Search results for YWHAZ

Showing 19 results out of 31

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Protein (2 results from a total of 2)

Identifier: R-HSA-206099
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: YWHAZ: P63104
Identifier: R-HSA-450469
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: YWHAZ: P63104

Complex (6 results from a total of 10)

Identifier: R-HSA-206751
Species: Homo sapiens
Compartment: cytosol
Identifier: R-NUL-9604401
Species: Mus musculus, Homo sapiens
Compartment: cytosol
Identifier: R-HSA-9604390
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-9614628
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-9614653
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-9614572
Species: Homo sapiens
Compartment: cytosol

Reaction (6 results from a total of 14)

Identifier: R-HSA-3769393
Species: Homo sapiens
Compartment: nucleoplasm
14-3-3 proteins, represented here as YWHAZ, bind directly to CBY1 after AKT-dependent phosphorylation of CBY1 serine 20. Tagged versions of beta-catenin, CBY1 and 14-3-3/YWHAZ expressed in HEK293 cells co-immunoprecipitate in a CBY1-phosphorylation dependent manner. 14-3-3/YWHAZ binding promotes sequestration of CBY1 and beta-catenin in the cytoplasm, thus antagonizing beta-catenin-dependent transcription (Li et al, 2008).
Identifier: R-HSA-9604387
Species: Homo sapiens
Compartment: cytosol
AKT1-mediated phosphorylation of NOTCH4 intracellular domain fragment NICD4 leads to binding of NICD4 to 14-3-3-zeta (YWHAZ). Binding to YWHAZ sequesters NICD4 to the cytosol, preventing its trafficking to the nucleus, and thus negatively regulates NOTCH4 signaling (Ramakrishnan et al. 2015).
Identifier: R-NUL-9604388
Species: Homo sapiens, Mus musculus
Compartment: cytosol
Recombinant human NOTCH4 intracellular domain fragment NICD4, phosphorylated by activated AKT1, binds to recombinant mouse 14-3-3-zeta (Ywhaz) (Ramakrishnan et al. 2015).
Identifier: R-HSA-3769392
Species: Homo sapiens
Compartment: cytosol, nucleoplasm
14-3-3/YWHAZ and XPO1 both contribute to the CBY1-mediated nuclear export of beta-catenin (Li et al, 2008; Li et al, 2010). The fate of the tripartite beta-catenin:CBY1:14-3-3/YWHAZ complex in the cytoplasm is unknown, although it may represent a reservoir of beta-catenin available for further signaling. CBY1 may remain associated with 14-3-3/YWHAZ in the cytoplasm, as 14-3-3/YWHAZ binding inhibits binding of alpha-importin to CBY1 (Li et al, 2010) . This suggests the presence of a phosphatase that dephosphorylates S20 on CBY1 to allow binding with alpha-importin and reimport into the nucleus.
Identifier: R-HSA-3769394
Species: Homo sapiens
Compartment: nucleoplasm
CBY1 is phosphorylated in vitro at serine 20 by AKT1 and AKT2. In vivo, this phosphorylation is required for the export of beta-catenin from the nucleus, facilitated by the binding of 14-3-3/YWHAZ proteins to the pS20 residue of CBY1 (Li et al, 2008).
Identifier: R-HSA-9604308
Species: Homo sapiens
Compartment: nuclear envelope
The cytosolic NICD4 translocates to the nucleus. Trafficking of NICD4 to the nucleus is negatively regulated by binding of NICD4 to 14-3-3-zeta (YWHAZ), which happens upon NICD4 phosphorylation by activated AKT1 (Ramakrishnan et al. 2015).

Set (2 results from a total of 2)

Identifier: R-HSA-9614627
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-9614573
Species: Homo sapiens
Compartment: cytosol

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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