Early embryonic lethality caused by targeted disruption of the TRAF-interacting protein (TRIP) gene.

@article{Park2007EarlyEL,
  title={Early embryonic lethality caused by targeted disruption of the TRAF-interacting protein (TRIP) gene.},
  author={Eui-Soon Park and Seunga Choi and Jin-man Kim and Yongsu Jeong and J. Choe and Chang-Sik Park and Yongwon Choi and J. Rho},
  journal={Biochemical and biophysical research communications},
  year={2007},
  volume={363 4},
  pages={
          971-7
        }
}
Tumor necrosis factor receptor (TNFR)-associated factors (TRAFs) are key adaptor molecules in the TNFR-signaling complexes that promote a wide variety of signaling cascades including cell proliferation, activation, differentiation, and apoptosis. TRAF-interacting protein (TRIP) is required for the inhibitory regulation of TNF-induced NF-kappaB signaling via the TNFR/TRAF-signaling complexes in vitro. TRIP also directly interacts with the familial cylindromatosis tumor suppressor gene (CYLD) and… Expand
The TRAF-interacting protein (TRIP) is a regulator of keratinocyte proliferation.
TLDR
The results underline the important role of TRIP in the regulation of cell cycle progression and the tight linkage of its expression to keratinocyte proliferation. Expand
Tumor Necrosis Factor (TNF) Receptor-associated Factor (TRAF)-interacting Protein (TRIP) Negatively Regulates the TRAF2 Ubiquitin-dependent Pathway by Suppressing the TRAF2-Sphingosine 1-Phosphate (S1P) Interaction*
TLDR
It is demonstrated that TRIP is negatively involved in the TNF-induced inflammatory response through the down-regulation of proinflammatory cytokine production and functions as a negative regulator of pro inflammation by inhibiting T NF-induced NF-κB activation. Expand
- 1-TRAF-interacting protein ( TRIP ) negatively regulates the TNF receptor-associated factor 2 ( TRAF 2 ) ubiquitin-dependent pathway by suppressing the TRAF 2-sphingosine-1-phosphate ( S 1 P ) interaction * s
The signaling pathway downstream of TNF receptor (TNFR) is involved in the induction of a wide range of cellular processes, including cell proliferation, activation, differentiation and apoptosis.Expand
The role of the TRAF‐interacting protein in proliferation and differentiation
TLDR
The findings underline the tight link between TRAIP and cell proliferation and put them into a larger perspective regarding the role of TRAIP in the control of tissue homeostasis. Expand
A TRIP Back in Time to TRIP
TLDR
The role of TRIP in various signaling pathway based on recent published research is explained and it is now clear that TRAF-N domain mediates the interaction with different intracellular signaling molecules. Expand
NOPO modulates Egr-induced JNK-independent cell death in Drosophila
TLDR
It is reported that Egr elicits a caspase-mediated cell death pathway independent of JNK signaling, and NOPO, the Drosophila ortholog of TRIP encoding an E3 ubiquitin ligase, modulates Egr-induced Caspases-induced cell death through transcriptional activation of pro-apoptotic genes reaper and hid. Expand
TRIP/NOPO E3 ubiquitin ligase promotes ubiquitylation of DNA polymerase η
TLDR
A model in which TRIP/NOPO ubiquitylates Polη to positively regulate its activity in translesion synthesis is presented and it is shown that TRIP promotes hPolη localization to nuclear foci in human cells and Drosophila embryos. Expand
Dimerization of TRAF-interacting protein (TRAIP) regulates the mitotic progression.
TLDR
A co-immunoprecipitation assay indicated that the TRAIP forms homo-dimerization through theCC domain, and cells, expressing the CC domain-deleted mutant that could not form a homo -dimer, increased the mitotic index and promoted mitotic progression. Expand
The TRAF-interacting protein (TRAIP) is a novel E2F target with peak expression in mitosis
TLDR
Findings suggest that TRAIP has important functions in mitosis and tumorigenesis and the combination of cell cycle-dependent transcription of the TRAIP gene by E2F and rapid protein degradation leads to cell Cycle-dependent expression with a maximum in G2/M. Expand
Molecular cloning, expression and functional characterization of tumor necrosis factor (TNF) receptor-associated factor (TRAF)-interacting protein (TRIP) in grass carp, Ctenopharyngodon idella.
