If the Prophet Does Not Come to the Mountain: Dynamics of Signaling Complexes in NF-κB Activation

Kovalenko, Andrew; Wallach, David

doi:10.1016/j.molcel.2006.05.002

Cited by 34 publications

(24 citation statements)

References 11 publications

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“…The UBDs in the TAB2/3 regulatory proteins of the TAK1 kinase complex also bind Lys-63-linked polyubiquitin chains, thus TAB2/3 is recruited to polyubiquitinated RIP on TNF-a stimulation (Kanayama et al 2004). The subsequent activation of the TAK1 complex promotes I-kK activation (Kovalenko and Wallach 2006). Lys-377 is likely the primary residue that is ubiquitinated on RIP and appears to be important for NF-kB activation, given that a Lys-377 mutation to arginine attenuates RIP ubiquitination, prevents the recruitment of TAK1 and I-kK complexes to TNFR1, and inhibits I-kK activation (Ea et al 2006).…”

Section: Tnfr1mentioning

confidence: 99%

Signaling to NF- B: Regulation by Ubiquitination

Wertz¹,

Dixit²

2009

Cold Spring Harbor Perspectives in Biology

269

241

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Section: Tnfr1mentioning

confidence: 99%

Signaling to NF- B: Regulation by Ubiquitination

Wertz¹,

Dixit²

2009

Cold Spring Harbor Perspectives in Biology

269

241

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“…An example of interest from the still small eukarytic interactome with these kinases might be the interaction of PPIP5K1 with CYLD, a probable ubiquitin carboxyl-terminal hydrolase, which is an anti-apoptotic protein. It is involved in the tumor necrosis factor (TNF) receptor driven NF-κ B signaling (Kovalenko and Wallach , 2006 ). An interaction protein of IP6K2, TRAF2 (Morrison et al , 2007 ) also participates in this anti-apoptotic signaling of TNF receptors.…”

Section: Future Researchmentioning

confidence: 99%

Synthesis and biological actions of diphosphoinositol phosphates (inositol pyrophosphates), regulators of cell homeostasis

Wundenberg

Mayr

2012

Biological Chemistry

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Diphosphoinositol phosphates are a subclass of inositol phosphates possessing one or two high energy diphosphate groups instead of phosphoester substituents of the myo -inositol. Here we describe the enzymes responsible for their synthesis and degradation and how these may be regulated. Formation of diphosphoinositol phosphates in yeast and mammals is driven by an increase of the cellular energy charge, a lack of inorganic phosphate, and in mammals by osmotic or heat stress and in some cases by receptor mediated signaling. Known cellular actions are an improvement of the cell homeostasis by a reduction of the energy charge, increased phosphate uptake, improvement of mitochondrial performance, and an increase of insulin secretion in mammals. The underlying molecular mechanisms of action are far from being clarifi ed but an increasing body of knowledge about molecular details has highlighted their complex participation in many cellular systems and metabolic processes.

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“…TRAF2 and TRAF5 are also RING domain proteins and likely function as ubiquitin ligases to promote the polyubiquitination of RIP1. The ubiquitinated RIP1 then activates TAK1 and IKK, leading to NF-kB activation (Chen, 2005;Krappmann and Scheidereit, 2005;Kovalenko and Wallach, 2006).…”

Section: Introductionmentioning

confidence: 99%

Ubiquitin-mediated activation of TAK1 and IKK

2007

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Transforming growth factor b activated kinase-1 (TAK1), a member of the mitogen-activated protein kinase kinase kinase family, has emerged as a key regulator of signal transduction cascades leading to the activation of the transcription factors nuclear factor-kappa B (NF-jB) and activator protein-1 (AP-1). Stimulation of cells with cytokines and microbial pathogens results in the activation of TAK1, which subsequently activates the I-kappa B kinase complex (IKK) and mitogen-activated protein (MAP) kinases, culminating in the activation of NF-jB and AP-1, respectively. Recent studies have shown that polyubiquitination of signalling proteins through lysine (Lys)-63-linked polyubiquitin chains plays an important role in the activation of TAK1 and IKK. Unlike Lys-48-linked polyubiquitination, which normally targets proteins for degradation by the proteasome, Lys-63-linked polyubiquitin chains act as scaffolds to assemble protein kinase complexes and mediate their activation through proteasome-independent mechanisms. The concept of ubiquitin-mediated activation of protein kinases is supported by the discoveries of ubiquitination and deubiquitination enzymes as well as ubiquitin-binding proteins that function upstream of TAK1 and IKK. Recent biochemical and genetic studies provide further insights into the mechanism and function of ubiquitin signalling and these advances will be the focus of this review.

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If the Prophet Does Not Come to the Mountain: Dynamics of Signaling Complexes in NF-κB Activation

Cited by 34 publications

References 11 publications

Signaling to NF- B: Regulation by Ubiquitination

Signaling to NF- B: Regulation by Ubiquitination

Synthesis and biological actions of diphosphoinositol phosphates (inositol pyrophosphates), regulators of cell homeostasis

Ubiquitin-mediated activation of TAK1 and IKK

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