M. J. S. Heine's research while affiliated with Collège de France and other places
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Publications (8)
PIAS3, a member of the protein inhibitor of activated STAT family, was found to interact in vivo and in vitro with TIF2, a previously described coactivator for nuclear receptors. The interaction is mediated by two distinct non-contiguous regions of TIF2. We found that TIF2-PIAS3 interaction occurs through a unique domain of PIAS3, very rich in acid...
A mouse cDNA that encodes a nuclear DNA binding protein was identified by yeast two-hybrid screening using the activation domain 2 of the nuclear receptor coactivator TIF2 as a bait. BLAST analysis revealed that the identified cDNA encodes a KDWK domain and contains sequences almost identical to three tryptic peptides of rat GMEB-1 which together w...
The nuclear receptor (NR) coactivator TIF2 possesses a single NR interaction domain (NID) and two autonomous activation domains, AD1 and AD2. The TIF2 NID is composed of three NR-interacting modules each containing the NR box motif LxxLL. Mutation of boxes I, II and III abrogates TIF2-NR interaction and stimulation, in transfected cells, of the lig...
Steroid receptors, a subgroup of the superfamily of nuclear receptors (Gronemeyer and Laudet 1995), have been the target for pharmacological drug design since their recognition as “master genes” with pleiotropic action on various physiological processes (for a review see De Groot 1995). All nuclear receptors (NRs) are transcription factors regulati...
Nuclear receptors (NRs) act as ligand-inducible transcription factors which regulate the expression of target genes upon binding to cognate response elements. The ligand-dependent activity of the NR activation function AF-2 is believed to be mediated to the transcription machinery through transcriptional mediators/intermediary factors (TIFs). We re...
Nuclear receptors (NRs) act as ligand‐inducible transcription factors which regulate the expression of target genes upon binding to cognate response elements. The ligand‐dependent activity of the NR activation function AF‐2 is believed to be mediated to the transcription machinery through transcriptional mediators/intermediary factors (TIFs). We re...
The activity of the ligand-inducible activation function 2 (AF-2) contained in the ligand binding domain (LBD) of nuclear receptors (NRs) is thought to be mediated by transcriptional intermediary factors (TIFs). We have recently reported the isolation and characterization of two novel mouse proteins, designated TIF1 and mSUG1, that interact in a li...
Using a yeast two-hybrid system we report the isolation of a novel mouse protein, mSUG1, that interacts with retinoic acid receptor alpha (RAR alpha) both in yeast cells and in vitro in a ligand- and AF-2 activating domain (AF-2 AD)-dependent manner and show that it is a structural and functional homologue of the essential yeast protein SUG1. mSUG1...
Citations
... Amongst the corepressors are NCOR1 and NCOR2 (or NCOR and SMRT, respectively) [173,174]. In agonist-bound GR, the AF2-H packs against helices 3, 4 and 10, stabilizing the receptor in the active conformation and promoting the association with coactivators proteins [142] such as NCOA1, 2, 3 and PPARγ coactivator 1α (PGC1α) [122,175,176]. Notably, some coregulators have the potential to act as either a coactivator or a corepressor, depending on the context, as was first shown for NCOA2 through the employment of distinct NCOA2 surfaces [177,178]. ...
![[object Object]](https://i1.rgstatic.net/ii/profile.image/272362025254939-1441947575301_Q64/Hinrich-Gronemeyer.jpg)
... First, high therapeutic doses (0.1-1 μM) of ATRA alter the repressive functions of the chimeric PML-RARα protein into transcriptional activation of genes involved in terminal myelocyte differentiation [21]. Second, ATRA facilitates PML-RARα proteasomal degradation via caspase-mediated cleavage and cyclic adenosine monophosphate (cAMP)-mediated degradation through ligand-binding domain phosphorylation [22][23][24]. Although both mechanisms are considered individual modes of action, both are required for APL remission, since terminally differentiated but PML-RARα-persistent myelocytes are prone to reinitiate APL [25]. ...
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... Notably, the majority of NHRs in group 1, which were correlated to favorable INSS stage, also showed a positive correlation to low age (<18 mo) and were linked to low-risk NB (Dataset S5). The nuclear receptor coactivator (NCOA) family members are important coactivators of different NHRs (41)(42)(43)(44). Since we previously found that NCOA1 is targeted by MYCN via miR-17∼92 and that low expression is linked to poor survival (32), we included this protein family in our analysis. ...
... TRIM24 has a characteristic amino-terminal RBCC (Ring, B-Box, Coiled-Coil) motif, common to members of the TRIM family of proteins (8). TRIM24 also functions as a transcriptional coregulator of numerous nuclear receptors, including estrogen receptor (ER) alpha (9)(10)(11). TRIM24 recognizes and binds a specific combinatorial signature of H3K4me0/K23ac via its carboxy-terminal tandem PHD-bromodomain. ...
... This interaction is essential to mediate the NR responses (53). Once the NR-bounded NCoA is activated, it recruits CBP, p300, p/CAF, and other transcriptional factors, leading to acetylation modulation of core histones, and chromatin decondensation (54). Since histone acetylation is not sufficient to activate the transcription of target genes, NCoA also serves as an important scaffold for the assembly of the transcription machinery and recruitment of transcription factors (TFIIB, TBP, TAFs, TFIIH) at the promoter and/or enhancer regions of NR targeted genes (55) (Fig. 3). ...
![[object Object]](https://i1.rgstatic.net/ii/profile.image/390994374742020-1470231731732_Q64/Valerie-Vivat-Hannah.jpg)
... In animals SAND domain-containing proteins are found in nucleus or cytoplasm, or have dual localization being present in both nucleus and cytoplasm [21][22][23]. In confirmation with this data pertaining to animal proteins, plant ultrapetala proteins with SAND domains are also demonstrated to localize to both the nucleus and the cytosol [15]. ...
... A rather intriguing aspect of PIAS family proteins involves their ability to not only act as coregulators to certain SHRs themselves, but to interact with and modify the actions of separate coregulators in distinct families (106,108,111,112). PIAS1 exerts a direct effect on SRC-3 coactivator proteins via promotion of their sumoylation. ...
