@misc{MTMT:34768197,
	title = {The regulatory role of the CD2AP/TKS4 interaction in EMT and its potential as a biomarker for colon cancer},
	url = {https://m2.mtmt.hu/api/publication/34768197},
	author = {Kurilla, Anita and László, Loretta and Takács, Tamás and Tilajka, Álmos and Laura, Lukacs and Julianna, Novak and Pancsa, Rita and Buday, László and Vas, Virág},
	unique-id = {34768197},
	year = {2023},
	orcid-numbers = {László, Loretta/0000-0003-0367-4900; Pancsa, Rita/0000-0003-0849-9312; Buday, László/0000-0003-3518-5757}
}

@article{MTMT:34266900,
	title = {Studying the Association of TKS4 and CD2AP Scaffold Proteins and Their Implications in the Partial Epithelial–Mesenchymal Transition (EMT) Process},
	url = {https://m2.mtmt.hu/api/publication/34266900},
	author = {Kurilla, Anita and László, Loretta and Takács, Tamás and Tilajka, Álmos and Lukács, L. and Novák, J. and Pancsa, Rita and Buday, László and Vas, Virág},
	doi = {10.3390/ijms242015136},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {24},
	unique-id = {34266900},
	issn = {1661-6596},
	year = {2023},
	eissn = {1422-0067},
	orcid-numbers = {László, Loretta/0000-0003-0367-4900; Pancsa, Rita/0000-0003-0849-9312; Buday, László/0000-0003-3518-5757}
}

@article{MTMT:33121755,
	title = {Structural insights into the pSer/pThr dependent regulation of the SHP2 tyrosine phosphatase in insulin and CD28 signaling},
	url = {https://m2.mtmt.hu/api/publication/33121755},
	author = {Zeke, András and Takács, Tamás and Sok, Péter Dániel and Németh, Krisztina and Kirsch, Klára and Egri, Péter and Póti, Ádám Levente and Bento, Isabel and Tusnády, Gábor and Reményi, Attila},
	doi = {10.1038/s41467-022-32918-5},
	journal-iso = {NAT COMMUN},
	journal = {NATURE COMMUNICATIONS},
	volume = {13},
	unique-id = {33121755},
	issn = {2041-1723},
	abstract = {Serine/threonine phosphorylation of insulin receptor substrate (IRS) proteins is well known to modulate insulin signaling. However, the molecular details of this process have mostly been elusive. While exploring the role of phosphoserines, we have detected a direct link between Tyr-flanking Ser/Thr phosphorylation sites and regulation of specific phosphotyrosine phosphatases. Here we present a concise structural study on how the activity of SHP2 phosphatase is controlled by an asymmetric, dual phosphorylation of its substrates. The structure of SHP2 has been determined with three different substrate peptides, unveiling the versatile and highly dynamic nature of substrate recruitment. What is more, the relatively stable pre-catalytic state of SHP2 could potentially be useful for inhibitor design. Our findings not only show an unusual dependence of SHP2 catalytic activity on Ser/Thr phosphorylation sites in IRS1 and CD28, but also suggest a negative regulatory mechanism that may also apply to other tyrosine kinase pathways as well.},
	year = {2022},
	eissn = {2041-1723},
	orcid-numbers = {Sok, Péter Dániel/0000-0001-8963-8163; Németh, Krisztina/0000-0003-1360-7648; Kirsch, Klára/0000-0003-0484-4473; Reményi, Attila/0000-0002-8345-1311}
}

