◀ Back to NOTCH4
CEBPZ — NOTCH4
Text-mined interactions from Literome
Furriols et al., Curr Biol 2001
:
It has been proposed that in the absence of
Notch , Su ( H )
/CBF1 acts as a repressor and is converted into an activator through interactions with the Notch intracellular domain [ 1 -- 4 ]
Raafat et al., Oncogene 2004
(Mammary Neoplasms, Experimental) :
We speculate that the Notch4/Int3 ICD induced block to mammary gland development and tumorigenesis are consequences of an increasing gradient of
CBF1 dependent Notch4/Int3 signaling
Duarte et al., Mol Biol Cell 2008
:
The sJ1 form produced as a result of thrombin cleavage inhibits
Notch mediated CBF1/Suppressor of Hairless [ ( Su ( H ) ] /Lag-1 dependent transcription and induces FGF1 expression and release
Kacer et al., J Cell Physiol 2011
(Cell Transformation, Neoplastic...) :
We found that FGF1 export and expression are regulated through
Notch signaling
mediated by transcription factor
CBF1 and its partner MAML ... We suggest that the regulation of FGF1 expression and release by
CBF1 mediated Notch signaling can play an important role in tumor formation
Guha et al., Basic Res Cardiol 2011
(Neointima) :
Modulation of GSK-3ß in vSMC following ectopic expression of constitutively active GSK-3ß, siRNA knockdown and pharmacological inhibition with SB-216763 demonstrated that GSK-3ß positively regulates
Notch intracellular domain expression,
CBF-1/RBP-J? transactivation and downstream target gene mRNA levels, while concomitantly promoting vSMC proliferation and inhibiting apoptosis
Miwa et al., Angiogenesis 2013
:
BAZF interacts with
CBF1 , a transcriptional
regulator of
Notch signaling, and downregulates Notch signaling by inducing the degradation of CBF1
Dai et al., Development 2013
:
In addition, its association with
Notch- and CBF1 regulated enhancers is
promoted by
CBF1 and antagonized by activated Notch
Hsieh et al., J Virol 1997
:
As is the case for Notch1,
Notch2 interacted with the minimal repression domain of CBF1 and was
targeted to
CBF1 through the intracellular, subtransmembrane domain