YEAF1/RYBP and YAF-2 Are Functionally Distinct Members of a Cofactor Family for the YY1 and E4TF1/hGABP Transcription Factors

Sawa, Chika; Yoshikawa, Tatsufumi; Matsuda-Suzuki, Fumihiko; Deléhouzée, Sophie; Goto, Masahide; Watanabe, Hidenobu; Sawada, Jun‐ichi; Kataoka, Kohsuke; Handa, Hiroshi

doi:10.1074/jbc.m203060200

Cited by 52 publications

(48 citation statements)

References 31 publications

(45 reference statements)

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“…DEDAF was isolated earlier in a yeast twohybrid screen, using the DED of pro-caspases 8 and 10, 16 and was also found by others as a binding partner for the transcription factor E4TF1/hGABP and named YEAF1. 17 RYBP, its murine homologue, was isolated in a yeast twohybrid screen with Ring1A, a member of the Polycomb group of transcription regulators. 18 DEDAF and RYBP have a close structural and functional homologue, termed YAF-2.…”

Section: Discussionmentioning

confidence: 99%

“…Recently, this protein was identified by another group as DEDAF, 16 and it has also been named YEAF1 (YY1-and E4TF1/hGABP-associated factor). 17 One of our clones contained the complete open reading frame (GenBank # AY228125). The other clone encoded DEDAF with an N-terminal deletion of 30 amino acids, and was designated DEDAF-DN30.…”

Section: Apoptin Interacts With Human Dedafmentioning

confidence: 99%

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Human death effector domain-associated factor interacts with the viral apoptosis agonist Apoptin and exerts tumor-preferential cell killing

Oorschot

Voskamp²,

Seelen³

et al. 2004

Cell Death Differ

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Apoptin, a protein from chicken anemia virus without an apparent cellular homologue, can induce apoptosis in mammalian cells. Its cytotoxicity is limited to transformed or tumor cells, making Apoptin a highly interesting candidate for cancer therapy. To elucidate Apoptin's mechanism of action, we have searched for binding partners in the human proteome. Here, we report that Apoptin interacts with DEDAF, a protein previously found to associate with death effector domain (DED)-containing pro-apoptotic proteins, and to be involved in regulation of transcription. Like Apoptin, after transient overexpression, DEDAF induced apoptosis in various human tumor cell lines, but not in primary fibroblasts or mesenchymal cells. DEDAF-induced cell death was inhibited by the caspase inhibitor p35. Together with the reported association of DEDAF with a DED-containing DNA-binding protein in the nucleus and the transcription regulatory activity, our findings may provide a clue for the mechanism of Apoptin's actions in mammalian cells.

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Section: Discussionmentioning

confidence: 99%

Section: Apoptin Interacts With Human Dedafmentioning

confidence: 99%

Human death effector domain-associated factor interacts with the viral apoptosis agonist Apoptin and exerts tumor-preferential cell killing

Oorschot

Voskamp²,

Seelen³

et al. 2004

Cell Death Differ

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“…Az Rybp protein különböző változatos funkciójú fehérjékkel alkotott funkcionális kapcsolatai révén számos fiziológiás és patológiás folyamathoz köthető [6]. Így kölcsönhatásba lép transzkripcionális ko-represszorokkal vagy a sejtproliferációban kulcsfontosságú géntermékekkel.…”

Section: Az Rybp Kölcsönhatásai Egyéb Ismert Fehérjékkelunclassified

“…A Yaf2 fehérjéről, ami aminosav szinten 55%-ban homológ az Rybp-vel, szintén kimutatták hogy kölcsönhatásba lép számos PRC1 komplex taggal és DNS kötő fehérjével [6,9,10].…”

Section: Az Rybp Homológ Yaf2 éS Feltételezett Szerepei: a Funkcionálunclassified

“…Egy korai modell szerint az Rybp transzkripcionális ko-represszorként, míg a Yaf2 ko-aktivátorként funkcionál [4,6,9], noha későbbi tanulmányok kimutatták ennek az ellenkezőjét is [7,11]. A két fejérje domén szerkezete is hasonló: azok N-terminális régiót kivéve, ahol a cink-finger domének találhatók, egy szerin-gazdag rész húzódik amely nem mutat homológiát más ismert fehérje doménekkel és nagyfokú rendezetlenséget muatat (IDP; intrinsically disordered proteins) [4,5,9].…”

Section: Az Rybp Homológ Yaf2 éS Feltételezett Szerepei: a Funkcionálunclassified

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A polycomb protein RYBP/DEDAF in vivo funkcióinak vizsgálata transzgenikus módszerekkel

Pirity

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PcG recruitment by the YY1 REPO domain can be mediated by Yaf2

Wilkinson

Pratt

Atchison

2009

J of Cellular Biochemistry

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The Polycomb Group (PcG) complex of transcriptional repressors is critical for the maintenance of stage-specific developmental gene expression, stem cell maintenance and for large-scale chromosomal dynamics. Functional deficiency of a single PcG gene can severely compromise PcG function, leading to developmental defects, embryonic lethality, or a number of malignancies. Despite the critical nature of PcG proteins, the mechanisms by which these complexes mediate their effects are relatively uncharacterized. Nearly all vertebrate PcG proteins lack inherent DNA binding capacity, making it unclear how they are targeted to Polycomb response element (PRE) sequences. Transcription factor YY1 is a functional ortholog of a Drosophila PcG protein, Pleiohomeotic (PHO), one of the few PcG proteins with specific DNA binding capability, and YY1 can recruit PcG proteins to specific DNA sequences. A small 25 amino acid YY1 domain (the REPO domain) is necessary and sufficient for recruitment of PcG proteins to DNA and for transcriptional repression. We show here that the YY1 REPO domain interacts with PcG protein Yaf2 and recruits Yaf2 to DNA. Interaction is lost when the YY1 REPO domain is deleted. In addition we show that Yaf2, when linked to a heterologous DNA binding domain, can recruit PcG proteins to DNA leading to transcriptional repression. When the Drosophila homolog of Yaf2 (dRYBP) is mutated, PcG recruitment to DNA is reduced. Taken together, our results suggest that Yaf2 serves as a molecular bridge between YY1 and other PcG complex proteins.

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YEAF1/RYBP and YAF-2 Are Functionally Distinct Members of a Cofactor Family for the YY1 and E4TF1/hGABP Transcription Factors

Cited by 52 publications

References 31 publications

Human death effector domain-associated factor interacts with the viral apoptosis agonist Apoptin and exerts tumor-preferential cell killing

Human death effector domain-associated factor interacts with the viral apoptosis agonist Apoptin and exerts tumor-preferential cell killing

A polycomb protein RYBP/DEDAF in vivo funkcióinak vizsgálata transzgenikus módszerekkel

PcG recruitment by the YY1 REPO domain can be mediated by Yaf2

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