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PAXIP1 and 53BP1 protein levels followed gene expression results, i.e., are intrinsically correlated, and also reduced in more advanced breast cancer tumors.
PAXIP1 is involved in sensitizing lung cancer cells to the WEE1 inhibitor AZD1775 in combination with platinum-based treatment.
PTIP promotes double-strand break repair through a direct role in homologous recombination.
PPM1B can dephosphorylate the Pax2 activation domain and displace the adaptor protein PTIP, thus inhibiting H3K4 methylation and gene activation.
uncovered a nuclease, Artemis, as a PTIP-binding protein
PITX2 and PTIP co-occupy the promoter of the PITX2's transcriptional target.
Polyglutamine expansion AR sequesters PTIP to attenuate DNA repair and increase genomic instability.
a new clue to identify the role of PTIP in DNA damage pathway
PTIP controls expression of PPARgamma and C/EBPalpha, the two principal adipogenic transcription factors, and is therefore required for adipogenesis.
PTIP (PAXIP1) is a strong inhibitor of the trans-activation activities of Pax2A and Pax2B on the glucagon gene promoter and p8 binding to PTIP prevents inhibition of this promoter.
identified tandem BRCT (BRCA1 carboxyl-terminal) domains in PTIP and in BRCA1 as phosphoserine- or phosphothreonine-specific binding modules that recognize substrates phosphorylated by the kinases ATM and ATR in response to gamma-irradiation
hPTIP (PAXIP1) shows increased association with 53BP1 in response to ionizing radiation but not in response to other DNA-damaging agents.
Determination of a single ATM-phosphorylated residue in 53BP1--Ser25--that is required for binding of 53BP1 to hPTIP.
PTIP depletion from mammalian cells by RNAi reduced PCNA ubiquitination in response to DNA damage, and also decreased the recruitment to chromatin of polymerase eta and the recombination protein Rad51
subset of PTIP.PA1 complex is recruited to DNA damage sites via the RNF8-dependent pathway and is required for cell survival in response to DNA damage.
PTIP regulates 53BP1-dependent signaling pathway following DNA damage
Without DNA damage agent treatment, endogenous PTIP associates with MLL3- and MLL4-containing histone H3 K4 methyltransferase complex that also contains ASH2L, RBBP5, WDR5, hDPY-30, NCOA6, PA1 and JmjC domain-containing putative histone demethylase UTX.
Immunodepletion of PTIP/Swift from Xenopus extracts prevented efficient proliferating cell nuclear antigen ubiquitination and polymerase eta recruitment to chromatin during replicative stress
PTIP as an epigenetic regulator of osteoclastogenesis.
The role for PTIP in promoting sterile transcription at the Igh locus.
a PTIP-PA1 subcomplex functions independently from the MLL3/MLL4 complex to mediate transcription during CSR
Study concludes that 53BP1 promotes productive class switch recombination and suppresses mutagenic DNA repair through distinct phosphodependent interactions with RIF1 and PTIP.
PAXIP1 controls distinct transcriptional programs during DP differentiation necessary for Tcra locus accessibility, licensing mature thymocytes for trafficking and natural killer T cell development.
PTIP plays an important role in the DNA repair process associated with the development of mature spermatozoa.
PTIP stabilizes the Pax5 DNA interactions that promote chromatin looping and regulate transcriptional responses needed for class switch recombination.
Data show that loss of PTIP resulting in subtle changes in gene expression patterns and lower H3K4 methylation.
PTIP accumulation at double stranded breaks contributes to class switch recombination and genome stability independently of Igh switch transcription
PTIP is an essential element of the cell proliferation machinery, perhaps by functioning in the DNA repair pathways
Pax transactivation domain-interacting protein is required for the urine concentration mechanism by modulating arginine vasopressin receptor 2 and AQP2 expression in the inner medulla.
PTIP bridges DNA-binding developmental regulators to histone methyltransferase-dependent epigenetic regulation.
These and other data suggest that PTIP has multiple functions, one of which is to promote the formation of transcriptional complexes that provide specificity of developmental gene expression.
The results suggest that the maintenance of H3K4 methylation is essential and requires PTIP function during the in vitro propagation of pluripotent ES cells.
The PTIP regulates PPAR gamma and C/EBPalpha expression in mouse embryonic fibroblasts as well as during preadipocyte differentiation.
This gene is a member of the paired box (PAX) gene family and encodes a nuclear protein with six BRCT (breast cancer carboxy-terminal) domains. This protein plays a critical role in maintaining genome stability, condensation of chromatin and progression through mitosis.
PAX transcription activation domain interacting protein 1 like
, PAX-interacting protein 1
, protein encoded by CAG trinucleotide repeats
, PAX transactivation activation domain-interacting protein
, SMAD wing for transcriptional activation
, protein Swift
, PAX interacting protein 1