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001-es BibID:	BIBFORM086696
035-os BibID:	(WoS)000553333300022 (Scopus)85088493600
Első szerző:	Fadel, Lina (gyógyszerész)
Cím:	Agonist binding directs dynamic competition among nuclear receptors for heterodimerization with retinoid X receptor / Lina Fadel, Bálint Rehó, Julianna Volkó, Dóra Bojcsuk, Zsuzsanna Kolostyák, Gergely Nagy, Gabriele Müller, Zoltán Simándi, Éva Hegedüs, Gábor Szabó, Katalin Tóth, Laszlo Nagy, György Vámosi
Dátum:	2020
ISSN:	0021-9258 1083-351X
Megjegyzések:	Retinoid X receptor (RXR) plays a pivotal role as a transcriptional regulator and serves as an obligatory heterodimerization partner for at least 20 other nuclear receptors (NRs). Given a potentially limiting/sequestered pool of RXR and simultaneous expression of several RXR partners, we hypothesized that NRs compete for binding to RXR and that this competition may be directed by specific agonist treatment. Here, we tested this hypothesis on three NRs: peroxisome proliferator-activated receptor γ (PPARγ), vitamin D receptor (VDR), and retinoic acid receptor α (RARα). Evaluation of competition relied on a nuclear-translocation assay applied in a three-color imaging model system by detecting changes in heterodimerization between RXRα and one of its partners (NR1), in the presence of another competing partner (NR2). Our results indicated dynamic competition between the NRs governed by two mechanisms. First, in the absence of agonist treatment, there is a hierarchy of affinities between RXRα and its partners in the following order: RARα>PPARγ>VDR. Second, upon agonist treatment, RXRα favors the liganded partner. We conclude that recruiting RXRα by the liganded NR not only facilitates a stimulus-specific cellular response, but might also impede other NR pathways involving RXRα.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Journal of Biological Chemistry. - 295 : 29 (2020), p. 10045-10061. -
További szerzők:	Rehó Bálint (1992-) Volkó Julianna (1983-) (biotechnológus) Bojcsuk Dóra (1990-) (klinikai laboratóriumi kutató) Kolostyák Zsuzsanna Nagy Gergely (1986-) (molekuláris biológus) Müller, Gabriele Simándi Zoltán (1984-) (Ph.D. hallgató, molekuláris biológus) Hegedűs Éva (1978-) (biofizikus) Szabó Gábor (1953-) (biofizikus) Tóth Katalin Nagy László (1966-) (molekuláris sejtbiológus, biokémikus) Vámosi György (1967-) (biofizikus)
Pályázati támogatás:	NKFIH NN129371 egyéb NKFIH KKP129909 egyéb NKFIH K124298 egyéb GINOP-2.3.2-15-2016-00050 GINOP GINOP-2.3.3-15-2016-00003 GINOP
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001-es BibID:	BIBFORM072900
035-os BibID:	(Cikkazonosító)12734 (WOS)000412491500006 (Scopus)85030764085
Első szerző:	Imre László (biológus)
Cím:	Nucleosome stability measured in situ by automated quantitative imaging / László Imre, Zoltán Simándi, Attila Horvath, György Fenyofalvi, Péter Nanasi Jr., Erfaneh Firouzi Niaki, Éva Hegedus, Zsolt Bacso, Urbain Weyemi, Rebekka Mauser, Juan Ausio, Albert Jeltsch, William Bonner, László Nagy, Hiroshi Kimura, Gábor Szabo
Dátum:	2017
ISSN:	2045-2322
Megjegyzések:	Current approaches have limitations in providing insight into the functional properties of particular nucleosomes in their native molecular environment. Here we describe a simple and powerful method involving elution of histones using intercalators or salt, to assess stability features dependent on DNA superhelicity and relying mainly on electrostatic interactions, respectively, and measurement of the fraction of histones remaining chromatin-bound in the individual nuclei using histone type- or posttranslational modification- (PTM-) specific antibodies and automated, quantitative imaging. The method has been validated in H3K4me3 ChIP-seq experiments, by the quantitative assessment of chromatin loop relaxation required for nucleosomal destabilization, and by comparative analyses of the intercalator and salt induced release from the nucleosomes of different histones. The accuracy of the assay allowed us to observe examples of strict association between nucleosome stability and PTMs across cell types, differentiation state and throughout the cell-cycle in close to native chromatin context, and resolve ambiguities regarding the destabilizing effect of H2A.X phosphorylation. The advantages of the in situ measuring scenario are demonstrated via the marked effect of DNA nicking on histone eviction that underscores the powerful potential of topological relaxation in the epigenetic regulation of DNA accessibility.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Fluorescence imaging Nuclear organization Epigenetics Molekuláris Medicina
