Transcription factor Sp3 is silenced through SUMO modification by PIAS1

Sapetschnig, Alexandra; Rischitor, Grigore; Braun, Harald; Doll, Andreas; Schergaut, Marion; Melchior, Frauke; Suske, Guntram

doi:10.1093/emboj/cdf510

Cited by 238 publications

(211 citation statements)

References 46 publications

(80 reference statements)

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“…54 Similarly, p300/CBP and Sp3 are both regulated in their cofactor function -whether they act as a coactivator or corepressor -via timely controlled SUMO conjugation and deconjugation. 44,55 Thus, SUMO is an important factor to control PML-NB assembly and transcription. For a detailed review about the function of SUMO, we refer to some recently published reviews on this topic.…”

Section: Pml and Its Associated Nbsmentioning

confidence: 99%

Body language: the function of PML nuclear bodies in apoptosis regulation

2003

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Promyelocytic leukaemia (PML) nuclear bodies (NBs) are macromolecular nuclear domains present in virtually every mammalian cell. PML nuclear bodies (PML-NBs) were functionally linked to various fundamental cellular processes, including transcriptional control, tumour suppression and apoptosis regulation. Supporting the important function of PML and its associated NBs in apoptosis regulation, several apoptotic regulators localise to PML-NBs, and cells from PMLdeficient mice show severe apoptotic defects, including induction of genotoxic stress and death receptor CD95 (Fas/ APO-1) activation. Based on the current literature, we hypothesise that PML-NBs regulate apoptosis through different molecular mechanisms, on the one hand by acting as macromolecular scaffolds for recruitment and post-translational modification of the apoptotic key regulator p53, and on the other by regulating the subcellular bioavailability and quality of some apoptotic signal transducers.

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Section: Pml and Its Associated Nbsmentioning

confidence: 99%

Body language: the function of PML nuclear bodies in apoptosis regulation

2003

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“…These include nuclear hormone receptors, such as the androgen receptor (AR), p53, Smad4, Sp3, HMGI-C, Gfi-1, IRF-1, TFII-I and yeast septins (11)(12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23)(24)(25). In mouse and man, four Pias genes (Pias1, Pias3, Piasx, and Piasy) have been identified, which encode proteins that share a similar domain structure but differ in their specificity of interaction with other proteins.…”

Section: Piasy-deficient Mice Display Modest Defects In Ifn Andmentioning

confidence: 99%

PIASy-Deficient Mice Display Modest Defects in IFN and Wnt Signaling

Roth

Sustmann

Kieslinger

et al. 2004

The Journal of Immunology

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Protein inhibitors of activated STATs (PIAS) represent a small family of nuclear proteins that modulate the activity of many transcription factors and act as E3 ligases for covalent modification of proteins with the small ubiquitin-like modifier (SUMO). In particular, PIASy has been shown to inhibit the activation of gene expression by the IFN-responsive transcription factor STAT1 and the Wnt-responsive transcription factor LEF1. To assess the function of PIASy in vivo, we generated and analyzed mice carrying a targeted mutation of the Piasy gene. We find that homozygous mutant mice have no obvious morphological defects and have a normal distribution of lymphocyte populations. Molecular analysis of signaling in response to IFN-γ and Wnt agonists revealed a modest reduction in the activation of endogenous and transfected target genes. Two-dimensional analysis of total proteins and SUMO-modified proteins in transformed pre-B cells showed no significant differences between wild-type mice and homozygous mutant mice. Taken together, our data indicate that PIASy has a modest effect on cytokine and Wnt signaling, suggesting a redundancy with other members of the family of PIAS proteins.

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“…Thus, for some target proteins sumoylation regulates their nucleo-cytoplasmic trafficking (Matunis et al, 1996;Epps and Tanda, 1998) and subnuclear localization. In particular, the formation of PML (promyelocytic leukemia) nuclear bodies (Muller et al, 1998), and the inactivation of several transcriptional activators like Lef-1 (Sachdev et al, 2001) and Sp3 (Ross et al, 2002;Sapetschnig et al, 2002) via a recruitment to these nuclear compartments have been shown to be sumoylation-dependent (reviewed in Gill, 2003). In addition, protein sumoylation is involved in the regulation of DNA repair (Hardeland et al, 2002;Hoege et al, 2002;Stelter and Ulrich, 2003) and is required for proper chromosome condensation and separation (Hari et al, 2001;Strunnikov et al, 2001;Bachant et al, 2002;Azuma et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

Ubc9 Regulates Mitosis and Cell Survival during Zebrafish Development

Nowak

Hammerschmidt

2006

MBoC

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Many proteins are modified by conjugation with Sumo, a gene-encoded, ubiquitin-related peptide, which is transferred to its target proteins via an enzymatic cascade. A central component of this cascade is the E2-conjugating enzyme Ubc9, which is highly conserved across species. Loss-of-function studies in yeast, nematode, fruit fly, and mouse blastocystes point to multiple roles of Ubc9 during cell cycle regulation, maintenance of nuclear architecture, chromosome segregation, and viability. Here we show that in zebrafish embryos, reduction of Ubc9 activity by expression of a dominant negative version causes widespread apoptosis, similar to the effect described in Ubc9-deficient mice. However, antisense-based knock down of zygotic ubc9 leads to much more specific defects in late proliferating tissues, such as cranial cartilage and eyes. Affected cartilaginous elements are of relatively normal size and shape, but consist of fewer and larger cells.

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Transcription factor Sp3 is silenced through SUMO modification by PIAS1

Cited by 238 publications

References 46 publications

Body language: the function of PML nuclear bodies in apoptosis regulation

Body language: the function of PML nuclear bodies in apoptosis regulation

PIASy-Deficient Mice Display Modest Defects in IFN and Wnt Signaling

Ubc9 Regulates Mitosis and Cell Survival during Zebrafish Development

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