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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
RC3H1 is a multifunctional regulator of immune homeostasis. (Review)
The authors unexpectedly uncover a ROQUIN-AMPK (show PRKAA1 Proteins) 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 (show EIF2C2 Proteins), a central component of the RNA-induced silencing complex, and miR (show MLXIP Proteins)-146a, a microRNA that targets Icos (show ICOS Proteins) mRNA.
small intestinal inflammation in Rc3h1(san/san) and Rc3h1(gt/gt (show FABP6 Proteins)) 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 (show IL6 Proteins), ICOS (show ICOS Proteins), c-Rel (show NFkBP65 Proteins), IRF4 (show IRF4 Proteins), IkappaBNS (show NFKBID Proteins) and IkappaBzeta (show NFKBIZ Proteins).
Results show an opposing relationship between Roquin-1 and the IL-17a (show IL17A Proteins) proinflammatory cytokine. Enforced expression of Rc3h1 restricts Il17a (show IL17A Proteins) expression, and exposure of T cells to IL-10 (show IL10 Proteins) 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.
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 (show TNFAIP3 Proteins) protein expression, thereby interfering with IkappaB kinase (show CHUK Proteins) and NF-kappaB (show NFKB1 Proteins) 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 (show ZFP36 Proteins), Roquins, and Regnase-1.
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 (show HMGXB3 Proteins) and IL6 (show IL6 Proteins) mRNAs in human cells, demonstrates the importance of both binding sites for mRNA decay.
Excessive interferon (IFN)-gamma (show IFNA Proteins) signaling promotes accumulation of Roquin-mutated, short-lived effector-like CD8 (show CD8A Proteins)+ T cells in autoimmune-prone transgenic mice.
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