The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and -independent pathways

Voegel, Johannes J.; Heine, Matthias J.S.; Tini, Marc; Vivat, Valérie; Chambon, Pierre; Gronemeyer, Hinrich

doi:10.1093/emboj/17.2.507

Cited by 468 publications

(483 citation statements)

References 64 publications

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“…In animals, this short L**LL motif exists in a large variety of nuclear proteins functioning as transcriptional coactivators, such as SRC-1/p160, TIF-2/GRIP-1, CBP/p300, and RIP-140. The animal L**LL motif mediates binding to liganded nuclear receptors and other transcription factors, such as the cAMP response element-binding (CREB) protein, which is one of the best characterized bZIP proteins in animals (Ribeiro et al, 1994;Le Douarin et al, 1996;Heery et al, 1997;Voegel et al, 1998).…”

Section: Discussionmentioning

confidence: 99%

“…2A). This peptide resembles the a-helical L**LL motif known to mediate the interaction between transcriptional coactivators and liganded nuclear receptors as well as many other transcription factors in animals through a hydrophobic face formed by its Leu residues (Le Douarin et al, 1996;Heery et al, 1997;Voegel et al, 1998). To test by yeast twohybrid interaction screens whether this a-helical L**LL motif of ROXY1 is essential for binding to plant TGA transcription factors, five mutagenized ROXY1 proteins were engineered by replacing one, two, or all three strongly hydrophobic Leu residues located in this motif by an Ala, which possesses a shorter and thus only weakly hydrophobic side chain ( Fig.…”

Section: Analysis Of the Roxy1 C-terminal L**ll Motifmentioning

confidence: 99%

“…This L**LL motif is shown to be essential for an interaction with TGA transcriptional factors and is indispensable for Arabidopsis petal development. Similar to the a-helical L**LL motifs of transcriptional coactivators that interact with liganded nuclear receptors as well as many other transcription factors in animals (Le Douarin et al, 1996;Heery et al, 1997;Voegel et al, 1998), a hydrophobic face formed by the conserved Leu residues in the L**LL motif of ROXY1 likely mediates the interaction with TGA transcription factors. Although crucial Cys residues of TGA proteins were identified as potential targets to be posttranslationally modified by ROXYs (Després et al, 2003;Murmu et al, 2010), little is known about the TGA domains mediating the interaction with ROXYs.…”

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confidence: 99%

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The ROXY1 C-Terminal L**LL Motif Is Essential for the Interaction with TGA Transcription Factors

Gutsche

Zachgo

2011

Plant Physiology

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Glutaredoxins (GRXs) are small, ubiquitous, glutathione-dependent oxidoreductases that participate in redox-regulated processes associated with stress responses. Recently, GRXs have been shown to exert crucial functions during flower developmental processes. GRXs modulate their target protein activities by the reduction of protein disulfide bonds or deglutathionylation reactions. The Arabidopsis (Arabidopsis thaliana) GRX ROXY1 participates in petal primordia initiation and further petal morphogenesis. ROXY1 belongs to a land plant-specific class of GRXs with a CC-type active site motif, deviating from the ubiquitously occurring CPYC and CGFS GRX classes. ROXY1 was previously shown to interact with floral TGA transcription factors in the nucleus, and this interaction is a prerequisite for ROXY1 to exert its activity required for Arabidopsis petal development. Deletion analysis further identified the importance of the ROXY1 C terminus for the ROXY1/ TGA protein interactions and for the ROXY1 function in petal development. Here, by dissecting the ROXY1 C terminus, an a-helical L**LL motif immediately adjacent to the ROXY1 C-terminal eight amino acids was identified that is essential for the interaction with TGA transcription factors and crucial for the ROXY1 function in planta. Similar to the a-helical L**LL motifs binding to transcriptional coactivators with liganded nuclear receptors in animals, a hydrophobic face formed by the conserved leucines in the L**LL motif of ROXY1 possibly mediates the interaction with TGA transcription factors. Thus, the a-helical L**LL sequence is a conserved protein-protein interaction motif in both animals and plants. Furthermore, two separate TGA domains were identified by deletion experiments as being essential for mediating TGA protein interactions with ROXYs.

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Section: Discussionmentioning

confidence: 99%

Section: Analysis Of the Roxy1 C-terminal L**ll Motifmentioning

confidence: 99%

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confidence: 99%

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The ROXY1 C-Terminal L**LL Motif Is Essential for the Interaction with TGA Transcription Factors

Gutsche

Zachgo

2011

Plant Physiology

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“…Taken together, these results suggested that p68 acts as a hERa AF-1 speci®c coactivator to constitute the cross-talk with growth factor signalling. During a detailed analysis of p68 as a hERa AF-1 coactivator, we isolated a common interactant ( two intrinsic transactivation domains (AD1 and AD2) (Kalkhoven et al 1998;Voegel et al 1998). Direct binding and potentiation by p300/CBP were reported in AD1, while a coactivator associating with AD2 remained unknown.…”

Section: Molecular Mechanism Of the Novel Cross-talk Between Oestrogementioning

confidence: 99%

Molecular mechanism of a cross‐talk between oestrogen and growth factor signalling pathways

et al. 2000

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Oestrogen (E 2 ) plays signi®cant roles in variety of biological events such as the development and maintenance of female reproductive organs, bone and lipid metabolisms. More recently, from study of knock-out mice de®cient in oestrogen receptor (ER) a and ERb it turned out that normal spermatogenesis requires the E 2 actions. Furthermore, this female steroid hormone is also well known to be deeply involved in many pathophysiological events such as osteoporosis and cancer development in female reproductive organs. It is particularly well known that most breast cancer is dependent on E 2 in its development. Such E 2 actions are thought to be mediated through two subtypes of ERs. Growth factors have been shown to synergize in this E 2 signalling pathway, although the actual molecular mechanism largely remains unknown.Recently, we found that the MAP kinase activated by growth factors phosphorylates the Ser 118 residue of the human ERa A/B domain and this phosphorylation potentiates the N-terminal transactivation function (AF-1) of human ERa, indicating the possible molecular mechanism of a novel cross-talk between E 2 and growth factor signalling pathways. More recently, we have identi®ed a coactivator associating with the hERa AF-1 in a MAPK-mediated phosphorylationdependent manner. In this review, the molecular mechanism of this cross-talk is discussed in terms of the transactivation function of ERs, and their coactivators.

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“…These proteins are grouped into three subclasses based on their sequence homology; i.e., SRC-1/NCoA-1 (Hong et al, 1997;Torchia et al, 1997;Voegel et al, 1998), TIF2/GRIP1/NCoA-2 (Hong et al, 1997;Voegel et al, 1998), and p/CIP/ ACTR/AIB1/xSRC-3 (Anzick et al, 1997;Chen et al, 1997;Kim et al, 1998;Torchia et al, 1997). A distinctive structural feature of the p160 coactivators is the presence of multiple LXXLL signature motifs (Heery et al, 1997;Torchia et al, 1997).…”

Section: The P160 Familymentioning

confidence: 99%

Dissecting the molecular mechanism of nuclear receptor action: transcription coactivators and corepressors

et al. 2000

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The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and -independent pathways

Cited by 468 publications

References 64 publications

The ROXY1 C-Terminal L**LL Motif Is Essential for the Interaction with TGA Transcription Factors

The ROXY1 C-Terminal L**LL Motif Is Essential for the Interaction with TGA Transcription Factors

Molecular mechanism of a cross‐talk between oestrogen and growth factor signalling pathways

Dissecting the molecular mechanism of nuclear receptor action: transcription coactivators and corepressors

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