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001-es BibID:	BIBFORM065104
035-os BibID:	(WoS)000380371400013 (Scopus)84993661764
Első szerző:	Mocsár Gábor (biofizikus)
Cím:	MHC I expression regulates co-clustering and mobility of interleukin-2 and -15 receptors in T cells / G. Mocsár, J. Volkó, D. Rönnlund, J. Widengren, P. Nagy, J. Szöllősi, K. Tóth, C. K. Goldman, S. Damjanovich, T. A. Waldmann, A. Bodnár, G. Vámosi
Dátum:	2016
ISSN:	0006-3495
Megjegyzések:	MHC glycoproteins form supramolecular clusters with interleukin-2 and -15 receptors in lipid rafts of T cells.The role of highly expressed MHC I in maintaining these clusters is unknown. We knocked down MHC I inFT7.10 human T cells, and studied protein clustering at two hierarchic levels: molecular aggregations andmobility by FRET and fluorescence correlation spectroscopy, and segregation into larger domains orsuperclusters by superresolution STED microscopy. FCS based molecular brightness analysis revealed thatthe studied molecules diffused as tight aggregates of several proteins of a kind. Knockdown reduced thenumber of MHC I containing molecular aggregates and their average MHC I content, and decreased theheteroassociation of MHC I with IL-2R?/IL-15R?. The mobility of not only MHC I but also that of IL-2R?/IL-15R? increased, corroborating the general size decrease of tight aggregates. A multifaceted analysis of STEDimages revealed that the diameter of MHC I superclusters diminished from 400-600 to 200-300 nm, whereasthose of IL-2R?/IL-15R? hardly changed. MHC I and IL-2R?/IL-15R? colocalized with GM1 gangliosiderichlipid rafts, but MHC I clusters retracted to smaller subsets of GM1- and IL-2R?/IL-15R?-rich areas uponknockdown. Our results prove that changes in expression level may significantly alter the organization andmobility of interacting membrane proteins.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Biophysical Journal. - 111 : 1 (2016), p. 100-112. -
További szerzők:	Volkó Julianna (1983-) (biotechnológus) Rönnlund, Daniel Widengren, Jerker Nagy Péter (1971-) (biofizikus) Szöllősi János (1953-) (biofizikus) Tóth Katalin (Heidelberg) Goldman, Caroline K. Damjanovich Sándor (1936-2017) (biofizikus) Waldmann, Thomas A. Dóczy-Bodnár Andrea (1970-) (biofizikus) Vámosi György (1967-) (biofizikus)
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001-es BibID:	BIBFORM076128
035-os BibID:	(Wos)000450299400006 (Scopus)85055751019
Első szerző:	Nizsalóczki Enikő
Cím:	Minimum degree of overlap between IL-9R and IL-2R on human T lymphoma cells : a quantitative CLSM and FRET analysis / Nizsalóczki Enikő, Nagy Péter, Mocsár Gábor, Szabó Ágnes, Csomós István, Waldmann Thomas A., Vámosi György, Mátyus László, Bodnár Andrea
Dátum:	2018
ISSN:	1552-4922 1552-4930
Megjegyzések:	The heterodimeric receptor complex of IL-9 consists of the cytokine-speci?c ?-subunit and the common ? -chain shared with other cytokines, including IL-2, a central regulator of T cell function. We have shown previously the bipartite spatial relationship of IL-9 and IL-2 receptors at the surface of human T lymphoma cells: in addition to common clusters, expression of the two receptor kinds could also be observed in segregated membrane areas. Here we analyzed further the mutual cell surface organization of IL-9 and IL-2 receptors. Complementing Pearson correlation data with co-occurrence analysis of confocal microscopic images revealed that a minimum degree of IL-9R/IL-2R co-localization exists at the cell surface regardless of the overall spatial correlation of the two receptor kinds. Moreover, our FRET experiments demonstrated molecular scale assemblies of the elements of the IL-9/IL-2R system. Binding of IL-9 altered the structure and/or composition of these clusters. It is hypothesized, that by sequestering receptor subunits in common membrane areas, the overlapping domains of IL-9R and IL-2R provide a platform enabling both the formation of the appropriate receptor complex as well as subunit sharing between related cytokines.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk IL-9 and -2 receptors uorescence resonance energy transfer Manders coef-cient co-occurrence analysis Pearson correlation analysis confocal microscopy human T lymphoma cells co-localization of membrane proteins
