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1.

001-es BibID:BIBFORM066241
Első szerző:Boratkó Anita (biokémikus, molekuláris biológus)
Cím:Regulation of merlin by protein phosphatase 1-TIMAP and EBP50 in endothelial cells / Anita Boratkó, Margit Péter, Csilla Csortos
Dátum:2017
Megjegyzések:Merlin (moesin-ezrin-radixin like protein), the product of neurofibromatosis type 2 gene, was primarily recognized as a tumor suppressor, but it also functions as a membrane-cytoskeletal linker and regulator of multiple signaling pathways. The activity and localization of merlin is regulated by head to tail folding that is controlled by phosphorylation of the Ser518 side chain. Merlin localizes in the nucleus when the Ser518 side chain is not phosphorylated, while the phosphorylated form is present in the cytoplasm and the plasma membrane. In this work interactions and their impact on the subcellular localization and phosphorylation state of the Ser518 side chain of merlin were investigated in endothelial cells. It is shown that merlin (dephospho-Ser518 form) interacts in the nucleus of endothelial cells with the scaffolding protein EBP50, a member of the Na+/H+exchanger regulatory factor family. Upon EBP50 depletion, merlin translocated from the nucleus, suggesting that binding of merlin to EBP50 is critical in the nuclear localization of merlin. Along with the translocation, the phosphorylation level of phospho-Ser518-merlin was increased in EBP50 depleted cells. TIMAP (TGF?-inhibited membrane-associated protein), a type 1 protein phosphatase (PP1) regulatory subunit, was newly recognized as an interacting partner for merlin. Domain mapping using truncated mutant forms in GST pull down revealed that the N-terminal half of TIMAP (aa 1-290) and the FERM domain of merlin are the regions responsible for the interaction.The catalytic subunit of PP1 (PP1c) was present in all merlin-TIMAP pull down or immunoprecipitation samples demonstrating that merlin actually interacts with the PP1c-TIMAP holoenzyme. On the other hand, from TIMAP depleted cells, without its targeting protein, PP1c could not bind to merlin. Also, when the phosphatase activity of PP1c-TIMAP was inhibited either with depletion of TIMAP or by treatment of the cells with specific PP1 inhibitor, there was an increase in the amount of phospho-Ser518 form of merlin in the membrane of the cells. These data strongly suggest that the PP1c-TIMAP- complex dephosphorylates phospho-Ser518-merlin. ECIS measurements indicate that phospho-merlin accelerates in vitro wound healing of the endothelial monolayer. In conclusion, in endothelial cells, EBP50 is required for the nuclear localization of merlin and the PP1c-TIMAP holoenzyme plays an important role in the dephosphorylation of merlin on its Ser518 side chain, which influence cell migration and proliferation.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
EBP50
Endothelial cells
Merlin
Protein phosphatase 1
TIMAP
Megjelenés:The International Journal of Biochemistry and Cell Biology 82 (2017), p. 10-17. -
További szerzők:Péter Margit (1987-) (Ph.D. hallgató) Csortos Csilla (1956-) (biokémikus)
Pályázati támogatás:PD116262
OTKA
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2.

001-es BibID:BIBFORM062307
Első szerző:Boratkó Anita (biokémikus, molekuláris biológus)
Cím:TIMAP-protein phosphatase 1-complex controls endothelin-1 production via ECE-1 dephosphorylation / Anita Boratkó, Zoltán Veréb, Goran Petrovski, Csilla Csortos
Dátum:2016
ISSN:1357-2725
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:International Journal Of Biochemistry & Cell Biology 73 (2016), p. 11-18. -
További szerzők:Veréb Zoltán (1980-) (immunológus, mikrobiológus, molekuláris biológus) Petrovski, Goran (1975-) (orvos) Csortos Csilla (1956-) (biokémikus)
Pályázati támogatás:TÁMOP-4.2.2.A-11/1/KONV-2012-0025
TÁMOP
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3.

