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Paul B. Rothman - One of the best experts on this subject based on the ideXlab platform.
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trim8 gerp RING Finger Protein interacts with socs 1
Journal of Biological Chemistry, 2002Co-Authors: Elena Toniato, Julie A. Losman, Vincenzo Flati, Liz Donahue, Peter X Chen, Paul B. RothmanAbstract:Members of the suppressor of cytokine signaling (SOCS) family of signaling molecules regulate the activation of cytokine signaling. Experimental evidence indicates that SOCS expression is induced by cytokines and pro-inflammatory stimuli and is controlled at both the transcriptional and post-transcriptional levels. SOCS Proteins are unstable and seem to be rapidly degraded by proteasomal pathways. However, the mechanisms by which SOCS Protein levels are regulated remain unclear. Here, we show that TRIM8/GERP, a RING Finger Protein, interacts with SOCS-1 in vitro and in vivo. TRIM8/GERP, previously identified as a new member of the family of Proteins containing a tripartite motif (TRIM), is a 551-amino acid RING Finger Protein conserved across species. TRIM8/GERP expression can be induced by interferon-gamma in epithelial and lymphoid cells. Coexpression of TRIM8/GERP with SOCS-1 decreases SOCS-1 Protein stability and levels. Functionally, expression of TRIM8/GERP decreases the repression of interferon-gamma signaling mediated by SOCS-1. These data suggest that TRIM8/GERP may be a regulator of SOCS-1 function.
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TRIM8/GERP RING Finger Protein interacts with SOCS-1.
The Journal of biological chemistry, 2002Co-Authors: Elena Toniato, X. Peter Chen, Julie A. Losman, Vincenzo Flati, Liz Donahue, Paul B. RothmanAbstract:Members of the suppressor of cytokine signaling (SOCS) family of signaling molecules regulate the activation of cytokine signaling. Experimental evidence indicates that SOCS expression is induced by cytokines and pro-inflammatory stimuli and is controlled at both the transcriptional and post-transcriptional levels. SOCS Proteins are unstable and seem to be rapidly degraded by proteasomal pathways. However, the mechanisms by which SOCS Protein levels are regulated remain unclear. Here, we show that TRIM8/GERP, a RING Finger Protein, interacts with SOCS-1 in vitro and in vivo. TRIM8/GERP, previously identified as a new member of the family of Proteins containing a tripartite motif (TRIM), is a 551-amino acid RING Finger Protein conserved across species. TRIM8/GERP expression can be induced by interferon-gamma in epithelial and lymphoid cells. Coexpression of TRIM8/GERP with SOCS-1 decreases SOCS-1 Protein stability and levels. Functionally, expression of TRIM8/GERP decreases the repression of interferon-gamma signaling mediated by SOCS-1. These data suggest that TRIM8/GERP may be a regulator of SOCS-1 function.
Elena Toniato - One of the best experts on this subject based on the ideXlab platform.
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trim8 gerp RING Finger Protein interacts with socs 1
Journal of Biological Chemistry, 2002Co-Authors: Elena Toniato, Julie A. Losman, Vincenzo Flati, Liz Donahue, Peter X Chen, Paul B. RothmanAbstract:Members of the suppressor of cytokine signaling (SOCS) family of signaling molecules regulate the activation of cytokine signaling. Experimental evidence indicates that SOCS expression is induced by cytokines and pro-inflammatory stimuli and is controlled at both the transcriptional and post-transcriptional levels. SOCS Proteins are unstable and seem to be rapidly degraded by proteasomal pathways. However, the mechanisms by which SOCS Protein levels are regulated remain unclear. Here, we show that TRIM8/GERP, a RING Finger Protein, interacts with SOCS-1 in vitro and in vivo. TRIM8/GERP, previously identified as a new member of the family of Proteins containing a tripartite motif (TRIM), is a 551-amino acid RING Finger Protein conserved across species. TRIM8/GERP expression can be induced by interferon-gamma in epithelial and lymphoid cells. Coexpression of TRIM8/GERP with SOCS-1 decreases SOCS-1 Protein stability and levels. Functionally, expression of TRIM8/GERP decreases the repression of interferon-gamma signaling mediated by SOCS-1. These data suggest that TRIM8/GERP may be a regulator of SOCS-1 function.
