PIAS/SUMO: new partners in transcriptional regulation

Schmidt, D; Müller, Stefan

doi:10.1007/s00018-003-3129-1

Cited by 243 publications

(219 citation statements)

References 104 publications

(96 reference statements)

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“…PIAS family proteins are conserved SUMO E3 ligases that can enhance SUMO conjugation of various targets (Schmidt and Muller, 2003). In man, four PIAS genes have been identified (PIAS1, PIAS3, PIASx and PIASy) which encode proteins that share a similar domain structure, but differ in their specificity of interaction with other proteins.…”

Section: Sumoylation and Ubiquitinylation Of Ets-1mentioning

confidence: 99%

Regulation of the Ets-1 transcription factor by sumoylation and ubiquitinylation

Degerny

Vintonenko

et al. 2006

Oncogene

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Sumoylation and ubiquitinylation reversibly regulate the activity of transcription factors through covalent attachment to lysine residues of target proteins. We examined whether the Ets-1 transcription factor is modified by sumoylation and/or ubiquitinylation. Among four potential SUMO motifs in Ets-1, we identified lysines 15 and 227 within the LK 15 YE and IK 227 QE motifs, as being the sumoylation acceptor sites. Using transfection of Ets-1 wildtype (WT) or its sumoylation deficient version (Ets-1 K15R/K227R), as well as WT or mutant proteins of the SUMO pathway, we further demonstrated that the E2 SUMO-conjugating enzyme Ubc9 and a E3 SUMO ligase, PIASy, can enhance Ets-1 sumoylation, while a SUMO protease, SENP1, can desumoylate Ets-1. We also found that Ets-1 is modified by K48-linked polyubiquitinylation independently of the sumoylation acceptor sites and is degraded through the 26S proteasome pathway, while sumoylation of Ets-1 does not affect its stability. Finally, sumoylation of Ets-1 leads to reduced transactivation and we demonstrated that previously identified critical lysine residues in Synergistic Control motifs are the sumoylation acceptor sites of Ets-1. These data show that Ets-1 can be modified by sumoylation and/or ubiquitinylation, with sumoylation repressing transcriptional activity of Ets-1 and having no clear antagonistic action on the ubiquitin-proteasome degradation pathway.

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Section: Sumoylation and Ubiquitinylation Of Ets-1mentioning

confidence: 99%

Regulation of the Ets-1 transcription factor by sumoylation and ubiquitinylation

Degerny

Vintonenko

et al. 2006

Oncogene

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“…Although the sumoylation process resembles ubiquitination, unlike ubiquitin ligation, target proteins typically include several sumoylation sites consisting of a short consensus sequence, Ψ-K-X-EED ( , large hydrophobic amino acid; K, Ψ the acceptor lysine; X, any amino acid; EED, glutamate or aspartate) (Schmidt and Müller, 2003). SUMO modification of substrate proteins in animals and yeasts participate in critical and diverse cellular processes, such as innate immunity, chromatin stability and cell division, DNA repair, nucleocytoplasmic trafficking, transcriptional regulation, and ubiquitination antagonism (Gill, 2005;Hay, 2005).…”

Section: Introductionmentioning

confidence: 99%

Identification and Molecular Properties of SUMO-Binding Proteins in Arabidopsis

Park

Choi

Park

et al. 2011

Molecules and Cells

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Reversible conjugation of the small ubiquitin modifier (SUMO) peptide to proteins (SUMOylation) plays important roles in cellular processes in animals and yeasts. However, little is known about plant SUMO targets. To identify SUMO substrates in Arabidopsis and to probe for biological functions of SUMO proteins, we constructed 6xHis-3xFLAG fused AtSUMO1 (HFAtSUMO1) controlled by the CaMV35S promoter for transformation into Arabidopsis Col-0. After heat treatment, an increased sumoylation pattern was detected in the transgenic plants. SUMO1-modified proteins were selected after two-dimensional gel electrophoresis (2-DE) image analysis and identified using matrix-assisted laser-desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS). We identified 27 proteins involved in a variety of processes such as nucleic acid metabolism, signaling, metabolism, and including proteins of unknown functions. Binding and sumoylation patterns were confirmed independently. Surprisingly, MCM3 (At5G46280), a DNA replication licensing factor, only interacted with and became sumoylated by AtSUMO1, but not by SUMO1ΔGG or AtSUMO3. The results suggest specific interactions between sumoylation targets and particular sumoylation enzymes.

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“…Ubiquitin and the small ubiquitin-like modifier (Sumo) are gene-encoded peptides that are conjugated to target proteins via a cascade of enzymatic reactions (Weissman, 2001;Schmidt and Muller, 2003). After processing from a precursor protein, the C-termini of ubiquitin or Sumo are activated by an E1 enzyme and covalently bound to an E2-conjugating enzymes, followed by the E3 ligase-catalyzed transfer to the substrate protein.…”

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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PIAS/SUMO: new partners in transcriptional regulation

Cited by 243 publications

References 104 publications

Regulation of the Ets-1 transcription factor by sumoylation and ubiquitinylation

Regulation of the Ets-1 transcription factor by sumoylation and ubiquitinylation

Identification and Molecular Properties of SUMO-Binding Proteins in Arabidopsis

Ubc9 Regulates Mitosis and Cell Survival during Zebrafish Development

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