Notch interferes with the scaffold function of JNK-interacting protein 1 to inhibit the JNK signaling pathway

Kim, Jin Woo; Kim, Myung Jin; Kim, Kwang Je; Hu, Yun; Chae, Ji Soo; Hwang, Sang Gil; Chang, Tong Shin; Park, Hee Sae; Lee, Kang Woo; Han, Pyung Lim; Cho, Ssang-Goo; Kim, Tae Wan; Choi, Eui Ju

doi:10.1073/pnas.0501600102

Cited by 64 publications

(73 citation statements)

References 51 publications

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“…Cross-talk between different signaling pathways is a common phenomenon. APP and Notch signaling pathways interact at various points, including direct interactions of Notch and APP (15,40) or competition for binding proteins such as Fe65, Jip1 or Numb, which can physically associate with AICD and NICD (16,19,49). A recent report showed that NICD can repress AFT-mediated transcription by direct interaction (21).…”

Section: Discussionmentioning

confidence: 99%

“…Both proteins undergo ectodomain shedding by the same α-secretases and regulated intramembrane proteolysis by γ-secretase complexes (13,29) leading to competition for these proteolytic cleavages (2) that are necessary for the translocation of the intracellular domains to the nucleus (N). Several adaptor proteins such as Fe65, Jip1 or numb can physically associate with AICD or NICD (3), thereby influencing their capacity of nuclear translocation and transcriptional activity (16,19,49). AICD is transported to the nucleus by Fe65 and together with Tip60 forms spherical nuclear AFT complexes (57) that represent transcription factories (TF).…”

Section: Discussionmentioning

confidence: 99%

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Co-localization of the amyloid precursor protein and Notch intracellular domains in nuclear transcription factories

Konietzko¹,

Goodger²,

Meyer³

et al. 2010

Neurobiology of Aging

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The β-amyloid precursor protein (APP) plays a major role in Alzheimer's disease. The APP intracellular domain (AICD), together with Fe65 and Tip60, localizes to spherical nuclear AFT complexes that might represent sites of transcription. We now show that endogenous AICD is targeted to similar nuclear spots. AFT complexes were closely associated with Cajal and PML bodies but did not localize to nucleoli or splicing speckles. Live imaging revealed that AFT complexes were highly mobile within nuclei. Following pharmacological inhibition of transcription AFT complexes merged into a few large assemblies. We have previously shown that AICD regulates the expression of its own precursor APP. Transfection of APP promoter plasmids as substrates resulted in cytosolic AFT complex formation at the labeled APP promoter plasmids. In addition, identification of chromosomal APP or KAI1 gene loci by fluorescence in situ hybridization showed their close association with nuclear AFT complexes. The transcriptional activator Notch intracellular domain (NICD) localized to the same nuclear spots as occupied by AFT complexes, suggesting that these nuclear compartments correspond to transcription factories. Fe65 and Tip60 also co-localized with APP in the neurites of primary neurons. Pre-assembled AFT complexes may serve to assist fast nuclear signaling upon endoproteolytic APP cleavage.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Co-localization of the amyloid precursor protein and Notch intracellular domains in nuclear transcription factories

Konietzko¹,

Goodger²,

Meyer³

et al. 2010

Neurobiology of Aging

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“…Several studies suggest the existence of an activity of Notch receptor that is independent of its Su(H)/CBF-mediated transcriptional activity (Matsuno et al, 1997;Ramain et al, 2001;Endo et al, 2003;Nicolas et al, 2003;Hayward et al, 2005;Kim et al, 2005;Deregowski et al, 2006). In a welldocumented instance, Notch modulates Wnt signalling (Martinez and there is some evidence that the target of this activity is the effector of Wnt signalling Armadillo/␤-catenin (Nicolas et al, 2003;Hayward et al, 2005;Deregowski et al, 2006).…”

Section: Discussionmentioning

confidence: 99%

Notch synergizes with axin to regulate the activity of armadillo in Drosophila

Hayward

Balayo

Arias

2006

Developmental Dynamics

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“…JNK-deficient mice have been shown to exhibit aberrant T cell activation and differentiation (23)(24)(25). Recently, Kim et al (26) reported that the active form of Notch1 negatively regulates the JNK pathway by antagonizing JNK-interacting protein 1-mediated activation of JNK signaling. It has also been shown earlier (23) and again demonstrated in the present experiments that T cells exposed to Ag showed significant JNK induction (Fig.…”

Section: Notch3 Inhibition Does Not Affect Jnk Signaling In Myelin-rementioning

confidence: 99%

Notch3 Inhibition in Myelin-Reactive T Cells Down-Regulates Protein Kinase Cθ and Attenuates Experimental Autoimmune Encephalomyelitis

Juryńczyk

Jurewicz

Raine

et al. 2008

The Journal of Immunology

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Among its varied functions, Notch signaling is involved in peripheral T cells responses. The activation and polarization of CD4+ T cells toward a Th1 lineage are essential steps in the pathogenesis of multiple sclerosis and its animal model, experimental autoimmune encephalomyelitis. Inhibition of all four Notch receptors with a γ-secretase inhibitor was shown to block Th1-type polarization and to attenuate the symptoms of experimental autoimmune encephalomyelitis. In this study, we have examined the role of individual Notch receptors in proliferation, cytokine production, and encephalitogenic potential of PLP-reactive T cells. Specific induction of Notch1 and Notch3 transcripts were noted in PLP-reactive T cells upon Ag stimulation. However, using γ-secretase inhibitor and Abs blocking distinct Notch receptors, we have found that selective inhibition of Notch3, but not Notch1, receptor abrogated proliferation, Th1- and Th17-type responses of PLP-reactive T cells. Moreover, Notch3 inhibition in T cells correlated with the down-regulated expression of protein kinase Cθ, a kinase with important regulatory function within mature T cells. Thus, selective inhibition of the Notch3 receptor may have important effects on peripheral T cell responses and may offer a new attractive target in treating autoimmune diseases, including multiple sclerosis.

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Notch interferes with the scaffold function of JNK-interacting protein 1 to inhibit the JNK signaling pathway

Abstract: scaffold ͉ apoptosis ͉ glucose deprivation

Cited by 64 publications

References 51 publications

Co-localization of the amyloid precursor protein and Notch intracellular domains in nuclear transcription factories

Co-localization of the amyloid precursor protein and Notch intracellular domains in nuclear transcription factories

Notch synergizes with axin to regulate the activity of armadillo in Drosophila

Notch3 Inhibition in Myelin-Reactive T Cells Down-Regulates Protein Kinase Cθ and Attenuates Experimental Autoimmune Encephalomyelitis

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