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TRIM8/GERP RING Finger Protein interacts with SOCS-1.
The Journal of biological chemistry, 2002Co-Authors: Elena Toniato, X. Peter Chen, Julie A. Losman, Vincenzo Flati, Liz Donahue, Paul B. RothmanAbstract:Members of the suppressor of cytokine signaling (SOCS) family of signaling molecules regulate the activation of cytokine signaling. Experimental evidence indicates that SOCS expression is induced by cytokines and pro-inflammatory stimuli and is controlled at both the transcriptional and post-transcriptional levels. SOCS Proteins are unstable and seem to be rapidly degraded by proteasomal pathways. However, the mechanisms by which SOCS Protein levels are regulated remain unclear. Here, we show that TRIM8/GERP, a RING Finger Protein, interacts with SOCS-1 in vitro and in vivo. TRIM8/GERP, previously identified as a new member of the family of Proteins containing a tripartite motif (TRIM), is a 551-amino acid RING Finger Protein conserved across species. TRIM8/GERP expression can be induced by interferon-gamma in epithelial and lymphoid cells. Coexpression of TRIM8/GERP with SOCS-1 decreases SOCS-1 Protein stability and levels. Functionally, expression of TRIM8/GERP decreases the repression of interferon-gamma signaling mediated by SOCS-1. These data suggest that TRIM8/GERP may be a regulator of SOCS-1 function.
Jorma J. Palvimo - One of the best experts on this subject based on the ideXlab platform.
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the RING Finger Protein snurf modulates nuclear trafficking of the androgen receptor
Journal of Cell Science, 2000Co-Authors: Hetti Poukka, Ulla Karvonen, Jorma J. Palvimo, Noritada Yoshikawa, Hirotoshi Tanaka, Olli A. JänneAbstract:The androgen receptor (AR) is a transcription factor that mediates androgen action. We have used the green fluorescent Protein (GFP) technique to investigate dynamics of nuclear trafficking of human AR in living cells. In the absence of ligand, the GFP-AR fusion Protein is distributed between cytoplasm and nuclei. Androgen exposure leads to a rapid and complete import of GFP-AR to nuclei of CV-1 cells (>=90% nuclear in 30 minutes), whereas a pure antiandrogen, Casodex, elicits a slower (<40% nuclear in 30 minutes) and incomplete transfer. Unliganded ARs with mutations in the basic amino acids of the bipartite nuclear localization signal (NLS) within the second zinc Finger and the hinge region are predominantly cytoplasmic and their androgen-dependent nuclear import is severely compromised ((3/4)20% nuclear in 30 minutes). Interestingly, substitutions of the Leu residues flanking the bipartite NLS lead to inefficient nuclear transfer in response to androgen ((3/4)20% nuclear in 30 minutes). The ligand-binding domain of AR, which represses bipartite NLS activity, contains an agonist-specific NLS. The small nuclear RING Finger Protein SNURF, which interacts with AR through a region overlapping with the bipartite NLS, facilitates AR import to nuclei and retards its export on hormone withdrawal. More AR is associated with the nuclear matrix in the presence than absence of coexpressed SNURF. We suggest that the SNURF-mediated tetheRING of AR in nuclei represents a novel mechanism for activating steroid receptor functions.
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coregulator small nuclear RING Finger Protein snurf enhances sp1 and steroid receptor mediated transcription by different mechanisms
Journal of Biological Chemistry, 2000Co-Authors: Hetti Poukka, Olli A. Jänne, Piia Aarnisalo, Henrikki Santti, Jorma J. PalvimoAbstract:The small nuclear RING Finger Protein SNURF is not only a coactivator in steroid receptor-dependent transcription but also activates transcription from steroid-independent promoters. In this work, we show that SNURF, via the RING Finger domain, enhances Protein binding to Sp1 elements/GC boxes and interacts and cooperates with Sp1 in transcriptional activation. The activation of androgen receptor (AR) function requires regions other than the RING Finger of SNURF, and SNURF does not influence binding of AR to cognate DNA elements. The zinc Finger region (ZFR) together with the hinge region of AR are sufficient for contacting SNURF. The nuclear localization signal in the boundary between ZFR and the hinge region participates in the association of AR with SNURF, and a receptor mutant lacking the C-terminal part of the bipartite nuclear localization signal shows attenuated response to coexpressed SNURF. Some AR ZFR point mutations observed in patients with partial androgen insensitivity syndrome or male breast cancer impair the interaction of AR with SNURF and also render AR refractory to the transcription-activating effect of SNURF. Collectively, SNURF modulates the transcriptional activities of androgen receptor and Sp1 via different domains, and it may act as a functional link between steroid- and Sp1-regulated transcription.