001-es BibID:BIBFORM061016
Első szerző:Boratkó Anita (biokémikus, molekuláris biológus)
Cím:Elongation factor-1A1 is a novel substrate of the protein phosphatase 1-TIMAP complex / Anita Boratkó, Margit Péter, Zsófia Thalwieser, Előd Kovács, Csilla Csortos
Dátum:2015
ISSN:1357-2725
Megjegyzések:TIMAP (TGF- inhibited membrane associated protein) is a protein phosphatase 1 (PP1) regulatory subunit highly abundant in endothelial cells and it is involved in the maintenance of pulmonary endothelial barrier function. It localizes mainly in the plasma membrane, but it is also present in the nuclei and cytoplasm. Direct interaction of TIMAP with the eukaryotic elongation factor 1 A1 (eEF1A1) is shown by pull-down, LC-MS/MS, Far-Western and immunoprecipitations. In connection with the so called moonlighting functions of the elongation factor, eEF1A is thought to establish protein-protein interactions through a transcription-dependent nuclear export motif, TD-NEM, and to aid nuclear export of TD-NEM containing proteins. We found that a TD-NEM-like motif of TIMAP has a critical role in its specific binding to eEF1A1. However, eEF1A1 is not or not exclusively responsible for the nuclear export of TIMAP. On the contrary, TIMAP seems to regulate membrane localization of eEF1A1 as the elongation factor co-localized with TIMAP in the plasma membrane fraction of control endothelial cells, but it has disappeared from the membrane in TIMAP depleted cells. It is demonstrated that membrane localization of eEF1A1 depends on the phosphorylation state of its Thr residue(s); and ROCK phosphorylated eEF1A1 is a novel substrate for TIMAP-PP1 underlining the complex regulatory role of TIMAP in the endothelium. The elongation factor seems to be involved in the regulation of endothelial cell attachment and spreading as silencing of eEF1A1 positively affected these processes which were monitored by transendothelial resistance measurements.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Endothelial cell
eEF1A1
Protein phosphatase 1
TIMAP
Megjelenés:International Journal Of Biochemistry & Cell Biology 69 (2015), p. 105-113. -
További szerzők:Péter Margit (1987-) (Ph.D. hallgató) Thalwieser Zsófia (1993-) (biológus) Kovács Előd Csortos Csilla (1956-) (biokémikus)
Pályázati támogatás:TÁMOP-4.2.2.A-11/1/KONV-2012-0025
TÁMOP
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4.

001-es BibID:BIBFORM096180
035-os BibID:(WoS)000709464800005 (Scopus)85107471683
Első szerző:Hardenberg, Maarten
Cím:Observation of an α-synuclein liquid droplet state and its maturation into Lewy body-like assemblies / Maarten C. Hardenberg, Tessa Sinnige, Sam Casford, Samuel T. Dada, Chetan Poudel, Elizabeth A. Robinson, Monika Fuxreiter, Clemens F. Kaminksi, Gabriele S. Kaminski-Schierle, Ellen A. A. Nollen, Christopher M. Dobson, Michele Vendruscolo
Dátum:2021
ISSN:1674-2788 1759-4685
Megjegyzések:Misfolded α-synuclein is a major component of Lewy bodies, which are a hallmark of Parkinson's disease (PD). A large body of evidence shows that α-synuclein can aggregate into amyloid fibrils, but the relationship between α-synuclein self-assembly and Lewy body formation remains unclear. Here, we show, both in vitro and in a Caenorhabditis elegans model of PD, that α-synuclein undergoes liquid?liquid phase separation by forming a liquid droplet state, which converts into an amyloid-rich hydrogel with Lewy-body-like properties. This maturation process towards the amyloid state is delayed in the presence of model synaptic vesicles in vitro. Taken together, these results suggest that the formation of Lewy bodies may be linked to the arrested maturation of α-synuclein condensates in the presence of lipids and other cellular components.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Parkinson's disease
liquid?liquid phase separation
α-synuclein
Megjelenés:Journal of Molecular Cell Biology. - 13 : 4 (2021), p. 282-294. -
További szerzők:Sinnige, Tessa Casford, Sam Dada, Samuel T. Poudel, Chetan Robinson, Elizabeth A. Fuxreiter Mónika (1969-) (kutató vegyész) Kaminksi, Clemens F. Kaminski-Schierle, Gabriele S. Nollen, Ellen A. A. Dobson, Christopher M. Vendruscolo, Michele
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5.

