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Binding of NUFIP2 to Roquin promotes recognition and regulation of ICOS mRNA.
RC3H1 is a multifunctional regulator of immune homeostasis. (Review)
Crystal structures, small-angle X-ray scattering, and E2 profiling revealed that while the two paralogs are highly homologous, RC3H2 and RC3H1 are different in their structures and functions.
A distinct, sequence-induced conformation is required for recognition of the constitutive decay element RNA by Roquin.
Roquin-1 and roquin-2 proteins function redundantly in mRNA degradation.
RC3H1 binds preferentially short-lived and DNA damage-induced mRNAs. Knockdown of RC3H1 resulted in increased A20 protein expression, thereby interfering with IkappaB kinase and NF-kappaB activities.
In this review we summarize current progress regarding the specific characteristics of sequences and structures in the 3' untranslated regions of mRNAs that are recognized by tristetraproline, Roquins, and Regnase-1.
decreased expression in colon biopsies of Crohn's disease patients but not in ulcerative colitis patients
Roquin binding to target mRNAs involves a winged helix-turn-helix motif.
Findings reveal that differential regulation of mRNAs by Regnase-1 and Roquin depends on their translation status and enables elaborate control of inflammation.
Roquin-mediated degradation of HMGXB3 and IL6 mRNAs in human cells, demonstrates the importance of both binding sites for mRNA decay.
Excessive interferon (IFN)-gamma signaling promotes accumulation of Roquin-mutated, short-lived effector-like CD8+ T cells in autoimmune-prone transgenic mice.
most Roquin targets are regulated by mRNA decay, whereas a small subset, including the Nfat5 mRNA, with more binding sites in their 3'-UTRs, are also subject to translational inhibition.
mutations of both Regnase-1 and Roquin in T cells leads to massive lymphocyte activation and increased TH1 cells. In contrast, mutation of either Regnase-1 or Roquin affected T cell activation to a lesser extent than the double mutation, indicating that Regnase-1 and Roquin function nonredundantly in T cells. Regnase-1 is capable of repressing Roquin mRNA.
Roquin-mediated control of PI3K-mTOR signaling prevents autoimmunity by restraining activation and differentiation of conventional T cells and specialization of Treg cells.
these studies suggest that modulation of Roquin in myeloid cells may reduce both inflammation and bacterial growth during the chronic phase of Mycobacterium tuberculosis infection
The authors unexpectedly uncover a ROQUIN-AMPK metabolic signaling nexus essential for selectively promoting T follicular helper cell responses.
Crystal structures and NMR data show that the Roquin-1 ROQ domain recognizes hexaloops in the SELEX-derived alternative decay element (ADE) and in an ADE-like variant present in the Ox40 3'-UTR with identical binding modes.
Roquin also directly binds Argonaute2, a central component of the RNA-induced silencing complex, and miR-146a, a microRNA that targets Icos mRNA.
small intestinal inflammation in Rc3h1(san/san) and Rc3h1(gt/gt) mice is due to a failure of Roquin expression in the immune system and not to insufficient systemic Roquin expression.
Over-expression of Roquin exacerbates T-cell mediated hepatitis.
Roquin inhibited T(H)17 cell differentiation and acted together with the endoribonuclease regnase-1 to repress target mRNA encoding the T(H)17 cell-promoting factors IL-6, ICOS, c-Rel, IRF4, IkappaBNS and IkappaBzeta.
Results show an opposing relationship between Roquin-1 and the IL-17a proinflammatory cytokine. Enforced expression of Rc3h1 restricts Il17a expression, and exposure of T cells to IL-10 increases Rc3h1 expression.
Roquin makes mainly non-sequence-specific contacts to the RNA, binding a more relaxed constitutive decay element consensus sequence than previously thought.
Study shows that neither alteration of ROQUIN gene nor deregulation of miR101 expression is likely to be a frequent recurrent event in AITL.
Extensive cytokine dysregulation resulting in both over-expression and under-expression of chemotactic cytokines occurred in the ileum of Roquin(san/san) mice, the region most prone to the development of inflammation
Study demonstrates that the constitutive decay element folds into an RNA stem-loop motif that is specifically recognized by Roquin and Roquin2. Binding of Roquin initiates degradation of TNF-alpha mRNA and limits TNF-alpha production in macrophages.
Roquin-1 and Roquin-2 proteins redundantly repressed the mRNA of inducible costimulator (Icos) and identified the Ox40 costimulatory receptor as another shared mRNA target.
overexpression of Roquin exacerbates the development of CIA and that enforced expression of Roquin in T cells may promote autoimmune diseases such as CIA
Heterozygosity for Roquinsan leads to angioimmunoblastic T-cell lymphoma-like tumors.
RC3H1, or roquin, encodes a highly conserved member of the RING type ubiquitin ligase protein family (Vinuesa et al., 2005
RING finger and C3H zinc finger protein 1
, RING finger protein 198
, probable E3 ubiquitin-protein ligase Roquin
, ring finger and CCCH-type zinc finger domains 1
, ring finger and CCCH-type domains 1
, protein Sanroque
, RING CCCH (C3H) domains 1
, RING finger and CCCH-type zinc finger domain-containing protein 1