@article{MTMT:34747207,
	title = {Ünnepelt a Debreceni Egyetem Orvosi Vegytani Intézete: 70 éves Dombrádi Viktor és Erdődi Ferenc},
	url = {https://m2.mtmt.hu/api/publication/34747207},
	author = {Lontay, Beáta},
	journal-iso = {BIOKÉMIA},
	journal = {BIOKÉMIA: A MAGYAR BIOKÉMIAI EGYESÜLET FOLYÓIRATA},
	volume = {XLVIII},
	unique-id = {34747207},
	issn = {0133-8455},
	year = {2024},
	eissn = {2060-8152},
	pages = {96-100}
}

@article{MTMT:33699950,
	title = {Phosphorylated Peptide Derived from the Myosin Phosphatase Target Subunit Is a Novel Inhibitor of Protein Phosphatase-1},
	url = {https://m2.mtmt.hu/api/publication/33699950},
	author = {Kónya, Zoltán and Tamás, István and Bécsi, Bálint and Lontay, Beáta and Hadháziné Raics, Mária and Timári, István and E Kövér, Katalin and Erdődi, Ferenc},
	doi = {10.3390/ijms24054789},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {24},
	unique-id = {33699950},
	issn = {1661-6596},
	abstract = {Identification of specific protein phosphatase-1 (PP1) inhibitors is of special importance regarding the study of its cellular functions and may have therapeutic values in diseases coupled to signaling processes. In this study, we prove that a phosphorylated peptide of the inhibitory region of myosin phosphatase (MP) target subunit (MYPT1), R690QSRRS(pT696)QGVTL701 (P-Thr696-MYPT1690−701), interacts with and inhibits the PP1 catalytic subunit (PP1c, IC50 = 3.84 µM) and the MP holoenzyme (Flag-MYPT1-PP1c, IC50 = 3.84 µM). Saturation transfer difference NMR measurements established binding of hydrophobic and basic regions of P-Thr696-MYPT1690−701 to PP1c, suggesting interactions with the hydrophobic and acidic substrate binding grooves. P-Thr696-MYPT1690−701 was dephosphorylated by PP1c slowly (t1/2 = 81.6–87.9 min), which was further impeded (t1/2 = 103 min) in the presence of the phosphorylated 20 kDa myosin light chain (P-MLC20). In contrast, P-Thr696-MYPT1690−701 (10–500 µM) slowed down the dephosphorylation of P-MLC20 (t1/2 = 1.69 min) significantly (t1/2 = 2.49–10.06 min). These data are compatible with an unfair competition mechanism between the inhibitory phosphopeptide and the phosphosubstrate. Docking simulations of the PP1c-P-MYPT1690−701 complexes with phosphothreonine (PP1c-P-Thr696-MYPT1690−701) or phosphoserine (PP1c-P-Ser696-MYPT1690−701) suggested their distinct poses on the surface of PP1c. In addition, the arrangements and distances of the surrounding coordinating residues of PP1c around the phosphothreonine or phosphoserine at the active site were distinct, which may account for their different hydrolysis rate. It is presumed that P-Thr696-MYPT1690−701 binds tightly at the active center but the phosphoester hydrolysis is less preferable compared to P-Ser696-MYPT1690−701 or phosphoserine substrates. Moreover, the inhibitory phosphopeptide may serve as a template to synthesize cell permeable PP1-specific peptide inhibitors.},
	keywords = {Molecular docking; saturation transfer difference NMR; protein phosphatase-1 (PP1); myosin phosphatase (MP); myosin phosphatase target subunit-1 (MYPT1); MYPT1 inhibitory peptide (P-Thr696-MYPT1690-701)},
	year = {2023},
	eissn = {1422-0067},
	orcid-numbers = {Timári, István/0000-0003-0504-6967}
}

