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001-es BibID:	BIBFORM071407
Első szerző:	Boratkó Anita (biokémikus, molekuláris biológus)
Cím:	TIMAP, the versatile protein phosphatase 1 regulator in endothelial cells / Boratkó Anita, Csortos Csilla
Dátum:	2017
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	IUBMB Life. - 69 : 12 (2017), p. 918-928. -
További szerzők:	Csortos Csilla (1956-) (biokémikus)
Pályázati támogatás:	PD116262 OTKA
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM004729
Első szerző:	Heilmeyer, Ludwig M. G. Jr.
Cím:	Mammalian phosphatidylinositol 4-kinases / Heilmeyer, L. M. G. Jr., Vereb, G. Jr., Vereb, G., Kakuk, A., Szivak, I.
Dátum:	2003
ISSN:	521-6543 (Print)
Megjegyzések:	Three phosphatidylinositol 4-kinase isoforms, PI4K 230, 92 and 55 have been cloned and sequenced allowing a much wider characterization than the previously employed enzymological typing into type II and III enzymes. PI4K 230 and 92 contain a highly conserved catalytic core, PI4K55 one with a much lower degree of similarity. Candidate kinase motifs, deduced from the protein kinase super family, are absolutely conserved in all isoforms. Kinase activities are described based on their sensitivity and reactivity towards wortmannin, phenylarsine oxide (PAO) and 5'-p-fluorosulfonylbenzoyladenosine (FSBA). Localization of all isoforms in the cell is reported. All enzymes contain nuclear localization and export sequence motifs (NLS and NES) leading to the expectation that they can be transferred to the nucleus. PI4K230 has been found in the nucleolus, PI4K92 in the nucleus, additionally further broadening the function of these enzymes. In the cytoplasm of neuronal cells, PI4K230 is distributed evenly on membranes that are ultra structurally cisterns of the rough endoplasmatic reticulum, outer membranes of mitochondria, multivesicular bodies, and are in close vicinity of synaptic contacts. PI4K92 is functionally characterized as a key enzyme regulating Golgi disintegration/reorganization during mitosis probably via phosphorylation by cyclin-dependent kinases on well-defined sites. PI4K55 is involved in the production of second messengers, diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (InsP3) at the plasma membrane, moreover, in the endocytotic pathway in the cytoplasm
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban 1-Phosphatidylinositol 4-Kinase Animals Cells Cytoplasm Enzymes genetics Humans Inositol 1,4,5-Trisphosphate metabolism Mitochondria Mitosis Phosphorylation Protein Isoforms Rats Research Support
Megjelenés:	IUBMB Life 55 : 2 (2003), p. 59-65. -
További szerzők:	Vereb György (1965-) (biofizikus, orvos) Vereb György (1938-) (biokémikus, sejtbiológus) Kakuk Annamária (1976-) (molekuláris biológus) Szivák Ilona
Internet cím:	elektronikus változat elektronikus változat DOI
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001-es BibID:	BIBFORM095937
Első szerző:	Király Nikolett (molekuláris biológus, biokémikus)
Cím:	Dephosphorylation of annexin A2 by protein phosphatase 1 regulates endothelial cell barrier / Nikolett Király, Zsófia Thalwieser, Márton Fonódi, Csilla Csortos, Anita Boratkó
Dátum:	2021
ISSN:	1521-6543 1521-6551
Megjegyzések:	Annexin A2 (ANXA2) is a multifunctional protein expressed in nearly all human tissues and cell types, playing a role in various signaling pathways. It is subjected to phosphorylation, but no specific protein phosphatase has been identified in its posttranslational regulation yet. Using pull down assay followed by LC-MS/MS analysis we found that ANXA2 interacts with TIMAP (TGF-beta-inhibited membrane-associated protein) in pulmonary artery endothelial cells. TIMAP is highly expressed in endothelial cells, where it acts as a regulatory and targeting subunit of protein phosphatase 1 (PP1). TIMAP plays an important role in the regulation of the endothelial barrier maintenance through the dephosphorylation of its several substrate proteins. In the present work phosphorylation of Ser25 side chain in ANXA2 by PKC was shown both in vivo and in vitro. Phosphorylation level of ANXA2 at Ser25 increased greatly by inhibition of PP1 and by depletion of its regulatory subunit, TIMAP, implying a role of this PP1 holoenzyme in the dephosphorylation of ANXA2. Immunofluorescence staining and subcellular fractionations revealed a diffuse subcellular localization for the endogenous ANXA2, but phospho-Ser25 ANXA2 was mainly detected in the membrane. ANXA2 depletion lowered the basal endothelial barrier and inhibited cell migration, but had no significant effect on cell proliferation or viability. ANXA2 depleted cells failed to respond to PMA treatment, indicating an intimately involvement of phosphoANXA2 in PKC signaling. Moreover, phosphorylation of ANXA2 disrupted its interaction with S100A10 suggesting a phosphorylation dependent multiple regulatory role of ANXA2 in endothelial cells. Our results demonstrate the pivotal role of PKC-ANXA2-PP1 pathway in endothelial cell signaling, especially in barrier function and cell migration.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk protein dephosphorylation protein phosphatase 1 annexin A2 PKC
Megjelenés:	IUBMB Life. - 2021 (2021), p. 1-12. -
További szerzők:	Thalwieser Zsófia (1993-) (biológus) Fonódi Márton (1995-) (molekuláris biológus) Csortos Csilla (1956-) (biokémikus) Boratkó Anita (1985-) (biokémikus, molekuláris biológus)
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM042252
Első szerző:	Pancsa Rita
Cím:	Interactions via intrinsically disordered regions : what kind of motifs? / Rita Pancsa, Monika Fuxreiter
Dátum:	2012
ISSN:	1521-6543
Megjegyzések:	Proteins containing intrinsically disordered (ID) regions are widespread in eukaryotic organisms and are mostly utilized in regulatory processes. ID regions can mediate binary interactions of proteins or promote organization of large assemblies. Post-translational modifications of ID regions often serve as decision points in signaling pathways. Why Nature distinguished ID proteins in molecular recognition functions? In a simple view, binding of ID regions is accompanied by a large entropic penalty as compared to folded proteins. Even in complexes however, ID regions can preserve their conformational freedom, thereby recruit further partners and perform various functions. What sort of benefits ID regions offer for molecular interactions and which properties are exploited in the corresponding complexes? Here, we review models explaining the recognition mechanisms of ID proteins. Motif-based interactions are central to all proposed scenarios, including prestructured elements, anchoring sites and linear motifs. We aim to extract consensus features of the models, which could be used to predict ID-binding sites for a variety of partners.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Molekuláris Medicina
Megjelenés:	Iubmb Life. - 64 : 6 (2012), p. 513-520. -
További szerzők:	Fuxreiter Mónika (1969-) (kutató vegyész)
Pályázati támogatás:	TÁMOP-4.2.1/B-09/1/KONV-2010-0007 TÁMOP Az apoptózis és a fagocitózis folyamatának összehangolása a szövetet tönkretevő gyulladási reakciók elkerülésére
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