@article{MTMT:33063952,
	title = {A Novel Cell-Based Model for a Rare Disease: The Tks4-KO Human Embryonic Stem Cell Line as a Frank-Ter Haar Syndrome Model System},
	url = {https://m2.mtmt.hu/api/publication/33063952},
	author = {László, Loretta and Maczelka, Hédi and Takács, Tamás and Kurilla, Anita and Tilajka, Álmos and Buday, László and Vas, Virág and Apáti, Ágota},
	doi = {10.3390/ijms23158803},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {23},
	unique-id = {33063952},
	issn = {1661-6596},
	abstract = {Tyrosine kinase substrate with four SH3 domains (Tks4) scaffold protein plays roles in cell migration and podosome formation and regulates systemic mechanisms such as adult bone homeostasis and adipogenesis. Mutations in the Tks4 gene (SH3PXD2b) cause a rare developmental disorder called Frank-Ter Haar syndrome (FTHS), which leads to heart abnormalities, bone tissue defects, and reduced adiposity. We aimed to produce a human stem cell-based in vitro FTHS model system to study the effects of the loss of the Tks4 protein in different cell lineages and the accompanying effects on the cell signalome. To this end, we used CRISPR/Cas9 (clustered, regularly interspaced, short palindromic repeats (CRISPR)/CRISPR associated (Cas9)) to knock out the SH3PXD2b gene in the HUES9 human embryonic stem cell line (hESC), and we obtained stable homo- and heterozygous knock out clones for use in studying the potential regulatory roles of Tks4 protein in embryonic stem cell biology. Based on pluripotency marker measurements and spontaneous differentiation capacity assays, we concluded that the newly generated Tks4-KO HUES9 cells retained their embryonic stem cell characteristics. We propose that the Tks4-KO HUES9 cells could serve as a tool for further cell differentiation studies to investigate the involvement of Tks4 in the complex disorder FTHS. Moreover, we successfully differentiated all of the clones into mesenchymal stem cells (MSCs). The derived MSC cultures showed mesenchymal morphology and expressed MSC markers, although the expression levels of mesodermal and osteogenic marker genes were reduced, and several EMT (epithelial mesenchymal transition)-related features were altered in the Tks4-KO MSCs. Our results suggest that the loss of Tks4 leads to FTHS by altering cell lineage differentiation and cell maturation processes, rather than by regulating embryonic stem cell potential.},
	year = {2022},
	eissn = {1422-0067},
	orcid-numbers = {László, Loretta/0000-0003-0367-4900; Maczelka, Hédi/0000-0001-6070-9343; Buday, László/0000-0003-3518-5757}
}

@article{MTMT:32020389,
	title = {Novel Roles of SH2 and SH3 Domains in Lipid Binding},
	url = {https://m2.mtmt.hu/api/publication/32020389},
	author = {Sipeki, Szabolcs and Koprivanacz, Kitti and Takács, Tamás and Kurilla, Anita and László, Loretta and Vas, Virag and Buday, László},
	doi = {10.3390/cells10051191},
	journal-iso = {CELLS-BASEL},
	journal = {CELLS},
	volume = {10},
	unique-id = {32020389},
	year = {2021},
	eissn = {2073-4409},
	orcid-numbers = {Sipeki, Szabolcs/0000-0002-9678-6743; László, Loretta/0000-0003-0367-4900; Vas, Virag/0000-0001-7249-6816; Buday, László/0000-0003-3518-5757}
}

@article{MTMT:31909245,
	title = {Recent updates on the significance of KRAS mutations in colorectal cancer biology},
	url = {https://m2.mtmt.hu/api/publication/31909245},
	author = {László, Loretta and Kurilla, Anita and Takács, Tamás and Kudlik, Gyöngyi and Koprivanacz, Kitti and Buday, László and Vas, Virág},
	doi = {10.3390/cells10030667},
	journal-iso = {CELLS-BASEL},
	journal = {CELLS},
	volume = {10},
	unique-id = {31909245},
	year = {2021},
	eissn = {2073-4409},
	orcid-numbers = {László, Loretta/0000-0003-0367-4900; Buday, László/0000-0003-3518-5757}
}

