protein interactions identify a demethylase complex required for chromosome segregation. Marcon E, Ni Z, Pu S, Turinsky AL, Trimble SS, Olsen JB, Silverman-Gavrila R, Silverman-Gavrila L, Phanse S, Guo H, Zhong G, Guo X, Young P, Bailey S, Roudeva D, Zhao D, Hewel J, Li J, Gräslund S, Paduch M, Kossiakoff AA, Lupien M, Emili A, Wodak SJ, Greenblatt J. | 08/29/2015 |
These results reveal that the N-terminal domain is essential for the nuclear localization of JMJD5 and its normal enzymatic function towards substrates in the nucleus | Identification and functional implication of nuclear localization signals in the N-terminal domain of JMJD5. Huang X, Zhang L, Qi H, Shao J, Shen J. | 05/17/2014 |
Comparison of the structure of JMJD5 with that of FIH, a well characterized protein hydroxylase, reveals that human JMJD5 might function as a protein hydroxylase. | Structure of the JmjC-domain-containing protein JMJD5. Wang H, Zhou X, Wu M, Wang C, Zhang X, Tao Y, Chen N, Zang J. | 05/3/2014 |
JMJD5 has a role in regulating PKM2 nuclear translocation and reprogramming HIF-1alpha-mediated glucose metabolism | JMJD5 regulates PKM2 nuclear translocation and reprograms HIF-1α-mediated glucose metabolism. Wang HJ, Hsieh YJ, Cheng WC, Lin CP, Lin YS, Yang SF, Chen CC, Izumiya Y, Yu JS, Kung HJ, Wang WC., Free PMC Article | 03/15/2014 |
The study reports high-resolution crystal structures of the human JMJD5 catalytic domain in complex with the substrate 2-oxoglutarate (2-OG) and the inhibitor N-oxalylglycine (NOG). | Crystal structure and functional analysis of JMJD5 indicate an alternate specificity and function. Del Rizzo PA, Krishnan S, Trievel RC., Free PMC Article | 12/8/2012 |
JMJD5 is a post-translational co-repressor for NFATc1 that attenuates osteoclastogenesis. | JMJD5, a Jumonji C (JmjC) domain-containing protein, negatively regulates osteoclastogenesis by facilitating NFATc1 protein degradation. Youn MY, Yokoyama A, Fujiyama-Nakamura S, Ohtake F, Minehata K, Yasuda H, Suzuki T, Kato S, Imai Y., Free PMC Article | 06/23/2012 |
Data show that both Arabidopsis jmjd5 mutant seedlings and mammalian cell cultures deficient for the human ortholog of this gene have similar fast-running circadian oscillations compared with WT. | Jumonji domain protein JMJD5 functions in both the plant and human circadian systems. Jones MA, Covington MF, DiTacchio L, Vollmers C, Panda S, Harmer SL., Free PMC Article | 05/14/2011 |
show that JMJD5 (now renamed KDM8), demethylates H3K36me2 and is required for cell cycle progression. | KDM8, a H3K36me2 histone demethylase that acts in the cyclin A1 coding region to regulate cancer cell proliferation. Hsia DA, Tepper CG, Pochampalli MR, Hsia EY, Izumiya C, Huerta SB, Wright ME, Chen HW, Kung HJ, Izumiya Y., Free PMC Article | 07/5/2010 |