TLDR
Results indicate that TRIP might play important roles in immune defense and has the potential to be used as a anti-inflammation target in grass carp. Expand
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References

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TRAF-interacting Protein (TRIP): A Novel Component of the Tumor Necrosis Factor Receptor (TNFR)- and CD30-TRAF Signaling Complexes That Inhibits TRAF2-mediated NF-κB Activation
  • Soo Young Lee, Sang Yull Lee, Yongwon Choi
  • Biology, Medicine
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TLDR
A novel component of the receptor–TRAF signaling complex, designated TRIP (TRAf-interacting protein), which contains a RING finger motif and an extended coiled-coil domain acts as a receptor–proximal regulator that may influence signals responsible for cell activation/proliferation and cell death induced by members of the TNFR superfamily. Expand
The tumour suppressor CYLD negatively regulates NF-κB signalling by deubiquitination
TLDR
CYLD, a tumour suppressor that is mutated in familial cylindromatosis, interacts with NEMO, the regulatory subunit of IKK, strengthening the notion that ubiquitination is involved in IKK activation by TRAFs and suggesting that CYLD functions in this process. Expand
TRAF2 deficiency results in hyperactivity of certain TNFR1 signals and impairment of CD40-mediated responses.
TLDR
It is demonstrated that TRAF2-deficient macrophages produce increased amounts of nitric oxide and TNF in response to TNF stimulation, and this data demonstrate two important roles of TRAf2, one as a negative regulator of certain TNFR1 signals and the other as a positive mediator of CD40 signaling. Expand
The Tumor Suppressor CYLD Interacts with TRIP and Regulates Negatively Nuclear Factor κB Activation by Tumor Necrosis Factor
TLDR
Findings indicate that cylindromas arise through constitutive NF-κB activation leading to hyperproliferation and tumor growth. Expand
Tumor necrosis factor receptor-associated factors (TRAFs)
Tumor necrosis factor receptor-associated factors (TRAFS) were initially discovered as adaptor proteins that couple the tumor necrosis factor receptor family to signaling pathways. More recently theyExpand
Tumor necrosis factor receptor-associated factors (TRAFs)--a family of adapter proteins that regulates life and death.
TLDR
An overview of current knowledge concerning the expression and function of the recently described family of TRAF proteins, which appear to be capable of both negatively regulating apoptotic pathway(s) as well as inducing the expression of genes that promote cell survival. Expand
The TRAF Family of Signal Transducers Mediates NF-κB Activation by the TRANCE Receptor*
TLDR
The TNF receptor-associated factor (TRAF) family of signal transducers as important components of TRANCE-R-mediated NF-κB activation is identified, suggesting a role of TRAFs in regulating DC and osteoclast function. Expand
TRAF5, a novel tumor necrosis factor receptor-associated factor family protein, mediates CD40 signaling.
  • T. Ishida, T. Tojo, +5 authors J. Inoue
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1996
TLDR
The results suggest that TRAF5 and TRAF3 could be involved in both common and distinct signaling pathways emanating from CD40, which play crucial roles in B-cell function. Expand
The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins
TLDR
The biochemical purification and subsequent molecular cloning of two novel TNFR2-associated proteins, designated c-IAP1 and c- IAP2, that are closely related mammalian members of the inhibitor of apoptosis protein (IAP) family originally identified in baculoviruses are reported. Expand
CD30/TNF receptor-associated factor interaction: NF-kappa B activation and binding specificity.
TLDR
It is shown that TRAF2-mediated activation of NF-kappa B plays a role in the activation of HIV transcription induced by CD30 cross-linking and that there are two independent binding sites for TRAF, each interacting with a different domain of TRAF. Expand
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