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The above findings suggest that USP39 plays a vital oncogenic role in the tumorigenesis of prostate cancer
Knockdown of USP39 expression in osteosarcoma cell line U2OS cell significantly decreased cell proliferation, impaired colony formation ability. A further analysis indicated suppression of USP39 arrested cell cycle progression at G2/M phase via p21 (Montrer CDKN1A Protéines) dependent way. In addition, the results of Annexin V (Montrer ANXA5 Protéines)/7-AAD staining suggested the knockdown of USP39 could promote U2OS cell apoptosis through PARP cleavage.
Data suggest that ZIP (Montrer DAPK3 Protéines), USP39, Prp24/p100/SART3, and Prp43 (Montrer DHX15 Protéines) associate to form complex instrumental in spliceosome assembly; ZIP (Montrer DAPK3 Protéines) regulates pre-mRNA splicing of USP39 independent of RNA binding; stable 35S tri (Montrer VANGL2 Protéines)-snRNP (Montrer LSM2 Protéines) particles are enriched in Cajal body. (ZIP (Montrer DAPK3 Protéines) = zinc finger and G-patch domain-containing protein (Montrer ZGPAT Protéines); SART3 (Montrer SART3 Protéines) = squamous cell carcinoma antigen recognised by T cells 3 (Montrer SART3 Protéines); Prp43 (Montrer DHX15 Protéines) = RNA helicase Prp43 (Montrer DHX15 Protéines))
High USP39 expression is associated with colon and lung cancer.
Data show that knockdown of ubiquitin specific peptidase 39 (USP39), a direct target of microRNA microRNA-133a, induced cell apoptosis through inhibition of proto-oncogene (Montrer RAB1A Protéines) proteins c-akt (AKT (Montrer AKT1 Protéines)) signaling pathway in pancreatic cancer (PC) cells.
Results show a significantly higher expression of USP39 in colorectal cancer tissues and cell lines and provide evidence that USP39 protein plays an important role in the growth and metastasis of colorectal cancer mainly through Wnt (Montrer WNT2 Protéines)/beta-catenin (Montrer CTNNB1 Protéines) pathway.
shRNA-mediated knockdown of USP39 inhibited the growth and colony formation ability of GC cells. suppression of USP39 induced G2/M-phase arrest and increased the cleavage of PARP (Asp214).
USP39 is upregulated in melanoma tissues and that it is implicated in melanoma progression by regulating cell cycle and apoptosis via ERK1/2 signal pathways.
study indicates that USP39 may be functionally involved in lung cancer growth and act as a potential molecular target for human lung cancer diagnosis and treatment.
Our data indicate that USP39 knockdown inhibited the growth of HCC (Montrer FAM126A Protéines) both in vitro and in vivo through G2/M arrest, which was partly achieved via the inhibition of FoxM1 (Montrer FOXM1 Protéines) splicing.
High expression of ubiquitin-specific peptidase 39 is associated with the development of vascular remodeling.
Zebrafish usp39 (Montrer USP37 Protéines) regulates embryonic pituitary homeostasis by targeting rb1 (Montrer RB1 Protéines) and e2f4 (Montrer E2F4 Protéines) expression, respectively, contributing to increased adenohypophyseal sensitivity to these altered cell cycle regulators
May play a role in mRNA splicing. It is unsure if the protein really exhibits hydrolase activity. Could be a competitor of ubiquitin C-terminal hydrolases (UCHs).
, SnRNP assembly defective 1 homolog
, U4/U6.U5 tri-snRNP-associated 65 kDa protein
, U4/U6.U5 tri-snRNP-associated protein 2
, inactive ubiquitin-specific peptidase 39
, small nuclear ribonucleoprotein 65kDa (U4/U6.U5)
, ubiquitin specific protease 39
, ubiquitin specific peptidase 39
, U4/U6.U5 tri-snRNP-associated protein 2-like
, u4/U6.U5 tri-snRNP-associated protein 2-like