The GOLD Domain-containing Protein TMED1 Is Involved in Interleukin-33 Signaling*

Connolly, Dympna J.; O’Neill, Luke A. J.; McGettrick, Anne F.

doi:10.1074/jbc.m112.403899

Cited by 39 publications

(40 citation statements)

References 29 publications

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“…184 Other molecules can be found within the IL-33R complex. The transmembrane protein TMED1 positively modulates IL-33-stimulated production of cytokines, 186 presumably protecting the receptor complex from degradation by interfering with its trafficking (reviewed in 187). Once internalized, IL-1R4 is polyubiquinated by the E3 ubiquitin ligase FBXL19 185 and subsequently degraded at the proteasome.…”

Section: Expression On Cells Of Innate Immune System and Tissuesmentioning

confidence: 99%

The family of the interleukin‐1 receptors

Boraschi

Italiani

Weil

et al. 2017

Immunological Reviews

275

225

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The extracellular forms of the IL-1 cytokines are active through binding to specific receptors on the surface of target cells. IL-1 ligands bind to the extracellular portion of their ligand-binding receptor chain. For signaling to take place, a non-binding accessory chain is recruited into a heterotrimeric complex. The intracellular approximation of the Toll-IL-1-receptor (TIR) domains of the 2 receptor chains is the event that initiates signaling. The family of IL-1 receptors (IL-1R) includes 10 structurally related members, and the distantly related soluble protein IL-18BP that acts as inhibitor of the cytokine IL-18. Over the years the receptors of the IL-1 family have been known with many different names, with significant confusion. Thus, we will use here a recently proposed unifying nomenclature. The family includes several ligand-binding chains (IL-1R1, IL-1R2, IL-1R4, IL-1R5, and IL-1R6), 2 types of accessory chains (IL-1R3, IL-1R7), molecules that act as inhibitors of signaling (IL-1R2, IL-1R8, IL-18BP), and 2 orphan receptors (IL-1R9, IL-1R10). In this review, we will examine how the receptors of the IL-1 family regulate the inflammatory and anti-inflammatory functions of the IL-1 cytokines and are, more at large, involved in modulating defensive and pathological innate immunity and inflammation. Regulation of the IL-1/IL-1R system in the brain will be also described, as an example of the peculiarities of organ-specific modulation of inflammation.

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Section: Expression On Cells Of Innate Immune System and Tissuesmentioning

confidence: 99%

The family of the interleukin‐1 receptors

Boraschi

Italiani

Weil

et al. 2017

Immunological Reviews

275

225

View full text Add to dashboard Cite

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“…These proteins contain a GOLD (Golgi dynamics) domain, which is a β-strand-rich domain found in several proteins that are involved in Golgi dynamics and intracellular protein trafficking1315. Many TMED proteins have been investigated and reported on in detail1617. TMED7, which negatively regulates TLR4 signaling, was identified as a specific inhibitor of the MyD88-independent TLR4 signaling pathway through its ability to facilitate the disruption of the TRIF/TRAM complex by TAG181920.…”

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confidence: 99%

TMED3 promotes hepatocellular carcinoma progression via IL-11/STAT3 signaling

Zheng

Yang

Han

et al. 2016

Sci Rep

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Transmembrane p24 trafficking protein 3(TMED3) is a metastatic suppressor in colon cancer, but its function in the progression of hepatocellular carcinoma (HCC) is unknown. Here, we report that TMED3 was up-regulated in HCC and portal vein tumor thrombus. TMED3 up-regulation in HCC was significantly correlated with aggressive characteristics and predicted poor prognosis in HCC patients. TMED3 overexpression in HCC cell lines promoted cell migration and invasion. In contrast, TMED3 knockdown suppressed HCC metastasis both in vitro and in vivo. Gene microarray analysis revealed decreased IL-11 expression in TMED3-knockdown cells. We propose that TMED3 promotes HCC metastasis through IL-11/STAT3 signaling. Taken together, these findings demonstrate that TMED3 promotes HCC metastasis and is a potential prognostic biomarker in HCC.

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“…Following TMED1 knockdown, production of IL-6 and IL-8downstream targets of IL-33was impaired, indicating that the absence of TMED1 reduced IL-33 signalling. Surprisingly, the interaction between TMED1 and ST2L was found to occur via a protrusion of the GOLD domain of TMED1 into the cytosolic compartment (Connolly et al, 2013).…”

Section: Dysregulated Immune Responsesmentioning

confidence: 95%

Transmembrane emp24 domain proteins in development and disease.

et al. 2019

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Regulated transport through the secretory pathway is essential for embryonic development and homeostasis. Disruptions in this process impact cell fate, differentiation and survival, often resulting in abnormalities in morphogenesis and in disease. Several congenital malformations are caused by mutations in genes coding for proteins that regulate cargo protein transport in the secretory pathway. The severity of mutant phenotypes and the unclear aetiology of transport protein-associated pathologies have motivated research on the regulation and mechanisms through which these proteins contribute to morphogenesis. This review focuses on the role of the p24/transmembrane emp24 domain (TMED) family of cargo receptors in development and disease.

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The GOLD Domain-containing Protein TMED1 Is Involved in Interleukin-33 Signaling*

Cited by 39 publications

References 29 publications

The family of the interleukin‐1 receptors

The family of the interleukin‐1 receptors

TMED3 promotes hepatocellular carcinoma progression via IL-11/STAT3 signaling

Transmembrane emp24 domain proteins in development and disease.

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