@article{MTMT:34573513,
	title = {PP2A Affects Angiogenesis via Its Interaction with a Novel Phosphorylation Site of TSP1},
	url = {https://m2.mtmt.hu/api/publication/34573513},
	author = {Thalwieser, Zsófia and Fonódi, Márton and Király, Nikolett and Csortos, Csilla and Boratkó, Anita},
	doi = {10.3390/ijms25031844},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {25},
	unique-id = {34573513},
	issn = {1661-6596},
	abstract = {Alterations in angiogenic properties play a pivotal role in the manifestation and onset of various pathologies, including vascular diseases and cancer. Thrombospondin-1 (TSP1) protein is one of the master regulators of angiogenesis. This study unveils a novel aspect of TSP1 regulation through reversible phosphorylation. The silencing of the B55α regulatory subunit of protein phosphatase 2A (PP2A) in endothelial cells led to a significant decrease in TSP1 expression. Direct interaction between TSP1 and PP2A-B55α was confirmed via various methods. Truncated TSP1 constructs were employed to identify the phosphorylation site and the responsible kinase, ultimately pinpointing PKC as the enzyme phosphorylating TSP1 on Ser93. The biological effects of B55α–TSP1 interaction were also analyzed. B55α silencing not only counteracted the increase in TSP1 expression during wound closure but also prolonged wound closure time. Although B55α silenced cells initiated tube-like structures earlier than control cells, their spheroid formation was disrupted, leading to disintegration. Cells transfected with phosphomimic TSP1 S93D exhibited smaller spheroids and reduced effectiveness in tube formation, revealing insights into the effects of TSP1 phosphorylation on angiogenic properties. In this paper, we introduce a new regulatory mechanism of angiogenesis by reversible phosphorylation on TSP1 S93 by PKC and PP2A B55α.},
	year = {2024},
	eissn = {1422-0067},
	pages = {1844}
}

@article{MTMT:34430018,
	title = {TIMAP, a Regulatory Subunit of Protein Phosphatase 1, Inhibits In Vitro Neuronal Differentiation},
	url = {https://m2.mtmt.hu/api/publication/34430018},
	author = {Fonódi, Márton and Thalwieser, Zsófia and Csortos, Csilla and Boratkó, Anita},
	doi = {10.3390/ijms242417360},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {24},
	unique-id = {34430018},
	issn = {1661-6596},
	abstract = {TIMAP (TGF-β-inhibited membrane associated protein) is abundant in endothelial cells, and it has been regarded as a member of the myosin phosphatase targeting protein (MYPT) family. Our workgroup previously identified several interacting protein partners of TIMAP and proved its regulatory subunit role for protein phosphatase 1 catalytic subunit (PP1c). TIMAP is also expressed in neuronal cells, but details of its function have not been studied yet. Therefore, we aimed to explore the role of TIMAP in neuronal cells, especially during differentiation. Expression of TIMAP was proved both at mRNA and protein levels in SH-SY5Y human neuroblastoma cells. Differentiation of SH-SY5Y cells was optimized and proved by the detection of neuronal differentiation markers, such as β3-tubulin, nestin and inhibitor of differentiation 1 (ID1) using qPCR and Western blot. We found downregulation of TIMAP during differentiation. In accordance with this, overexpression of recombinant TIMAP attenuated the differentiation of neuronal cells. Moreover, the subcellular localization of TIMAP has changed during differentiation as it translocated from the plasma membrane into the nucleus. The nuclear interactome of TIMAP revealed more than 50 proteins, offering the possibility to further investigate the role of TIMAP in several key physiological pathways of neuronal cells.},
	year = {2023},
	eissn = {1422-0067}
}

@article{MTMT:32124402,
	title = {Dephosphorylation of annexin A2 by protein phosphatase 1 regulates endothelial cell barrier},
	url = {https://m2.mtmt.hu/api/publication/32124402},
	author = {Király, Nikolett and Thalwieser, Zsófia and Fonódi, Márton and Csortos, Csilla and Boratkó, Anita},
	doi = {10.1002/iub.2538},
	journal-iso = {IUBMB LIFE},
	journal = {IUBMB LIFE},
	volume = {2021},
	unique-id = {32124402},
	issn = {1521-6543},
	year = {2021},
	eissn = {1521-6551},
	pages = {1257-1268}
}

