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  PIASy, a nucler matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies.

Sachdev, S., Bruhn, L., Sieber, H., Pichler, A., Melchior, F., & Grosschedl, R. (2001). PIASy, a nucler matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies. Genes and Development, 15, 3088-3103. doi:10.1101/gad.944801.

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 Creators:
Sachdev, Shrikesh1, Author
Bruhn, Laurakay1, Author
Sieber, Heidemarie1, Author
Pichler, Andrea2, Author              
Melchior, Frauke1, Author
Grosschedl, Rudolf3, Author              
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1External Organizations, ou_persistent22              
2Department of Epigenetics, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society, ou_2243644              
3Department of Cellular and Molecular Immunology, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society, ou_2243641              

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Free keywords: PIAS; SUMO; LEF1/TCF; nuclear matrix; PML bodies
 Abstract: The Wnt-responsive transcription factor LEF1 can activate transcription in association with beta-catenin and repress transcription in association with Groucho. In search of additional regulatory mechanisms of LEF1 function, we identified the protein inhibitor of activated STAT, PIASy, as a novel interaction partner of LEF1. Coexpression of PIASy with LEF1 results in potent repression of LEF1 activity and in covalent modification of LEF1 with SUMO. PIASy markedly stimulates the sumoylation of LEF1 and multiple other proteins in vivo and functions as a SUMO E3 ligase for LEF1 in a reconstituted system in vitro. Moreover, PIASy binds to nuclear matrix-associated DNA sequences and targets LEF1 to nuclear bodies, suggesting that PIASy-mediated subnuclear sequestration accounts for the repression of LEF1 activity.

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Language(s): eng - English
 Dates: 2001
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: DOI: 10.1101/gad.944801
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Title: Genes and Development
Source Genre: Journal
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Publ. Info: Cold Spring Harbor Laboratory Press
Pages: - Volume / Issue: 15 Sequence Number: - Start / End Page: 3088 - 3103 Identifier: ISSN: 0890-9369
CoNE: https://pure.mpg.de/cone/journals/resource/954925557453