TRIM Protein-Mediated Regulation of Inflammatory and Innate Immune Signaling and Its Association with Antiretroviral Activity

Uchil, Pradeep D.; Hinz, Angelika; Siegel, Steven J.; Coenen-Stass, Anna M.L.; Pertel, Thomas; Luban, Jeremy; Mothes, Walther

doi:10.1128/jvi.01804-12

Cited by 193 publications

(194 citation statements)

References 75 publications

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“…In these TRIM molecules, the B30. (46)(47)(48). The presence of a large cytosolic protein domain at the C terminus of two protein families that are otherwise unrelated appears to be unique in the human protein catalog (35).…”

Section: Tripartite Motif Molecules In Cell-autonomous Immunitymentioning

confidence: 99%

Regulation of Immunity by Butyrophilins

Rhodes

Reith

Trowsdale

2016

Annu. Rev. Immunol.

134

137

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Butyrophilin molecules (commonly contracted to BTN), collectively take their name from the eponymous protein in cow's milk. They are considered to be members of the B7 family of costimulatory receptors, which includes B7.1 (CD80), B7.2 (CD86), and related molecules, such as PD-L1 (B7-H1, CD274), ICOS-L (CD275), and B7-H3 (CD276). These coreceptors modulate T cell responses upon antigen presentation by major histocompatibility complex and cognate αβ T cell receptor engagement. Molecules such as BTN3A1 (CD277), myelin oligodendrocyte glycoprotein, and mouse Skint1 and Btnl2, all members of the butyrophilin family, show greater structural and functional diversity than the canonical B7 receptors. Some butyrophilins mediate complex interactions between antigen-presenting cells and conventional αβ T cells, and others regulate the immune responses of specific γδ T cell subsets by mechanisms that have characteristics of both innate and adaptive immunity.

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Section: Tripartite Motif Molecules In Cell-autonomous Immunitymentioning

confidence: 99%

Regulation of Immunity by Butyrophilins

Rhodes

Reith

Trowsdale

2016

Annu. Rev. Immunol.

134

137

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“…In support of this hypothesis, we observed that TRIM15 disassembles from focal adhesions predominantly as oligomeric bodies, in contrast to zyxin, which dispersed readily into the actin stress fibers and cytoplasm during focal adhesion disassembly (supplementary material Movie 5). Thus, these data add to the emerging ability of TRIM proteins to form higher-order oligomers due to interactions through their B-box, a feature crucial for their ability to form signaling platforms as well as to their function (Borden et al, 1996;Diaz-Griffero et al, 2009;Ganser-Pornillos et al, 2011;Pertel et al, 2011;Uchil et al, 2013).…”

Section: Discussionmentioning

confidence: 99%

“…The presence of a RING domain suggests that it can function as an E3 ligase. The B-box and coiled-coil domains are believed to participate in protein-protein interactions and the formation of oligomers that are crucial for the biological activities of TRIM proteins (Borden et al, 1996;Diaz-Griffero et al, 2009;Ganser-Pornillos et al, 2011;Uchil et al, 2013). The PRY and SPRY/B30.2 domains can function as immune defense components and in pathogen sensing (Pertel et al, 2011;Rhodes et al, 2005;Stremlau et al, 2005;Uchil et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

“…Like many other TRIM proteins, TRIM15 forms cytoplasmic bodies upon ectopic expression (Stremlau et al, 2004;Uchil et al, 2008). TRIM15 has been shown to regulate inflammatory and innate immune signaling, in addition to displaying antiviral activities (Uchil et al, 2013;Uchil et al, 2008). Cellular interactors of TRIM15 that could potentially provide further understanding of its physiological function are unknown.…”

Section: Introductionmentioning

confidence: 99%

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TRIM15 is a focal adhesion protein that regulates focal adhesion disassembly

Uchil

Pawliczek

Reynolds

et al. 2014

Journal of Cell Science

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Focal adhesions are macromolecular complexes that connect the actin cytoskeleton to the extracellular matrix. Dynamic turnover of focal adhesions is crucial for cell migration. Paxillin is a multiadaptor protein that plays an important role in regulating focal adhesion dynamics. Here, we identify TRIM15, a member of the tripartite motif protein family, as a paxillin-interacting factor and a component of focal adhesions. TRIM15 localizes to focal contacts in a myosin-II-independent manner by an interaction between its coiled-coil domain and the LD2 motif of paxillin. Unlike other focal adhesion proteins, TRIM15 is a stable focal adhesion component with restricted mobility due to its ability to form oligomers. TRIM15-depleted cells display impaired cell migration and reduced focal adhesion disassembly rates, in addition to enlarged focal adhesions. Thus, our studies demonstrate a cellular function for TRIM15 as a regulatory component of focal adhesion turnover and cell migration.

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“…Many TRIM proteins are upregulated in response to IFN stimulation (6) and are revealed to play important roles in antiviral immune responses (4,5,(7)(8)(9)(10). TRIM22 was originally identified as an IFN-inducible gene in Daudi cells (11) and was recently found to be implicated in IFN-mediated antiretroviral activity in recent years (12,13).…”

mentioning

confidence: 99%

Inhibition of Histone Deacetylase Activity Suppresses IFN-γ Induction of Tripartite Motif 22 via CHIP-Mediated Proteasomal Degradation of IRF-1

Gao

Wang

et al. 2013

The Journal of Immunology

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Tripartite motif (TRIM)22 plays an important role in IFN-mediated antiviral activity. We previously demonstrated that IFN regulatory factor (IRF)-1 was crucial for basal and IFN-induced TRIM22 transcription via binding to a novel cis-element named 5′ extended IFN-stimulating response element. In this study, we investigated the role of histone deacetylase (HDAC) activity in TRIM22 induction by IFN-γ and its underlying mechanism. We found that the HDAC activity, especially that conferred by HDAC6, was required for IFN-γ–induced TRIM22 transcription. Importantly, inhibition of HDAC activity by trichostatin A (TSA) enhanced the hyperacetylation of heat shock protein (HSP)90 and suppressed its chaperone activity for IRF-1. Further study showed that TSA treatment promoted the proteasomal degradation of IRF-1 protein via enhancing the association of IRF-1 with the ubiquitin E3 ligase carboxyl terminus of Hsc70-interacting protein. Moreover, carboxyl terminus of Hsc70-interacting protein was found to be involved in the TSA-mediated inhibitory effect on IFN-γ induction of TRIM22 as well as other IRF-1–dependent IFN-stimulated genes. This study may provide novel insight into the role of HDAC activity in the transcriptional control of IFN-stimulated gene induction.

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TRIM Protein-Mediated Regulation of Inflammatory and Innate Immune Signaling and Its Association with Antiretroviral Activity

Cited by 193 publications

References 75 publications

Regulation of Immunity by Butyrophilins

Regulation of Immunity by Butyrophilins

TRIM15 is a focal adhesion protein that regulates focal adhesion disassembly

Inhibition of Histone Deacetylase Activity Suppresses IFN-γ Induction of Tripartite Motif 22 via CHIP-Mediated Proteasomal Degradation of IRF-1

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