Search results for YWHAZ

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Reaction (14 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).
Identifier: R-HSA-9614423
Species: Homo sapiens
Compartment: cytosol
Nuclear exclusion and cytoplasmic retention of AKT-phosphorylated FOXO1 is promoted by binding of FOXO1 to 14-3-3 proteins: YWHAZ (14-3-3 zeta), YWHAQ (14-3-3 theta), YWHAB (14-3-3 beta) and YWHAG (14-3-3 gamma) (Rena et al. 2001).
Identifier: R-HSA-9614564
Species: Homo sapiens
Compartment: cytosol
Nuclear exclusion and cytoplasmic retention of AKT-phosphorylated FOXO4 is promoted by binding of FOXO4 to 14-3-3 zeta (YWHAZ) (Obsilova et al. 2005, Boura et al. 2007, Silhan et al. 2009).
Identifier: R-HSA-3769391
Species: Homo sapiens
Compartment: nucleoplasm
CBY1 contains both NLS and NES sequences and continuously shuttles between the cytoplasm and the nucleus. Treatment of cells with leptomycin B (LMB), an inhibitor of XPO1-mediated nuclear export, results in nuclear accumulation of both CBY1 and 14-3-3/YWHAZ proteins (Li et al, 2008; Li et al, 2010). Consistent with this, CBY1 binds to XPO1 in an NES-dependent manner. 14-3-3/YWHAZ enhances the CBY1-XPO1 interaction, possibly by inducing a conformational change that exposes the adjacent NES sequence. Binding of 14-3-3/YWHAZ also inhibits the interaction of CBY1 with alpha-importin, additionally favouring its cytoplasmic localization. CBY1 NES mutants that are incapable of nuclear export show reduced ability to repress a beta-catenin-dependent reporter, and knockdown of endogenous CBY1 causes an accumulation of beta-catenin in the nucleus. These data support a role for CBY1 in the nuclear export of beta-catenin (Li et al, 2010). Despite growing evidence for a role for CBY1 in regulating WNT signaling, a formal requirement for CBY1 in vivo is still lacking.
Identifier: R-HSA-9614562
Species: Homo sapiens
Compartment: cytosol
Nuclear exclusion and cytoplasmic retention of AKT-phosphorylated FOXO3 is promoted by binding of FOXO3 to 14-3-3 proteins: YWHAZ (14-3-3 zeta), YWHAQ (14-3-3 theta), and SFN (14-3-3 sigma) (Brunet et al. 1999, Arimoto-Ishida et al. 2004).
Identifier: R-HSA-450620
Species: Homo sapiens
Compartment: cytosol, nucleoplasm
KSRP phosphorylated at serine193 binds 14-3-3zeta (YWHAZ) which impairs the ability of KSRP to destabilize RNA. Thus the RNAs become stabilized. KSRP is able to shuttle between the nucleus and the cytoplasm. 14-3-3zeta is nucleoplasmic. Binding of KSRP to 14-3-3zeta causes KSRP to be retained in the nucleus.
Identifier: R-HSA-5632732
Species: Homo sapiens
Compartment: cytosol
Phosphorylation of TSC2 by AKT enables association of TSC2 with 14-3-3 proteins YWHAB (14-3-3 protein beta/alpha), YWHAQ (14-3-3 protein theta), YWHAG (14-3-3 protein gamma), YWHAH (14-3-3 protein eta), YWHAE (14-3-3 protein epsilon), YWHAZ (14-3-3 protein zeta/delta) or SFN (14-3-3 protein sigma) (Liu et al. 2002). Binding to 14-3-3 proteins sequesters TSC2 to the cytosol and prevents its association with TSC1 (Cai et al. 2006).
Identifier: R-HSA-1445149
Species: Homo sapiens
Compartment: cytoplasmic vesicle membrane, cytosol
AS160 (TBC1D4) phosphorylated on serines 318, 341, 570, 588, and 751 and threonine 642 binds to all 14-3-3 proteins, although binding to 14-3-3 delta (YWHAZ) is comparatively low (Ramm et al. 2006, Howlett et al. 2007, Ngo et al. 2009, Treebak et al. 2009, Koumanov et al. 2011). As inferred from mouse, binding to 14-3-3 does not interfere with the interaction between AS160 and IRAP (LNPEP).
Identifier: R-HSA-139899
Species: Homo sapiens
Compartment: cytosol
14-3-3 proteins bind BAD phosphorylated by activated AKT on serine residue S99 (corresponds to mouse Bad serine residue S136). Binding of 14-3-3 proteins to p-S99-BAD facilitates subsequent phosphorylation of BAD on serine residue S118 (corresponds to mouse serine S155), which disrupts binding of BAD to BCL2 proteins and promotes cell survival (Datta et al. 2000). Caspase-3 mediated cleavage of 14-3-3 proteins releases BAD and promotes apoptosis (Won et al. 2003). All known 14-3-3 protein isoforms (beta/alpha i.e. YWHAB, gamma i.e. YWHAG, zeta/delta i.e. YWHAZ, epsilon i.e. YWHAE, eta i.e. YWHAH, sigma i.e. SFN and theta i.e. YWHAQ) can interact with BAD and inhibit it (Subramanian et al. 2001, Chen et al. 2005).
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