@article{MTMT:31662756,
	title = {Advances in Understanding TKS4 and TKS5: Molecular Scaffolds Regulating Cellular Processes from Podosome and Invadopodium Formation to Differentiation and Tissue Homeostasis},
	url = {https://m2.mtmt.hu/api/publication/31662756},
	author = {Kudlik, Gyöngyi and Takács, Tamás and Radnai, L. and Kurilla, Anita and Szeder, Bálint and Koprivanacz, Kitti and Merő, Balázs László and Buday, László and Vas, Virág},
	doi = {10.3390/ijms21218117},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {21},
	unique-id = {31662756},
	issn = {1661-6596},
	abstract = {Scaffold proteins are typically thought of as multi-domain "bridging molecules." They serve as crucial regulators of key signaling events by simultaneously binding multiple participants involved in specific signaling pathways. In the case of epidermal growth factor (EGF)-epidermal growth factor receptor (EGFR) binding, the activated EGFR contacts cytosolic SRC tyrosine-kinase, which then becomes activated. This process leads to the phosphorylation of SRC-substrates, including the tyrosine kinase substrates (TKS) scaffold proteins. The TKS proteins serve as a platform for the recruitment of key players in EGFR signal transduction, promoting cell spreading and migration. The TKS4 and the TKS5 scaffold proteins are tyrosine kinase substrates with four or five SH3 domains, respectively. Their structural features allow them to recruit and bind a variety of signaling proteins and to anchor them to the cytoplasmic surface of the cell membrane. Until recently, TKS4 and TKS5 had been recognized for their involvement in cellular motility, reactive oxygen species-dependent processes, and embryonic development, among others. However, a number of novel functions have been discovered for these molecules in recent years. In this review, we attempt to cover the diverse nature of the TKS molecules by discussing their structure, regulation by SRC kinase, relevant signaling pathways, and interaction partners, as well as their involvement in cellular processes, including migration, invasion, differentiation, and adipose tissue and bone homeostasis. We also describe related pathologies and the established mouse models.},
	keywords = {INVASION; Adipose Tissue; Mesenchymal Stem Cells; scaffold protein; EPITHELIAL-MESENCHYMAL TRANSITION; Tks5; Tks4; bone homeostasis; tyrosine kinase substrates},
	year = {2020},
	eissn = {1422-0067},
	orcid-numbers = {Buday, László/0000-0003-3518-5757}
}

@article{MTMT:31400188,
	title = {The effects of mutant Ras proteins on the cell signalome},
	url = {https://m2.mtmt.hu/api/publication/31400188},
	author = {Takács, Tamás and Kudlik, Gyöngyi and Kurilla, Anita and Szeder, Bálint and Buday, László and Vas, Virág},
	doi = {10.1007/s10555-020-09912-8},
	journal-iso = {CANCER METAST REV},
	journal = {CANCER AND METASTASIS REVIEWS},
	volume = {39},
	unique-id = {31400188},
	issn = {0167-7659},
	abstract = {The genetic alterations in cancer cells are tightly linked to signaling pathway dysregulation. Ras is a key molecule that controls several tumorigenesis-related processes, and mutations in RAS genes often lead to unbiased intensification of signaling networks that fuel cancer progression. In this article, we review recent studies that describe mutant Ras-regulated signaling routes and their cross-talk. In addition to the two main Ras-driven signaling pathways, i.e., the RAF/MEK/ERK and PI3K/AKT/mTOR pathways, we have also collected emerging data showing the importance of Ras in other signaling pathways, including the RAC/PAK, RalGDS/Ral, and PKC/PLC signaling pathways. Moreover, microRNA-regulated Ras-associated signaling pathways are also discussed to highlight the importance of Ras regulation in cancer. Finally, emerging data show that the signal alterations in specific cell types, such as cancer stem cells, could promote cancer development. Therefore, we also cover the up-to-date findings related to Ras-regulated signal transduction in cancer stem cells. © 2020, The Author(s).},
	keywords = {PHOSPHORYLATION; signal transduction; Tumorigenesis; Mutant Ras protein},
	year = {2020},
	eissn = {1573-7233},
	pages = {1051-1065},
	orcid-numbers = {Buday, László/0000-0003-3518-5757}
}