Erratum: ABIN-1 is a ubiquitin sensor that restricts cell death and sustains embryonic development

Turer, Emre E.; Callahan, Joseph A.; Chai, Sophia; Advincula, Rommel; Barrera, Julio; Shifrin, Nataliya; Lee, Bettina; Yen, T. S. Benedict; Woo, Tammy T.; Malynn, Barbara A.; Ma, Averil

doi:10.1038/nature07941

Cited by 15 publications

(23 citation statements)

References 1 publication

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Page 22 of 38 A c c e p t e d M a n u s c r i p t 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60 61 62 63 64 [12,47], but the specific targets still need to be identified. Moreover, it is not unlikely that the ubiquitinbinding potential of ABINs might also provide ABINs the potential to regulate endocytosis and intracellular trafficking of specific receptors and signaling proteins.…”

Section: Discussionmentioning

confidence: 99%

“…Initial evidence for this was again based on overexpression of ABIN-1, showing that it prevents TNF-induced apoptosis of hepatocytes both in vitro and in vivo [46]. Recently, these findings were confirmed with the generation of ABIN-1 deficient mice, which die during embryogenesis with fetal liver apoptosis, anemia and hypoplasia that can be rescued by additional TNF deletion [47]. The embryonic lethality of ABIN-1 deficient mice contrasts with the phenotype of A20 deficient mice that do not show any defects in embryonic development but die shortly after birth due to cachexia and severe inflammation.…”

mentioning

confidence: 93%

See 1 more Smart Citation

ABINs: A20 binding inhibitors of NF-κB and apoptosis signaling

Verstrepen¹,

Carpentier²,

Verhelst³

et al. 2009

Biochemical Pharmacology

161

126

View full text Add to dashboard Cite

ABINs have been described as three different proteins (ABIN-1, ABIN-2, that bind the ubiquitin-editing nuclear factor-B (NF-B) inhibitor protein A20 and which show limited sequence homology. Overexpression of ABINs inhibits NF-B activation by tumor necrosis factor (TNF) and several other stimuli. Similar to A20, ABIN-1 and ABIN-3 expression is NF-B dependent, implicating a potential role for the A20/ABIN complex in the

show abstract

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 93%

ABINs: A20 binding inhibitors of NF-κB and apoptosis signaling

Verstrepen¹,

Carpentier²,

Verhelst³

et al. 2009

Biochemical Pharmacology

161

126

View full text Add to dashboard Cite

show abstract

“…Furthermore, the ubiquitin-binding activity of ABIN1 is required for association with FADD and RIP1 and also for ABIN1-mediated inhibition of FADD/ caspase-8 binding. 102 Thus, it is possible that association of ABIN1 with ubiquitinated RIP1 somehow inhibits the FADD/ caspase-8 interaction. The function of ABIN1-deficient cells was evaluated in the context of TNF-a-mediated signaling pathways, thus it would also be interesting to determine whether ABIN1 inhibits Fas-induced FADD/caspase-8 binding.…”