@article{MTMT:32124398,
	title = {Ser69 phosphorylation of TIMAP affects endothelial cell migration},
	url = {https://m2.mtmt.hu/api/publication/32124398},
	author = {Király, Nikolett and Csortos, Csilla and Boratkó, Anita},
	doi = {10.1080/01902148.2021.1960651},
	journal-iso = {EXP LUNG RES},
	journal = {EXPERIMENTAL LUNG RESEARCH},
	volume = {47},
	unique-id = {32124398},
	issn = {0190-2148},
	abstract = {TIMAP (TGF-β-inhibited membrane-associated protein) is a regulatory subunit of protein phosphatase 1 (PP1). The N-terminal region contains a binding motif for the catalytic subunit of PP1 (PP1c) and a nuclear localization signal (NLS). Phosphorylation of TIMAP on Ser331, Ser333 and Ser337 side chains was shown to regulate the activity of the TIMAP-PP1c complex. Several studies, however, reported an additional side chain of TIMAP. Ser69 is located near to the PP1c binding motif and NLS, therefore, we hypothesized that the phosphorylation of this side chain perhaps may regulate the interaction between TIMAP and PP1c, or may affect the nuclear transport of TIMAP. Materials and Methods: To study the significance of Ser69 phosphorylation, GST-tagged or c-myc-tagged wild type, phosphomimic S69D and phosphonull S69A recombinant TIMAP proteins were expressed in bacteria or endothelial cells, respectively. Protein-protein interactions of the wild type or mutant forms of TIMAP were studied by pull-down and Western blot. Localization of TIMAP S69 mutants in pulmonary artery endothelial cells was detected by immunofluorescent staining and expression and localization of the recombinants were investigated by subcellular fractionation and Western blot. Results: Modifications of Ser69 of TIMAP had no effect on binding of PP1c, ERM or RACK1. However, S69D TIMAP showed enhanced membrane localization and an increased number of membrane protrusions were observed in the cells overexpressing this phosphomimic mutant. Furthermore, significantly faster wound healing and migration rate of the S69D mutant overexpressing cells were detected by endothelial barrier resistance measurements (ECIS). Specific interaction was shown between TIMAP and polo-like kinase 4 (PLK4), a potential kinase to phosphorylate Ser69. Conclusions: Altogether, our results indicate that Ser69 phosphorylation by PLK4 may evoke an enrichment of TIMAP in the plasma membrane region and may play an important role in endothelial cell migration without affecting the PP1c binding ability of TIMAP.},
	keywords = {PHOSPHATASE; PHOSPHORYLATION; ENDOTHELIUM; cell migration; TIMAP},
	year = {2021},
	eissn = {1521-0499},
	pages = {334-343}
}

@article{MTMT:30929385,
	title = {Protein phosphatase 2A-mediated flotillin-1 dephosphorylation up-regulates endothelial cell migration and angiogenesis regulation},
	url = {https://m2.mtmt.hu/api/publication/30929385},
	author = {Thalwieser, Zsófia and Király, Nikolett and Fonódi, Márton and Csortos, Csilla and Boratkó, Anita},
	doi = {10.1074/jbc.RA119.007980},
	journal-iso = {J BIOL CHEM},
	journal = {JOURNAL OF BIOLOGICAL CHEMISTRY},
	volume = {294},
	unique-id = {30929385},
	issn = {0021-9258},
	year = {2019},
	eissn = {1083-351X},
	pages = {20196-20206}
}

@article{MTMT:3291997,
	title = {TIMAP, the versatile protein phosphatase 1 regulator in endothelial cells},
	url = {https://m2.mtmt.hu/api/publication/3291997},
	author = {Boratkó, Anita and Csortos, Csilla},
	doi = {10.1002/iub.1695},
	journal-iso = {IUBMB LIFE},
	journal = {IUBMB LIFE},
	volume = {69},
	unique-id = {3291997},
	issn = {1521-6543},
	year = {2017},
	eissn = {1521-6551},
	pages = {918-928}
}

@article{MTMT:3152378,
	title = {PKC mediated phosphorylation of TIMAP regulates PP1c activity and endothelial barrier function},
	url = {https://m2.mtmt.hu/api/publication/3152378},
	author = {Boratkó, Anita and Csortos, Csilla},
	doi = {10.1016/j.bbamcr.2016.12.001},
	journal-iso = {BBA-MOL CELL RES},
	journal = {BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH},
	volume = {1864},
	unique-id = {3152378},
	issn = {0167-4889},
	year = {2017},
	eissn = {1879-2596},
	pages = {431-439}
}

@article{MTMT:3144986,
	title = {Regulation of merlin by protein phosphataswe 1-TIMAP and EBP50 in endothelial cells},
	url = {https://m2.mtmt.hu/api/publication/3144986},
	author = {Boratkó, Anita and Péter, Margit and Csortos, Csilla},
	doi = {10.1016/j.biocel.2016.11.010},
	journal-iso = {INT J BIOCHEM CELL B},
	journal = {INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY},
	volume = {82},
	unique-id = {3144986},
	issn = {1357-2725},
	year = {2017},
	eissn = {1878-5875},
	pages = {10-17}
}

@article{MTMT:3068290,
	title = {Role of human corneal stroma-derived mesenchymal-like stem cells in corneal immunity and wound healing},
	url = {https://m2.mtmt.hu/api/publication/3068290},
	author = {Veréb, Zoltán and Póliska, Szilárd and Albert, Réka and Olstad, OK and Boratkó, Anita and Csortos, Csilla and Moe, MC and Facskó, Andrea and Petrovski, Goran},
	doi = {10.1038/srep26227},
	journal-iso = {SCI REP},
	journal = {SCIENTIFIC REPORTS},
	volume = {6},
	unique-id = {3068290},
	issn = {2045-2322},
	year = {2016},
	eissn = {2045-2322},
	orcid-numbers = {Veréb, Zoltán/0000-0002-9518-2155}
}

@article{MTMT:3015616,
	title = {TIMAP-protein phosphatase 1-complex controls endothelin-1 production via ECE-1 dephosphorylation},
	url = {https://m2.mtmt.hu/api/publication/3015616},
	author = {Boratkó, Anita and Veréb, Zoltán and Petrovski, Goran and Csortos, Csilla},
	doi = {10.1016/j.biocel.2016.01.016},
	journal-iso = {INT J BIOCHEM CELL B},
	journal = {INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY},
	volume = {73},
	unique-id = {3015616},
	issn = {1357-2725},
	year = {2016},
	eissn = {1878-5875},
	pages = {11-18},
	orcid-numbers = {Veréb, Zoltán/0000-0002-9518-2155}
}