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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.
The protease activities of JMJD5 and JMJD7 (show JMJD7 Antibodies) represent a mechanism for removal of histone tails bearing methylated arginine residues and define a potential mechanism of transcription regulation.
JMJD5 depletion increases the susceptibility of cancer cells to microtubule-destabilizing agents.
JMJD5 is a tumor suppressor gene in HCC (show FAM126A Antibodies) pathogenesis, and the epigenetic silencing of JMJD5 promotes HCC (show FAM126A Antibodies) cell proliferation by directly down-regulating CDKN1A transcription.
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.
These results suggest that direct interaction of JMJD5 with HBx facilitates hepatitis B virus replication through the hydroxylase activity of JMJD5.
Suggest JMJD5 as a potential oncogene (show RAB1A Antibodies) in colon carcinogenesis.
results reveal that JMJD5 is a novel binding partner of p53 (show TP53 Antibodies) and it functions as a positive modulator of cell cycle and cell proliferation mainly through the repression of p53 (show TP53 Antibodies) pathway.
we provide genetic and biochemical evidence that the JMJD5/CDKN1A (p21 (show CDKN1A Antibodies)) axis is essential to maintaining the short G1 phase which is critical for pluripotency in human embryonic stem cells
RCCD1 and KDM8 form a histone demethylase (show MBD2 Antibodies) complex.
Jmjd5 is involved in the transcriptional regulation of a subset of p53 (show TP53 Antibodies)-regulated genes, possibly through the control of p53 (show TP53 Antibodies) recruitment at the gene loci.
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.
Collectively, these data indicate that JMJD5 is essential during embryonal development and a repressor of p53 (show TP53 Antibodies) expression. The latter suggests that JMJD5 has oncogenic activity and accordingly JMJD5 is upregulated in leukemias and breast cancer.
Results suggest that Jmjd5 physiologically moderates embryonic cell proliferation through the epigenetic control of Cdkn1a (show CDKN1A Antibodies) expression.
This gene likely encodes a histone lysine demethylase. Studies of a similar protein in mouse indicate a potential role for this protein as a tumor suppressor. Alternatively spliced transcript variants have been described.
jumonji domain containing 5
, JmjC domain-containing protein 5
, Jumonji domain-containing protein 5
, lysine-specific demethylase 8
, jmjC domain-containing protein 5
, jumonji domain-containing protein 5