Megjelenés:	Scientific Reports. - 7 : 1 (2017), p. 1-15. -
További szerzők:	Simándi Zoltán (1984-) (Ph.D. hallgató, molekuláris biológus) Horváth Attila (1988-) (programtervező informatikus) Fenyőfalvi György Nánási Péter Pál ifj. (1987-) (sejtbiológus) Firouzi Niaki, Erfaneh Hegedűs Éva (1978-) (biofizikus) Bacsó Zsolt (1963-) (biofizikus) Weyemi, Urbain Mauser, Rebekka Ausio, Juan Jeltsch, Albert Bonner, William Nagy László (1966-) (molekuláris sejtbiológus, biokémikus) Kimura, Hiroshi Szabó Gábor (1953-) (biofizikus)
Pályázati támogatás:	K72762 OTKA NK101337 OTKA TÁMOP-4.2.2-08/1-2008-0015 TÁMOP TÁMOP-4.2.1/B-09/1/KONV-2010-0007 TÁMOP I. ABC transzporterek; II. Magasabbrendű kromatinszerkezet TÁMOP 4.2.2.A- 11/1/KONV-2012-0023 "VÉD-ELEM TÁMOP TÁMOP 4.2.4. A/2-11-1-2012-0001 TÁMOP GINOP-2.3.2-15-2016-00044 GINOP
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001-es BibID:	BIBFORM107128
035-os BibID:	(cikkazonosító)102896 (WoS)001009016200001 (Scopus)85147540608
Első szerző:	Rehó Bálint
Cím:	Agonist-controlled competition of RAR and VDR nuclear receptors for heterodimerization with RXR is manifested in their DNA-binding / Rehó Bálint, Fadel Lina, Brazda Peter, Benziane Anass, Hegedüs Éva, Sen Pialy, Gadella Theodorus W. Jr., Tóth Katalin, Nagy László, Vámosi György
Dátum:	2023
ISSN:	0021-9258 1083-351X
Megjegyzések:	We found previously that nuclear receptors (NRs) compete for heterodimerization with their common partner, retinoid X receptor (RXR), in a ligand-dependent manner. To investigate potential competition in their DNA binding, we monitored the mobility of retinoic acid receptor (RAR) and vitamin D receptor (VDR) in live cells by fluorescence correlation spectroscopy. First, specific agonist treatment and RXR coexpression additively increased RAR DNA binding, while both agonist and RXR were required for increased VDR DNA binding, indicating weaker DNA binding of the VDR/RXR dimer. Second, coexpression of RAR, VDR, and RXR resulted in competition for DNA binding. Without ligand, VDR reduced the DNA-bound fraction of RAR and vice versa, i.e., a fraction of RXR molecules was occupied by the competing partner. The DNA-bound fraction of either RAR or VDR was enhanced by its own and diminished by the competing NR`s agonist. When treated with both ligands, the DNA-bound fraction of RAR increased as much as due to its own agonist, whereas that of VDR increased less. RXR agonist also increased DNA binding of RAR at the expense of VDR. In summary, competition between RAR and VDR for RXR is also manifested in their DNA binding in an agonist-dependent manner: RAR dominates over VDR in the absence of agonist or with both agonists present. Thus, side effects of NR-ligand-based (retinoids, thiazolidinediones) therapies may be ameliorated by other NR ligands and be at least partly explained by reduced DNA binding due to competition. Our results also complement the model of NR action by involving competition both for RXR and for DNA sites.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Journal Of Biological Chemistry. - 299 : 2 (2023), p. 1-16. -
További szerzők:	Fadel, Lina (1988-) (gyógyszerész) Brázda Péter (1980-) (biológus, angol-magyar szakfordító) Benziane, Anass (1990-) (molekuláris biológus) Hegedűs Éva (1978-) (biofizikus) Sen, Pialy Gadella, Theodorus W. Jr. Tóth Katalin (biofizikus) Nagy László (1966-) (molekuláris sejtbiológus, biokémikus) Vámosi György (1967-) (biofizikus)
Pályázati támogatás:	GINOP-2.3.2-15-2016-00026 GINOP NN129371 OTKA ANN135107 OTKA Tempus Public Foundation: Stipendium Hungaricum scholarship Egyéb German Academic Exchange Service and the Tempus Public Foundation #273478 Egyéb
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