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These results reveal a novel RTK-AKT (show AKT1 Proteins)-p300 (show EP300 Proteins)-ADA3 signaling pathway involved in growth factor-induced cell cycle progression.
PCAF (show KAT2B Proteins) and ADA3 transcriptionally regulate PACS1 and PACS1 is a key regulator of BAX (show BAX Proteins)/BAK (show BAK1 Proteins) oligomerization and the intrinsic (mitochondrial) pathway to apoptosis.
ADA3 overexpression enhances cell proliferation that is associated with increased expression of c-MYC (show MYC Proteins). Expression patterns with respect to ADA3/c-MYC (show MYC Proteins) can divide patients into four significantly different subgroups, with c-MYC (show MYC Proteins) High and ADA3 Low status independently predicting poor survival in patients.
review on hADA3 with a comprehensive outlook on the molecular and functional roles of hADA3
Findings demonstrate that acetylation of ADA3 by its associated histone acetyltransferases is essential for its key role in histone acetylation and cell cycle progression.
results thus demonstrate that the catalytic activity of GCN5 (show KAT2A Proteins) is stimulated by subunits of the ADA2a (show TADA2A Proteins)- or ADA2b (show TADA2B Proteins)-containing HAT (show MGEA5 Proteins) modules and is further increased by incorporation of the distinct HAT (show MGEA5 Proteins) modules in the ATAC (show XCL1 Proteins) or SAGA holo-complexes
PCAF (show KAT2B Proteins) and ADA3 regulate Bid (show BID Proteins) processing via PACS2 (show PACS2 Proteins), to modulate the mitochondrial cell death pathway in response to hGrzB.
Cytoplasmic localization of alteration/deficiency in activation 3 (ADA3) predicts poor clinical outcome in breast cancer patients.
Expression of the interacting proteins altered expression of an hADA3-regulated reporter gene, suggesting functional consequences for the interactions.
a critical role of Ada3 in embryogenesis and cell cycle progression as an essential component of HAT complex.
demonstrate a novel ADA3 interaction with CENP-B (show CENPB Proteins)-centromere that may account for its previously known function in mitosis
The loss of Ada3 led to enhanced chromosomal aberrations, such as chromosome breaks, fragments, deletions and translocations, which further increased upon DNA damage.
Many DNA-binding transcriptional activator proteins enhance the initiation rate of RNA polymerase II-mediated gene transcription by interacting functionally with the general transcription machinery bound at the basal promoter. Adaptor proteins are usually required for this activation, possibly to acetylate and destabilize nucleosomes, thereby relieving chromatin constraints at the promoter. The protein encoded by this gene is a transcriptional activator adaptor and has been found to be part of the PCAF histone acetylase complex. In addition, it associates with the tumor suppressor protein p53 and is required for full activity of p53 and p53-mediated apoptosis. At least four alternatively spliced variants have been found for this gene, but the full-length nature of some variants has not been determined.
, ADA3-like protein
, transcriptional adapter 3
, transcriptional adaptor 3
, transcriptional adapter 3-like
, ADA3 homolog B
, ADA3-like protein B
, Transcriptional adapter 3-like B
, transcriptional adapter 3-B