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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Receptor-interacting serine-threonine kinase 3

RIP3, M-RIP, p116Rip, RIPK3, myosin phosphatase-Rho interacting protein
The product of this gene is a member of the receptor-interacting protein (RIP) family of serine/threonine protein kinases, and contains a C-terminal domain unique from other RIP family members. The encoded protein is predominantly localized to the cytoplasm, and can undergo nucleocytoplasmic shuttling dependent on novel nuclear localization and export signals. It is a component of the tumor necrosis factor (TNF) receptor-I signaling complex, and can induce apoptosis and weakly activate the NF-kappaB transcription factor. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: PrP, CAN, caspase-8, V1a, HAD
Papers using RIP3 antibodies
In TNF-stimulated cells, RIPK1 promotes cell survival by stabilizing TRAF2 and cIAP1, which limits induction of non-canonical NF-{kappa}B and activation of caspase-8
Vanden Berghe T et al., In Cell Death & Disease, 2010
... (1G12, Alexis, Enzo Life Sciences, Zandhoven, Belgium); anti-RIP1 (610459, BD Biosciences, Franklin Lakes, NJ, USA); anti-RIP3 (R4277, Sigma Aldrich); rabbit polyclonal antibody against ...
Papers on RIP3
Regulation of RIPK3 and RHIM-dependent necroptosis by the proteasome.
Chan et al., United States. In J Biol Chem, Feb 2016
UNASSIGNED: Receptor interacting protein kinase 3 (RIPK3) is a serine/threonine kinase with essential function in necroptosis.
Increased hepatic receptor interacting protein kinase 3 expression due to impaired proteasomal functions contributes to alcohol-induced steatosis and liver injury.
Ding et al., Guangzhou, China. In Oncotarget, Feb 2016
In the present study, we demonstrated that chronic alcohol feeding plus binge (Gao-binge) increased RIP3 but not RIP1 protein levels in mouse livers.
CaMKII is a RIP3 substrate mediating ischemia- and oxidative stress-induced myocardial necroptosis.
Xiao et al., Beijing, China. In Nat Med, Feb 2016
Here we show that receptor-interacting protein 3 (RIP3) triggers myocardial necroptosis, in addition to apoptosis and inflammation, through activation of Ca(2+)-calmodulin-dependent protein kinase (CaMKII) rather than through the well-established RIP3 partners RIP1 and MLKL.
Functional Comparison of the Molluscum Contagiosum Virus vFLIP MC159 with the Murine Cytomegalovirus M36/vICA and M45/vIRA Proteins.
Brune et al., Hamburg, Germany. In J Virol, Jan 2016
M36 encodes a viral inhibitor of caspase-8-induced apoptosis (vICA) and M45 a viral inhibitor of RIP activation (vIRA), which inhibits RIP1/RIP3-mediated necroptosis.
HSP90 activity is required for MLKL oligomerisation and membrane translocation and the induction of necroptotic cell death.
Murphy et al., Australia. In Cell Death Dis, Dec 2015
The pseudokinase, Mixed Lineage Kinase Domain-Like (MLKL), is the most terminal known obligatory effector in the necroptosis pathway, and is activated following phosphorylation by Receptor Interacting Protein Kinase-3 (RIPK3).
New insights into the regulation of innate immunity by caspase-8.
Vince et al., Brisbane, Australia. In Arthritis Res Ther, Dec 2015
In a recent article in Arthritis Research & Therapy, Cuda et al. report that myeloid cell-restricted caspase-8 loss leads to a very mild RIPK3-dependent inflammatory phenotype.
The diverse role of RIP kinases in necroptosis and inflammation.
Gerlic et al., Australia. In Nat Immunol, Jul 2015
Necroptosis was originally defined as being dependent on the kinase RIPK1 but is now known to be dependent on RIPK3 and the pseudo-kinase MLKL.
The ubiquitin-modifying enzyme A20 restricts ubiquitination of the kinase RIPK3 and protects cells from necroptosis.