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Identification of a novel RING Finger Protein as a coregulator in steroid receptor-mediated gene transcription.
Molecular and cellular biology, 1998Co-Authors: Anu-maarit Moilanen, Hetti Poukka, Ulla Karvonen, Marika Häkli, Olli A. Jänne, Jorma J. PalvimoAbstract:Using the DNA-binding domain of androgen receptor (AR) as a bait in a yeast two-hybrid screening, we have identified a small nuclear RING Finger Protein, termed SNURF, that interacts with AR in a hormone-dependent fashion in both yeast and mammalian cells. Physical interaction between AR and SNURF was demonstrated by coimmunoprecipitation from cell extracts and by Protein-Protein affinity chromatography. Rat SNURF is a highly hydrophilic Protein consisting of 194 amino acid residues and comprising a consensus C3HC4 zinc Finger (RING) structure in the C-terminal region and a bipartite nuclear localization signal near the N terminus. Immunohistochemical experiments indicated that SNURF is a nuclear Protein. SNURF mRNA is expressed in a variety of human and rat tissues. Overexpression of SNURF in cultured mammalian cells enhanced not only androgen, glucocorticoid, and progesterone receptor-dependent transactivation but also basal transcription from steroid-regulated promoters. Mutation of two of the potential Zn2+ coordinating cysteines to serines in the RING Finger completely abolished the ability of SNURF to enhance basal transcription, whereas its ability to activate steroid receptor-dependent transcription was maintained, suggesting that there are separate domains in SNURF that mediate interactions with different regulatory factors. SNURF is capable of interacting in vitro with the TATA-binding Protein, and the RING Finger domain is needed for this interaction. Collectively, we have identified and characterized a ubiquitously expressed RING Finger Protein, SNURF, that may function as a bridging factor and regulate steroid receptor-dependent transcription by a mechanism different from those of previously identified coactivator or integrator Proteins.
Vincenzo Flati - One of the best experts on this subject based on the ideXlab platform.
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trim8 gerp RING Finger Protein interacts with socs 1
Journal of Biological Chemistry, 2002Co-Authors: Elena Toniato, Julie A. Losman, Vincenzo Flati, Liz Donahue, Peter X Chen, Paul B. RothmanAbstract:Members of the suppressor of cytokine signaling (SOCS) family of signaling molecules regulate the activation of cytokine signaling. Experimental evidence indicates that SOCS expression is induced by cytokines and pro-inflammatory stimuli and is controlled at both the transcriptional and post-transcriptional levels. SOCS Proteins are unstable and seem to be rapidly degraded by proteasomal pathways. However, the mechanisms by which SOCS Protein levels are regulated remain unclear. Here, we show that TRIM8/GERP, a RING Finger Protein, interacts with SOCS-1 in vitro and in vivo. TRIM8/GERP, previously identified as a new member of the family of Proteins containing a tripartite motif (TRIM), is a 551-amino acid RING Finger Protein conserved across species. TRIM8/GERP expression can be induced by interferon-gamma in epithelial and lymphoid cells. Coexpression of TRIM8/GERP with SOCS-1 decreases SOCS-1 Protein stability and levels. Functionally, expression of TRIM8/GERP decreases the repression of interferon-gamma signaling mediated by SOCS-1. These data suggest that TRIM8/GERP may be a regulator of SOCS-1 function.
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TRIM8/GERP RING Finger Protein interacts with SOCS-1.
