14-3-3 is not essential for Raf-1 function: identification of Raf-1 proteins that are biologically activated in a 14-3-3- and Ras-independent manner
about
Nuclear localization of protein kinase U-alpha is regulated by 14-3-3Phosphorylation of grb10 regulates its interaction with 14-3-3Nuclear export regulation of COP1 by 14-3-3σ in response to DNA damageDynamic changes in C-Raf phosphorylation and 14-3-3 protein binding in response to growth factor stimulation: differential roles of 14-3-3 protein binding sitesCOP9 signalosome subunit 6 stabilizes COP1, which functions as an E3 ubiquitin ligase for 14-3-3σSerine phosphorylation of Cbl induced by phorbol ester enhances its association with 14-3-3 proteins in T cells via a novel serine-rich 14-3-3-binding motifActivation-modulated association of 14-3-3 proteins with Cbl in T cellsThe RafC1 cysteine-rich domain contains multiple distinct regulatory epitopes which control Ras-dependent Raf activation14-3-3 isotypes facilitate coupling of protein kinase C-zeta to Raf-1: negative regulation by 14-3-3 phosphorylationMeaningful relationships: the regulation of the Ras/Raf/MEK/ERK pathway by protein interactionsPhosphorylation of human keratin 18 serine 33 regulates binding to 14-3-3 proteinsSerine and tyrosine phosphorylations cooperate in Raf-1, but not B-Raf activationThe strength of interaction at the Raf cysteine-rich domain is a critical determinant of response of Raf to Ras family small GTPasesInhibition of phosphatidylinositol 3-kinase activity by association with 14-3-3 proteins in T cellsDirect interaction between protein kinase C theta (PKC theta) and 14-3-3 tau in T cells: 14-3-3 overexpression results in inhibition of PKC theta translocation and functionSuppression of apoptosis signal-regulating kinase 1-induced cell death by 14-3-3 proteinsAutoregulation of the Raf-1 serine/threonine kinaseDiscovery and structural characterization of a small molecule 14-3-3 protein-protein interaction inhibitorRaf-interactome in tuning the complexity and diversity of Raf function.14-3-3zeta binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic grooveCdc37p is required for stress-induced high-osmolarity glycerol and protein kinase C mitogen-activated protein kinase pathway functionality by interaction with Hog1p and Slt2p (Mpk1p)Cell type-specific regulation of B-Raf kinase by cAMP and 14-3-3 proteins14-3-3beta is a p90 ribosomal S6 kinase (RSK) isoform 1-binding protein that negatively regulates RSK kinase activityRegulation of Raf through phosphorylation and N terminus-C terminus interaction14-3-3 Binding to Na+/H+ exchanger isoform-1 is associated with serum-dependent activation of Na+/H+ exchangeProtein phosphatases 1 and 2A promote Raf-1 activation by regulating 14-3-3 interactions14-3-3 (epsilon) interacts with the insulin-like growth factor I receptor and insulin receptor substrate I in a phosphoserine-dependent manner14-3-3 zeta negatively regulates raf-1 activity by interactions with the Raf-1 cysteine-rich domain14-3-3 proteins interact with specific MEK kinasesRegulation of Raf-1 activation and signalling by dephosphorylationDrosophila-raf acts to elaborate dorsoventral pattern in the ectoderm of developing embryosRas-induced activation of Raf-1 is dependent on tyrosine phosphorylation14-3-3 proteins interact with the insulin-like growth factor receptor but not the insulin receptor.Raf-1 kinase and exoenzyme S interact with 14-3-3zeta through a common site involving lysine 49.14-3-3gamma induces oncogenic transformation by stimulating MAP kinase and PI3K signaling.Sulfur dioxide inhibits vascular smooth muscle cell proliferation via suppressing the Erk/MAP kinase pathway mediated by cAMP/PKA signaling.Epidermal Growth Factor Receptor Cell Proliferation Signaling Pathways14-3-3 facilitates Ras-dependent Raf-1 activation in vitro and in vivo.Mammalian Raf-1 is activated by mutations that restore Raf signaling in DrosophilaPositive and negative regulation of Raf kinase activity and function by phosphorylation.
P2860
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P2860
14-3-3 is not essential for Raf-1 function: identification of Raf-1 proteins that are biologically activated in a 14-3-3- and Ras-independent manner
description
1995 nî lūn-bûn
@nan
1995 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
14-3-3 is not essential for Ra ...... -3- and Ras-independent manner
@ast
14-3-3 is not essential for Ra ...... -3- and Ras-independent manner
@en
14-3-3 is not essential for Ra ...... -3- and Ras-independent manner
@en-gb
14-3-3 is not essential for Ra ...... -3- and Ras-independent manner
@nl
type
label
14-3-3 is not essential for Ra ...... -3- and Ras-independent manner
@ast
14-3-3 is not essential for Ra ...... -3- and Ras-independent manner
@en
14-3-3 is not essential for Ra ...... -3- and Ras-independent manner
@en-gb
14-3-3 is not essential for Ra ...... -3- and Ras-independent manner
@nl
prefLabel
14-3-3 is not essential for Ra ...... -3- and Ras-independent manner
@ast
14-3-3 is not essential for Ra ...... -3- and Ras-independent manner
@en
14-3-3 is not essential for Ra ...... -3- and Ras-independent manner
@en-gb
14-3-3 is not essential for Ra ...... -3- and Ras-independent manner
@nl
P2093
P2860
P356
P1476
14-3-3 is not essential for Ra ...... -3- and Ras-independent manner
@en
P2093
D K Morrison
J R Fabian
K D Mathes
N R Michaud
P2860
P304
P356
10.1128/MCB.15.6.3390
P407
P577
1995-06-01T00:00:00Z