The tripartite motif family identifies cell compartments

Reymond, Alexandre; Meroni, Germana; Fantozzi, Anna; Merla, Giuseppe; Cairo, Stefano; Luzi, Lucilla; Riganelli, Daniela; Zanaria, Elena; Messali, Silvia; Cainarca, Silvia; Guffanti, Alessandro; Minucci, Saverio; Pelicci, Pier Giuseppe; Ballabio, Andrea

doi:10.1093/emboj/20.9.2140

Cited by 1,220 publications

(1,360 citation statements)

References 67 publications

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“…In addition, BBCC is most likely responsible for self-interaction of all TRIMs. 25 We also expressed the RFP domain of as yet unknown function, which is present in different types of proteins. 31 ProIL-1b consists of the prosequence, which inhibits receptor binding, and of the mature part.…”

Section: Identification Of the Interaction Domains Of Ebbp And Its Bimentioning

confidence: 99%

“…Apart from its pyrin domain, Pyrin is a typical member of the TRIM (tripartite motif) family. 25 These proteins share at least two domains, a B box and a coiled-coil domain, allowing self-interaction and the generation of large protein complexes. 25 The estrogen-responsive B box protein (EBBP, TRIM16) is a close homolog of Pyrin (TRIM20), but it lacks the pyrin domain.…”

Section: Introductionmentioning

confidence: 99%

“…25 These proteins share at least two domains, a B box and a coiled-coil domain, allowing self-interaction and the generation of large protein complexes. 25 The estrogen-responsive B box protein (EBBP, TRIM16) is a close homolog of Pyrin (TRIM20), but it lacks the pyrin domain. 25,26 We have recently characterized EBBP and we showed that it accelerates differentiation of cultured keratinocytes.…”

Section: Introductionmentioning

confidence: 99%

“…25 The estrogen-responsive B box protein (EBBP, TRIM16) is a close homolog of Pyrin (TRIM20), but it lacks the pyrin domain. 25,26 We have recently characterized EBBP and we showed that it accelerates differentiation of cultured keratinocytes. 27 To elucidate the function of this ubiquitously expressed protein at the molecular level we performed a yeast two-hybrid screen with the RFP domain and identified proIL-1b as an EBBP-binding protein.…”

Section: Introductionmentioning

confidence: 99%

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The estrogen-responsive B box protein: a novel enhancer of interleukin-1β secretion

et al. 2006

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The estrogen-responsive B box protein (EBBP) and Pyrin belong to a family of structurally related proteins. While mutations in the pyrin gene cause an autoinflammatory disease, the biological function of EBBP is unknown. In this study, we identified the proinflammatory cytokine interleukin1b (IL-1b) as an EBBP-binding partner. Furthermore, caspase-1 and NACHT, LRR and Pyrin domain containing protein (NALP) 1, two components of the recently identified inflammasome, a platform for the activation of caspase-1, also interact with EBBP. These proteins bind to the RFP domain of EBBP, suggesting that this domain of so far unknown function is an important protein-binding domain. EBBP was secreted in a caspase-1-dependent manner from cultured cells, and its secretion was enhanced by IL-1b. Vice versa, endogenous and overerexpressed EBBP increased IL-1b secretion. These results provide evidence for a role of EBBP in innate immunity by enhancing the alternative secretion pathway of IL-1b.

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Section: Identification Of the Interaction Domains Of Ebbp And Its Bimentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

The estrogen-responsive B box protein: a novel enhancer of interleukin-1β secretion

et al. 2006

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“…10 The MID1 protein consists of 667 amino acids and belongs to the tripartite motif family. 14,15 The N-terminus of the protein is composed of a RING finger motif (R), two B-box zinc-fingers (B1 and B2) and a coiled coil region. 14 The C-terminus consists of a COS box, fibronectin type 3 domain and a B30.2 domain (PRY+SPRY).…”

Section: Introductionmentioning

confidence: 99%

Hypospadias associated with hypertelorism, the mildest phenotype of Opitz syndrome

et al. 2011

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Hypospadias is a common congenital malformation in boys in which the urethral meatus opens on the underside of the penis. It is considered a complex disorder with several genes involved and the molecular etiology is just beginning to be revealed. As more than 85% of Opitz G/BBB syndrome (OS) patients with MID1 mutations are manifested with hypospadias, we have investigated the association between the MID1 gene and hypospadias. DNA from 114 hypospadias cases was analyzed with direct sequencing of the MID1 gene. Genotyping analysis was performed for the single-nucleotide polymorphism (SNP) c.1230G4A in 370 individuals with varying degrees of hypospadias and compared with 759 healthy controls. We identified one nonsense mutation c.712G4T (p.E238X), one missense mutation c.1679A4G (p.K560R) and two synonymous variants c.1230G4A (p.S410S) and c.1284T4G (p.V428V). We also detected a significant difference in the rare allele frequency of SNP c.1230G4A in hypospadias patients as compared with controls (P¼0.016). Our finding suggests that hypospadias associated with hypertelorism is the mildest phenotype in OS caused by MID1 mutations.

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TRIM8 regulates stemness in glioblastoma through PIAS3‐STAT3

et al. 2017

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Glioblastoma (GBM) is the most malignant form of primary brain tumor, and GBM stem‐like cells (GSCs) contribute to the rapid growth, therapeutic resistance, and clinical recurrence of these fatal tumors. STAT3 signaling supports the maintenance and proliferation of GSCs, yet regulatory mechanisms are not completely understood. Here, we report that tri‐partite motif‐containing protein 8 (TRIM8) activates STAT3 signaling to maintain stemness and self‐renewing capabilities of GSCs. TRIM8 (also known as ‘glioblastoma‐expressed ring finger protein’) is expressed equally in GBM and normal brain tissues, despite its hemizygous deletion in the large majority of GBMs, and its expression is highly correlated with stem cell markers. Experimental knockdown of TRIM8 reduced GSC self‐renewal and expression of SOX2, NESTIN, and p‐STAT3, and promoted glial differentiation. Overexpression of TRIM8 led to higher expression of p‐STAT3, c‐MYC, SOX2, NESTIN, and CD133, and enhanced GSC self‐renewal. We found that TRIM8 activates STAT3 by suppressing the expression of PIAS3, an inhibitor of STAT3, most likely through E3‐mediated ubiquitination and proteasomal degradation. Interestingly, we also found that STAT3 activation upregulates TRIM8, providing a mechanism for normalized TRIM8 expression in the setting of hemizygous gene deletion. These data demonstrate that bidirectional TRIM8‐STAT3 signaling regulates stemness in GSC.

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The tripartite motif family identifies cell compartments

Cited by 1,220 publications

References 67 publications

The estrogen-responsive B box protein: a novel enhancer of interleukin-1β secretion

The estrogen-responsive B box protein: a novel enhancer of interleukin-1β secretion

Hypospadias associated with hypertelorism, the mildest phenotype of Opitz syndrome

TRIM8 regulates stemness in glioblastoma through PIAS3‐STAT3

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