The Journal of biological chemistry, 2002Co-Authors: Elena Toniato, X. Peter Chen, Julie A. Losman, Vincenzo Flati, Liz Donahue, Paul B. RothmanAbstract:Members of the suppressor of cytokine signaling (SOCS) family of signaling molecules regulate the activation of cytokine signaling. Experimental evidence indicates that SOCS expression is induced by cytokines and pro-inflammatory stimuli and is controlled at both the transcriptional and post-transcriptional levels. SOCS Proteins are unstable and seem to be rapidly degraded by proteasomal pathways. However, the mechanisms by which SOCS Protein levels are regulated remain unclear. Here, we show that TRIM8/GERP, a RING Finger Protein, interacts with SOCS-1 in vitro and in vivo. TRIM8/GERP, previously identified as a new member of the family of Proteins containing a tripartite motif (TRIM), is a 551-amino acid RING Finger Protein conserved across species. TRIM8/GERP expression can be induced by interferon-gamma in epithelial and lymphoid cells. Coexpression of TRIM8/GERP with SOCS-1 decreases SOCS-1 Protein stability and levels. Functionally, expression of TRIM8/GERP decreases the repression of interferon-gamma signaling mediated by SOCS-1. These data suggest that TRIM8/GERP may be a regulator of SOCS-1 function.
Liz Donahue - One of the best experts on this subject based on the ideXlab platform.
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trim8 gerp RING Finger Protein interacts with socs 1
Journal of Biological Chemistry, 2002Co-Authors: Elena Toniato, Julie A. Losman, Vincenzo Flati, Liz Donahue, Peter X Chen, Paul B. RothmanAbstract:Members of the suppressor of cytokine signaling (SOCS) family of signaling molecules regulate the activation of cytokine signaling. Experimental evidence indicates that SOCS expression is induced by cytokines and pro-inflammatory stimuli and is controlled at both the transcriptional and post-transcriptional levels. SOCS Proteins are unstable and seem to be rapidly degraded by proteasomal pathways. However, the mechanisms by which SOCS Protein levels are regulated remain unclear. Here, we show that TRIM8/GERP, a RING Finger Protein, interacts with SOCS-1 in vitro and in vivo. TRIM8/GERP, previously identified as a new member of the family of Proteins containing a tripartite motif (TRIM), is a 551-amino acid RING Finger Protein conserved across species. TRIM8/GERP expression can be induced by interferon-gamma in epithelial and lymphoid cells. Coexpression of TRIM8/GERP with SOCS-1 decreases SOCS-1 Protein stability and levels. Functionally, expression of TRIM8/GERP decreases the repression of interferon-gamma signaling mediated by SOCS-1. These data suggest that TRIM8/GERP may be a regulator of SOCS-1 function.
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TRIM8/GERP RING Finger Protein interacts with SOCS-1.
The Journal of biological chemistry, 2002Co-Authors: Elena Toniato, X. Peter Chen, Julie A. Losman, Vincenzo Flati, Liz Donahue, Paul B. RothmanAbstract:Members of the suppressor of cytokine signaling (SOCS) family of signaling molecules regulate the activation of cytokine signaling. Experimental evidence indicates that SOCS expression is induced by cytokines and pro-inflammatory stimuli and is controlled at both the transcriptional and post-transcriptional levels. SOCS Proteins are unstable and seem to be rapidly degraded by proteasomal pathways. However, the mechanisms by which SOCS Protein levels are regulated remain unclear. Here, we show that TRIM8/GERP, a RING Finger Protein, interacts with SOCS-1 in vitro and in vivo. TRIM8/GERP, previously identified as a new member of the family of Proteins containing a tripartite motif (TRIM), is a 551-amino acid RING Finger Protein conserved across species. TRIM8/GERP expression can be induced by interferon-gamma in epithelial and lymphoid cells. Coexpression of TRIM8/GERP with SOCS-1 decreases SOCS-1 Protein stability and levels. Functionally, expression of TRIM8/GERP decreases the repression of interferon-gamma signaling mediated by SOCS-1. These data suggest that TRIM8/GERP may be a regulator of SOCS-1 function.
