Search results for YWHAZ

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Pathway (3 results from a total of 3)

Identifier: R-HSA-450604
Species: Homo sapiens
Compartment: cytosol, nucleoplasm
KSRP binds to AU-rich sequences in the 3' untranslated regions of mRNAs. KSRP causes the bound mRNA to be targeted for hydrolysis by recruiting exonucleases and decapping enzymes. The activity of KSRP is regulated by phosphorylation. Protein kinase B/Akt phosphorylates KSRP at serine193. The phosphorylation inhibits the ability of KSRP to destabilize mRNA. KSRP phosphorylated at serine193 binds 14-3-3zeta (YWHAZ) which causes KSRP to be retained in the nucleus.
Identifier: R-HSA-3769402
Species: Homo sapiens
The mechanisms involved in downregulation of TCF-dependent transcription are not yet very well understood. beta-catenin is known to recruit a number of transcriptional repressors, including Reptin, SMRT and NCoR, to the TCF/LEF complex, allowing the transition from activation to repression (Bauer et al, 2000; Weiske et al, 2007; Song and Gelmann, 2008). CTNNBIP1 (also known as ICAT) and Chibby are inhibitors of TCF-dependent signaling that function by binding directly to beta-catenin and preventing interactions with critical components of the transactivation machinery (Takemaru et al, 2003; Li et al, 2008; Tago et al, 2000; Graham et al, 2002; Daniels and Weiss, 2002). Chibby additionally promotes the nuclear export of beta-catenin in conjunction with 14-3-3/YWHAZ proteins (Takemura et al, 2003; Li et al, 2008). A couple of recent studies have also suggested a role for nuclear APC in the disassembly of the beta-catenin activation complex (Hamada and Bienz, 2004; Sierra et al, 2006). It is worth noting that while some of the players involved in the disassembly of the beta-catenin transactivating complex are beginning to be worked out in vitro, the significance of their role in vivo is not yet fully understood, and some can be knocked out with little effect on endogenous WNT signaling (see for instance Voronina et al, 2009).
Identifier: R-HSA-9604323
Species: Homo sapiens
NOTCH4 signaling can be negatively regulated at the level of nuclear translocation of the NOTCH4 intracellular domain fragment (NICD4). AKT-mediated phosphorylation of NICD4 promotes binding of NICD4 with 14-3-3-zeta (YWHAZ), leading to retention of NICD4 in the cytosol (Ramakrishnan et al. 2015).

The E3 ubiquitin ligase FBXW7, a component of the SCF ubiquitin ligase complex, binds to and ubiquitinates phosphorylated NICD4, targeting it for proteasome-mediated degradation (Wu et al. 2001). The level of NICD4 is significantly increased in Fbxw7 knockout mouse embryos, which die in utero and have impaired development of the vascular system (Tsunematsu et al. 2004).

Binding of NOTCH4 to ELOC (elongin C) is involved in proteasome-mediated degradation of NOTCH4, but the exact mechanism has not been elucidated (Cummins et al. 2011). MDM2, a TP53-induced ubiquitin ligase, was reported to ubiquitinate NICD4 and target it for degradation in response to TP53 activation (Sun et al. 2011).

NOTCH4 signaling is inhibited by binding of NICD4 to the transforming acidic coiled-coil protein-3, but he mechanism is not known (Bargo et al. 2010).
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