Ma et al., San Francisco, United States. In Nat Immunol, Jun 2015
We found that A20-deficient T cells and fibroblasts were susceptible to caspase-independent and kinase RIPK3-dependent necroptosis.
Caspase-8 functions as a key mediator of inflammation and pro-IL-1β processing via both canonical and non-canonical pathways.
Bryant et al., Cambridge, United Kingdom. In Immunol Rev, May 2015
Activated caspase-8 can drive classical caspase-dependent apoptosis and actively inhibits cell death mediated by RIPK3-driven necroptosis.
A20 restricts ubiquitination of pro-interleukin-1β protein complexes and suppresses NLRP3 inflammasome activity.
Ma et al., San Francisco, United States. In Immunity, Feb 2015
The kinase RIPK3, but not the adaptor MyD88, is required for this response.
Necroptosis and its role in inflammation.
Vandenabeele et al., Köln, Germany. In Nature, Feb 2015
Necroptosis is a newly discovered pathway of regulated necrosis that requires the proteins RIPK3 and MLKL and is induced by death receptors, interferons, toll-like receptors, intracellular RNA and DNA sensors, and probably other mediators.
Necrostatin-1 reduces intestinal inflammation and colitis-associated tumorigenesis in mice.
Chen et al., Xi'an, China. In Am J Cancer Res, 2014
Necrostatin-1 (Nec-1), known as a specific inhibitor of necroptosis, through preventing the receptor-interacting protein (RIP) 1 and RIP3 interaction.
Cell Death Signaling.
Llambi et al., Memphis, United States. In Cold Spring Harb Perspect Biol, 2014
This form of cell death can result from active signaling pathways, the best characterized of which is dependent on the activity of the protein kinase RIP3.
Necroptotic Cell Death Signaling and Execution Pathway: Lessons from Knockout Mice.
Enns et al., São Paulo, Brazil. In Mediators Inflamm, 2014
Caspase-8 has a critical role in pro- and antinecrotic signaling pathways leading to the activation of receptor interacting protein kinase 1 (RIPK1), RIPK3, and the mixed kinase domain-like (MLKL) for a convergent execution pathway of necroptosis or regulated necrosis.
Programmed necrosis and necroptosis - molecular mechanisms.
Chorostowska-Wynimko et al., Warsaw, Poland. In Postepy Hig Med Dosw (online), 2014
The role of RIP1 and RIP3 kinases in this process is presented, as well as the diverse pathways induced by ligation of tumor necrosis factor α, to its receptor, TNFR1, i.e. cell survival, apoptosis or necroptosis.
The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis.
Wu et al., New York City, United States. In Cell, 2012
Study shows that RIP1 and RIP3 form an amyloid structure through their RIP homotypic interaction motifs and that this heterodimeric amyloid structure is a functional signaling complex that mediates programmed necrosis.
Mixed lineage kinase domain-like is a key receptor interacting protein 3 downstream component of TNF-induced necrosis.
Liu et al., Bethesda, United States. In Proc Natl Acad Sci U S A, 2012
study suggests that MLKL is a key RIP3 downstream component of TNF-induced necrotic cell death
DAI/ZBP1/DLM-1 complexes with RIP3 to mediate virus-induced programmed necrosis that is targeted by murine cytomegalovirus vIRA.
Mocarski et al., Atlanta, United States. In Cell Host Microbe, 2012
DAI interacts with RIP3 to mediate virus-induced necrosis analogous to the RIP1-RIP3 complex controlling death receptor-induced necroptosis.
Association of syntenin-1 with M-RIP polarizes Rac-1 activation during chemotaxis and immune interactions.
Yáñez-Mó et al., Madrid, Spain. In J Cell Sci, 2012
Our data identify M-RIP as a crucial local regulator of the Rho-Rac balance during chemotaxis and antigen recognition.
Inhibitor of apoptosis proteins limit RIP3 kinase-dependent interleukin-1 activation.
Tschopp et al., Lausanne, Switzerland. In Immunity, 2012
activation of the cell death-inducing ripoptosome platform and RIP3 can generate bioactive IL-1beta
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