Section: Fadd-mediated Dr Signaling: Fas/dr4/dr5mentioning

confidence: 99%

Regulation of death receptor signaling by the ubiquitin system

Wertz¹,

Dixit²

2009

Cell Death Differ

112

View full text Add to dashboard Cite

The study of death receptor (DR) signaling has led to the discovery of new signaling paradigms, including the first example of direct receptor-mediated activation of a protease (caspase-8) that functions as a second messenger to initiate a 'death cascade' of downstream protease activation. More recently, this receptor system has underscored the importance of ubiquitin modification in NF-jB activation. Both degradative lysine 48-linked polyubiquitin and scaffolding lysine 63-linked polyubiquitin have an essential role in signal propagation. Remarkably, a negative feedback process, termed ubiquitin editing, regulates signaling that emanates from certain DRs. Ubiquitin editing is mediated by a complex interplay between the ubiquitination and deubiquitination machinery, resulting in the replacement of signal enhancing lysine 63-linked polyubiquitin with signal extinguishing lysine 48-linked polyubiquitin. The ubiquitination machinery and its regulation in the context of DR signaling are discussed herein. The tumor necrosis factor receptor (TNFR) family is characterized by the presence of a variable number of cysteinerich domains within the extracellular segment and includes receptors known as the death receptors (DRs). The cognate ligands function in concert with the receptors to orchestrate immune responses, generate secondary lymphoid organs, and modulate the survival, proliferation, and differentiation of responding cells. When this axis goes awry, it can contribute to sepsis, cachexia, and autoimmune disorders including rheumatoid arthritis, inflammatory bowel disease, and psoriasis. 1,2 Indeed, therapeutics based on neutralization of tumor necrosis factor-a (TNF-a) have met unparalleled success in the treatment of many autoimmune disorders. Furthermore, there has been a recent groundswell of enthusiasm for exploiting the proapoptotic properties of the DRs for TRAIL/ Apo2 ligand that selectively mediate the demise of tumor cells.There are six TNFR family DRs identified in humans to date: Fas/CD-95, TNFR1, DR3, DR4, DR5, and DR6. They are characterized by the presence of an B80-residue motif within their cytosolic segments dubbed the death domain (DD). 1,2 The integrity of this domain is essential for engaging downstream signaling components that, depending on the cellular context, promote either prosurvival and proinflammatory signaling pathways or promote apoptosis. 1,2 The DD is sixhelical fold that adopts a 'Greek key' topology and mediates homotypic interactions. There are four death-fold motifs: the DD itself, the death effector domain (DED), caspase activation and recruitment domain (CARD), and the Pyrin domain. 3 Although these folds all possess a similar topological configuration, their surface charge is distinct such that specificity of association is dictated by electrostatic interactions. 3 The DRs initiate signaling by recruiting one of two DD-containing platform adaptor molecules: FADD (Fas Associated Death Domain) that generally mediates apoptosis and/or TRADD (TNF Receptor Associated Death Domain)...

show abstract

“…Although these data suggested a cooperative function of the two proteins in TNFR signaling, ABIN1 recently has been found to counteract TNF-α-mediated liver cell death during embryonic development, a function that is independent of A20 (ref. 20 and below). Therefore, ABIN1 and A20 may cooperate in some functions but not in others.…”

mentioning

confidence: 91%

A20-binding inhibitor of NF-κB (ABIN1) controls Toll-like receptor-mediated CCAAT/enhancer-binding protein β activation and protects from inflammatory disease

Zhou¹,

Wu²,

High

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

107

View full text Add to dashboard Cite

Toll-like receptors (TLRs) are expressed on innate immune cells and trigger inflammation upon detection of pathogens and host tissue injury. TLR-mediated proinflammatory-signaling pathways are counteracted by partially characterized anti-inflammatory mechanisms that prevent exaggerated inflammation and host tissue damage as manifested in inflammatory diseases. We biochemically identified a component of TLR-signaling pathways, A20-binding inhibitor of NF-κB (ABIN1), which recently has been linked by genome-wide association studies to the inflammatory diseases systemic lupus erythematosus and psoriasis. We generated ABIN1-deficient mice to study the function of ABIN1 in vivo and during TLR activation. Here we show that ABIN1-deficient mice develop a progressive, lupus-like inflammatory disease characterized by expansion of myeloid cells, leukocyte infiltrations in different parenchymatous organs, activated T and B lymphocytes, elevated serum Ig levels, and the appearance of autoreactive antibodies. Kidneys develop glomerulonephritis and proteinuria, reflecting tissue injury. Surprisingly, ABIN1-deficient macrophages exhibit normal regulation of major proinflammatory signaling pathways and mediators but show selective deregulation of the transcription factor CCAAT/enhancer binding protein β (C/EBPβ) and its target genes, such as colony-stimulating factor 3 ( Csf3 ) , nitric oxide synthase, inducible (Nos2 ), and S100 calcium-binding protein A8 ( S100a8 ). Their gene products, which are intimately linked to innate immune cell expansion (granulocyte colony-stimulating factor), cytotoxicity (inducible nitric oxide synthase), and host factor-derived inflammation (S100A8), may explain, at least in part, the inflammatory phenotype observed. Together, our data reveal ABIN1 as an essential anti-inflammatory component of TLR-signaling pathways that controls C/EBPβ activity.

show abstract

Erratum: ABIN-1 is a ubiquitin sensor that restricts cell death and sustains embryonic development

Cited by 15 publications

References 1 publication

ABINs: A20 binding inhibitors of NF-κB and apoptosis signaling

ABINs: A20 binding inhibitors of NF-κB and apoptosis signaling

Regulation of death receptor signaling by the ubiquitin system

A20-binding inhibitor of NF-κB (ABIN1) controls Toll-like receptor-mediated CCAAT/enhancer-binding protein β activation and protects from inflammatory disease

Contact Info

Product

Resources

About