001-es BibID:BIBFORM074369
035-os BibID:(WoS)000446007700011 (Scopus)85054070208
Első szerző:Karányi Zsolt (biostatisztikus, bioinformatikus)
Cím:Nuclear dynamics of the Set1C subunit Spp1 prepares meiotic recombination sites for break formation / Zsolt Karányi, László Halász, Laurent Acquaviva, Dávid Jónás, Szabolcs Hetey, Beáta Boros-Oláh, Feng Peng, Doris Chen, Franz Klein, Vincent Géli, Lóránt Székvölgyi
Dátum:2018
ISSN:0021-9525
Megjegyzések:Spp1 is the H3K4me3 reader subunit of the Set1 complex (COMPASS/Set1C) that contributes to the mechanism by which meiotic DNA break sites (DSBs) are mechanistically selected. We previously proposed a model in which Spp1 interacts with H3K4me3 and the chromosome axis protein Mer2 that leads to DSB formation. Here we show that spatial interactions of Spp1 and Mer2 occur independently of Set1C. Spp1 exhibits dynamic chromatin binding features during meiosis with many de novo appearing and disappearing binding sites. Spp1 chromatin binding dynamics depends on its PHD finger and Mer2-interacting domain, and on modifiable histone residues (H3R2/K4). Remarkably, association of Spp1 with Mer2 axial sites reduces the effective turnover rate and diffusion coefficient of Spp1 upon chromatin binding, compared to other Set1C subunits. Our results indicate that "chromosomal turnover rate" is a major molecular determinant of Spp1 function in the framework of meiotic chromatin structure that prepares recombination initiation sites for break formation.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
recombination
meiosis
COMPASS/Set1C
ChIP
chromatin structure
Megjelenés:Journal of Cell Biology. - 217 : 10 (2018), p. 3398-3415. -
További szerzők:Halász László (1989-) (molekuláris biológus) Acquaviva, Laurent Jonás Dávid Hetey Szabolcs Boros-Oláh Beáta (1989-) (molekuláris biológus) Peng, Feng Chen, Doris Klein, Franz Géli, Vincent Székvölgyi Lóránt (1977-) (biofizikus, biokémikus, sejtbiológus)
Pályázati támogatás:NKFIH-ERC-HU-117670
NKFIH
GINOP-2.3.2-15-2016-00024
GINOP
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6.

001-es BibID:BIBFORM002145
Első szerző:Kosztáczky Béla (orvos)
Cím:Leptin stimulates endogenous cholesterol synthesis in human monocytes : new role of an old player in atherosclerotic plaque formation / Kosztáczky Béla, Fóris Gabriella, ifj. Paragh György, Seres Ildikó, Zsíros Emese, Koncsos Péter, Balogh Zoltán, Paragh György
Dátum:2007
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:The International Journal of Biochemistry and Cell Biology. - 39 : 9 (2007), p. 1637-1645. -
További szerzők:Fóris Gabriella (1937-) (belgyógyász) Paragh György Jr. (1978-) (bőrgyógyász) Seres Ildikó (1954-) (biokémikus) Zsíros Emese (1980-) (orvos) Koncsos Péter (1982-) (belgyógyász) Balogh Zoltán (1965-) (belgyógyász, gasztroenterológus, diabetológus) Paragh György (1953-) (belgyógyász)
Internet cím:elektronikus változat
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7.

001-es BibID:BIBFORM099848
035-os BibID:(cikkazonosító)e201910132 (WoS)000573632300003 (Scopus)85088158064
Első szerző:Zagryazhskaya-Masson, Anna
Cím:Intersection of TKS5 and FGD1/CDC42 signaling cascades directs the formation of invadopodia / Zagryazhskaya-Masson Anna, Monteiro Pedro, Macé Anne-Sophie, Castagnino Alessia, Ferrari Robin, Infante Elvira, Duperray-Susini Aléria, Dingli Florent, Lanyi Arpad, Loew Damarys, Génot Elisabeth, Chavrier Philippe
Dátum:2020
ISSN:0021-9525
Megjegyzések:Tumor cells exposed to a physiological matrix of type I collagen fibers form elongated collagenolytic invadopodia, which differ from dotty-like invadopodia forming on the gelatin substratum model. The related scaffold proteins, TKS5 and TKS4, are key components of the mechanism of invadopodia assembly. The molecular events through which TKS proteins direct collagenolytic invadopodia formation are poorly defined. Using coimmunoprecipitation experiments, identification of bound proteins by mass spectrometry, and in vitro pull-down experiments, we found an interaction between TKS5 and FGD1, a guanine nucleotide exchange factor for the Rho-GTPase CDC42, which is known for its role in the assembly of invadopodial actin core structure. A novel cell polarity network is uncovered comprising TKS5, FGD1, and CDC42, directing invadopodia formation and the polarization of MT1-MMP recycling compartments, required for invadopodia activity and invasion in a 3D collagen matrix. Additionally, our data unveil distinct signaling pathways involved in collagenolytic invadopodia formation downstream of TKS4 or TKS5 in breast cancer cells.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Journal Of Cell Biology. - 219 : 9 (2020), p. 1-18. -
További szerzők:Monteiro, Pedro Macé, Anne-Sophie Castagnino, Alessia Ferrari, Robin Infante, Elvira Duperray-Susini, Aléria Dingli, Florent Lányi Árpád (1962-) (biológus, immunológus) Loew, Damarys Génot, Elisabeth Chavrier, Philippe
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