JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of c-Abl in the apoptotic response to DNA damage (Q24294273)

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Tomoko Yamaguchi

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Tohru Natsume

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Yoshio Miki

Nuclear-cytoplasmic shuttling of C-ABL tyrosine kinase

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language of work or name

English

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publication date

March 2005

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published in

Nature Cell Biology

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volume

7

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page(s)

278-85

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issue

3

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cites work

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Regulation of DNA damage-induced apoptosis by the c-Abl tyrosine kinase

20 April 2017

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Interaction between protein kinase C delta and the c-Abl tyrosine kinase in the cellular response to oxidative stress

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Effects of a selective inhibitor of the Abl tyrosine kinase on the growth of Bcr-Abl positive cells

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c-Abl tyrosine kinase regulates the human Rad9 checkpoint protein in response to DNA damage

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The tyrosine kinase c-Abl regulates p73 in apoptotic response to cisplatin-induced DNA damage

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Interaction of c-Abl and p73alpha and their collaboration to induce apoptosis

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p73 is regulated by tyrosine kinase c-Abl in the apoptotic response to DNA damage

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Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)

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Suppression of apoptosis signal-regulating kinase 1-induced cell death by 14-3-3 proteins

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Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine

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14-3-3 Interacts directly with and negatively regulates pro-apoptotic Bax

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Role for Lyn tyrosine kinase as a regulator of stress-activated protein kinase activity in response to DNA damage

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Protein kinase Cdelta is responsible for constitutive and DNA damage-induced phosphorylation of Rad9

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The structural basis for 14-3-3:phosphopeptide binding specificity

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Activation of the c-Abl tyrosine kinase in the stress response to DNA-damaging agents

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Subcellular localization of Bcr, Abl, and Bcr-Abl proteins in normal and leukemic cells and correlation of expression with myeloid differentiation

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Induction of apoptosis in chronic myelogenous leukemia cells through nuclear entrapment of BCR-ABL tyrosine kinase.

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A direct nanoflow liquid chromatography-tandem mass spectrometry system for interaction proteomics

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14-3-3 proteins: active cofactors in cellular regulation by serine/threonine phosphorylation

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14-3-3 proteins: regulation of subcellular localization by molecular interference

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JNK promotes Bax translocation to mitochondria through phosphorylation of 14-3-3 proteins

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Akt inhibits the orphan nuclear receptor Nur77 and T-cell apoptosis

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Specificity of 14-3-3 isoform dimer interactions and phosphorylation

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Cleavage of 14-3-3 protein by caspase-3 facilitates bad interaction with Bcl-x(L) during apoptosis

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A JNK-Dependent Pathway Is Required for TNFα-Induced Apoptosis

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