@article{MTMT:33151445,
	title = {The Structural Effects of Phosphorylation of Protein Arginine Methyltransferase 5 on Its Binding to Histone H4},
	url = {https://m2.mtmt.hu/api/publication/33151445},
	author = {Börzsei, Rita and Bayarsaikhan, Bayartsetseg and Zsidó, Balázs Zoltán and Lontay, Beáta and Hetényi, Csaba},
	doi = {10.3390/ijms231911316},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {23},
	unique-id = {33151445},
	issn = {1661-6596},
	abstract = {The protein arginine methyltransferase 5 (PRMT5) enzyme is responsible for arginine methylation on various proteins, including histone H4. PRMT5 is a promising drug target, playing a role in the pathomechanism of several diseases, especially in the progression of certain types of cancer. It was recently proved that the phosphorylation of PRMT5 on T80 residue increases its methyltransferase activity; furthermore, elevated levels of the enzyme were measured in the case of human hepatocellular carcinoma and other types of tumours. In this study, we constructed the complexes of the unmodified human PRMT5-methylosome protein 50 (MEP50) structure and its T80-phosphorylated variant in complex with the full-length histone H4 peptide. The full-length histone H4 was built in situ into the human PRMT5-MEP50 enzyme using experimental H4 fragments. Extensive molecular dynamic simulations and structure and energy analyses were performed for the complexed and apo protein partners, as well. Our results provided an atomic level explanation for two important experimental findings: (1) the increased methyltransferase activity of the phosphorylated PRMT5 when compared to the unmodified type; (2) the PRMT5 methylates only the free form of histone H4 not bound in the nucleosome. The atomic level complex structure H4-PRMT5-MEP50 will help the design of new inhibitors and in uncovering further structure–function relationships of PRMT enzymes.},
	year = {2022},
	eissn = {1422-0067}
}

@article{MTMT:32806727,
	title = {Mechanisms by which smoothelin-like protein 1 reverses insulin resistance in myotubules and mice},
	url = {https://m2.mtmt.hu/api/publication/32806727},
	author = {Tamás, István and Major, Evelin and Horváth, Dániel and Keller, Ilka and Ungvári , Ádám and Haystead, Timothy A. and MacDonald, Justin A. and Lontay, Beáta},
	doi = {10.1016/j.mce.2022.111663},
	journal-iso = {MOL CELL ENDOCRINOL},
	journal = {MOLECULAR AND CELLULAR ENDOCRINOLOGY},
	volume = {551},
	unique-id = {32806727},
	issn = {0303-7207},
	year = {2022},
	eissn = {1872-8057},
	orcid-numbers = {MacDonald, Justin A./0000-0002-9238-8473}
}

@article{MTMT:32282625,
	title = {Smoothelin-like protein 1 regulates development and metabolic transformation of skeletal muscle in hyperthyroidism},
	url = {https://m2.mtmt.hu/api/publication/32282625},
	author = {Major, Evelin and Győry, Ferenc and Horváth, Dániel and Keller, Ilka and Tamás, István and Uray (Davis), Karen L. and Fülöp, Péter and Lontay, Beáta},
	doi = {10.3389/fendo.2021.751488},
	journal-iso = {FRONT ENDOCRINOL},
	journal = {FRONTIERS IN ENDOCRINOLOGY},
	volume = {12},
	unique-id = {32282625},
	issn = {1664-2392},
	abstract = {Hyperthyroidism triggers a glycolytic shift in skeletal muscle (SKM) by altering the expression of metabolic proteins, which is often accompanied by peripheral insulin resistance. Our previous results show that smoothelin-like protein 1 (SMTNL1), a transcriptional co-regulator, promotes insulin sensitivity in SKM. Our aim was to elucidate the role of SMTNL1 in SKM under physiological and pathological 3,3 ',5-Triiodo-L-thyronine (T3) concentrations. Human hyper- and euthyroid SKM biopsies were used for microarray analysis and proteome profiler arrays. Expression of genes related to energy production, nucleic acid- and lipid metabolism was changed significantly in hyperthyroid samples. The phosphorylation levels and activity of AMPK alpha 2 and JNK were increased by 15% and 23%, respectively, in the hyperthyroid samples compared to control. Moreover, SMTNL1 expression showed a 6-fold decrease in the hyperthyroid samples and in T3-treated C2C12 cells. Physiological and supraphysiological concentrations of T3 were applied on differentiated C2C12 cells upon SMTNL1 overexpression to assess the activity and expression level of the elements of thyroid hormone signaling, insulin signaling and glucose metabolism. Our results demonstrate that SMTNL1 selectively regulated TR alpha expression. Overexpression of SMTNL1 induced insulin sensitivity through the inhibition of JNK activity by 40% and hampered the non-genomic effects of T3 by decreasing the activity of ERK1/2 through PKC delta. SMTNL1 overexpression reduced IRS1 Ser307 and Ser612 phosphorylation by 52% and 53%, respectively, in hyperthyroid model to restore the normal responsiveness of glucose transport to insulin. SMTNL1 regulated glucose phosphorylation and balances glycolysis and glycogen synthesis via the downregulation of hexokinase II by 1.3-fold. Additionally, mitochondrial respiration and glycolysis were measured by SeaHorse analysis to determine cellular metabolic function/phenotype of our model system in real-time. T3 overload strongly increased the rate of acidification and a shift to glycolysis, while SMTNL1 overexpression antagonizes the T3 effects. These lines of evidence suggest that SMTNL1 potentially prevents hyperthyroidism-induced changes in SKM, and it holds great promise as a novel therapeutic target in insulin resistance.},
	year = {2021},
	eissn = {1664-2392}
}

@article{MTMT:32242201,
	title = {Smoothelin-like Protein 1 Regulates the Thyroid Hor-Mone-Induced Homeostasis and Remodeling of C2C12 Cells via the Modulation of Myosin Phosphatase},
	url = {https://m2.mtmt.hu/api/publication/32242201},
	author = {Major, Evelin and Keller, Ilka and Horváth, Dániel and Tamás, István and Erdődi, Ferenc and Lontay, Beáta},
	doi = {10.3390/ijms221910293},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {22},
	unique-id = {32242201},
	issn = {1661-6596},
	abstract = {The pathological elevation of the active thyroid hormone (T-3) level results in the manifestation of hyperthyroidism, which is associated with alterations in the differentiation and contractile function of skeletal muscle (SKM). Myosin phosphatase (MP) is a major cellular regulator that hydrolyzes the phosphoserine of phosphorylated myosin II light chain. MP consists of an MYPT1/2 regulatory and a protein phosphatase 1 catalytic subunit. Smoothelin-like protein 1 (SMTNL1) is known to inhibit MP by directly binding to MP as well as by suppressing the expression of MYPT1 at the transcriptional level. Supraphysiological vs. physiological concentration of T-3 were applied on C2C12 myoblasts and differentiated myotubes in combination with the overexpression of SMTNL1 to assess the role and regulation of MP under these conditions. In non-differentiated myoblasts, MP included MYPT1 in the holoenzyme complex and its expression and activity was regulated by SMTNL1, affecting the phosphorylation level of MLC20 assessed using semi-quantitative Western blot analysis. SMTNL1 negatively influenced the migration and cytoskeletal remodeling of myoblasts measured by high content screening. In contrast, in myotubes, the expression of MYPT2 but not MYPT1 increased in a T-3-dependent and SMTNL1-independent manner. T-3 treatment combined with SMTNL1 overexpression impeded the activity of MP. In addition, MP interacted with Na+/K+-ATPase and dephosphorylated its inhibitory phosphorylation sites, identifying this protein as a novel MP substrate. These findings may help us gain a better understanding of myopathy, muscle weakness and the disorder of muscle regeneration in hyperthyroid patients.},
	keywords = {Thyroid hormone; myogenesis; Na+/K+-ATPase; MYOSIN PHOSPHATASE; SMTNL1},
	year = {2021},
	eissn = {1422-0067}
}

@{MTMT:31678760,
	title = {The interaction between PAK1 and CXCL1 in the development of ileus},
	url = {https://m2.mtmt.hu/api/publication/31678760},
	author = {Gergely, B and Sipos, Ádám and Docsa, Tibor and Lontay, Beáta and Varga, L and Uray (Davis), Karen L.},
	booktitle = {Proceedings of the EFOP-3.6.2-16-2017-00006 (LIVE LONGER) project},
	unique-id = {31678760},
	year = {2020},
	pages = {64-64}
}

@{MTMT:31678751,
	title = {Effects of hyperpolarization activated cyclic nucleotide gated potassium and sodium channel 2 (HCN2) on intestinal motility},
	url = {https://m2.mtmt.hu/api/publication/31678751},
	author = {Sipos, Ádám and Gergely, B and Docsa, Tibor and Lontay, Beáta and Varga, L and Uray (Davis), Karen L.},
	booktitle = {Proceedings of the EFOP-3.6.2-16-2017-00006 (LIVE LONGER) project},
	unique-id = {31678751},
	year = {2020},
	pages = {65-65}
}

@{MTMT:31678735,
	title = {The regulation of Na+-K+-ATPase by myosin phosphatase in smooth muscle},
	url = {https://m2.mtmt.hu/api/publication/31678735},
	author = {Horváth, Dániel and Tamás, István and Docsa, Tibor and Uray (Davis), Karen L. and Lontay, Beáta},
	booktitle = {Proceedings of the EFOP-3.6.2-16-2017-00006 (LIVE LONGER) project},
	unique-id = {31678735},
	year = {2020},
	pages = {98-98}
}

@article{MTMT:31408798,
	title = {MicroRNA Regulatory Pathways in the Control of the Actin–Myosin Cytoskeleton},
	url = {https://m2.mtmt.hu/api/publication/31408798},
	author = {Uray (Davis), Karen L. and Major, Evelin and Lontay, Beáta},
	doi = {10.3390/cells9071649},
	journal-iso = {CELLS-BASEL},
	journal = {CELLS},
	volume = {9},
	unique-id = {31408798},
	year = {2020},
	eissn = {2073-4409}
}