Megjelenés:	Cytometry Part A. - 93 : 11 (2018), p. 1106-1117. -
További szerzők:	Nagy Péter (1971-) (biofizikus) Mocsár Gábor (1981-) (biofizikus) Nagyné Szabó Ágnes Timea (1982-) (vegyész) Csomós István (1983-) (molekuláris biológus) Waldmann, Thomas A. Vámosi György (1967-) (biofizikus) Mátyus László (1956-) (biofizikus) Dóczy-Bodnár Andrea (1970-) (biofizikus)
Pályázati támogatás:	EFOP-3.6.3-VEKOP-16-2017-00009 EFOP GINOP-2.3.2-15-2016-00026 GINOP GINOP-2.3.3-15-2016-00003 GINOP K120302 OTKA Intramural research program of the National Cancer Institute, NIH Egyéb
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001-es BibID:	BIBFORM057902
Első szerző:	Nizsalóczki Enikő
Cím:	Distinct spatial relationship of the interleukin-9 receptor with interleukin-2 receptor and major histocompatibility complex glycoproteins in human T lymphoma cells / Enikő Nizsalóczki, István Csomós, Péter Nagy, Zsolt Fazekas, Carolyn K. Goldman, Thomas A. Waldmann, Sándor Damjanovich, György Vámosi, László Mátyus, Andrea Bodnár
Dátum:	2014
ISSN:	1439-4235
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk confocal microscopy membrane proteins FRET protein protein interactions receptors Molekuláris Medicina Doktori iskola
Megjelenés:	Chemphyschem. - 15 : 18 (2014), p. 3969-3978. -
További szerzők:	Csomós István (1983-) (molekuláris biológus) Nagy Péter (1971-) (biofizikus) Fazekas Zsolt (1971-) (biofizikus) Goldman, Caroline K. Waldmann, Thomas A. Damjanovich Sándor (1936-2017) (biofizikus) Vámosi György (1967-) (biofizikus) Mátyus László (1956-) (biofizikus) Dóczy-Bodnár Andrea (1970-) (biofizikus)
Pályázati támogatás:	TÁMOP-4.2.1/B-09/1/KONV-2010-0007 TÁMOP Sejtfelszíni fehérjék szerveződése: az MHC I. szerepe TÁMOP-4.2.2/B-10/1-2010-0024 TÁMOP Molekuláris Orvostudomány Doktori Iskola TÁMOP-4.2.2.A-11/1/KONV-2012-0023 TÁMOP TÁMOP-4.2.2.A-11/1/KONV-2012-0025 TÁMOP TÁMOP-4.2.4.A/2-11/1-2012-0001 TÁMOP CK 78179 OTKA K 103965 OTKA K 103906 OTKA NK 101337 OTKA Baross Gábor Program REG-EA-09-1-2009-0010 Egyéb Internal Research Program of the University of Debrecen RH/885/2013 Egyéb Intramural Research Program of the National Cancer Institute, National Institutes of Health Egyéb
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001-es BibID:	BIBFORM004743
035-os BibID:	(scopus)0038492661 (wos)000184222500005
Első szerző:	Vereb György (biofizikus, orvos)
Cím:	Dynamic, yet structured : the cell membrane three decades after the Singer-Nicolson model / Vereb, G., Szollosi, J., Matko, J., Nagy, P., Farkas, T., Vigh, L., Matyus, L., Waldmann, T. A., Damjanovich, S.
Dátum:	2003
ISSN:	027-8424 (Print)
Megjegyzések:	The fluid mosaic membrane model proved to be a very useful hypothesis in explaining many, but certainly not all, phenomena taking place in biological membranes. New experimental data show that the compartmentalization of membrane components can be as important for effective signal transduction as is the fluidity of the membrane. In this work, we pay tribute to the Singer-Nicolson model, which is near its 30th anniversary, honoring its basic features, "mosaicism" and "diffusion," which predict the interspersion of proteins and lipids and their ability to undergo dynamic rearrangement via Brownian motion. At the same time, modifications based on quantitative data are proposed, highlighting the often genetically predestined, yet flexible, multilevel structure implementing a vast complexity of cellular functions. This new "dynamically structured mosaic model" bears the following characteristics: emphasis is shifted from fluidity to mosaicism, which, in our interpretation, means nonrandom codistribution patterns of specific kinds of membrane proteins forming small-scale clusters at the molecular level and large-scale clusters (groups of clusters, islands) at the submicrometer level. The cohesive forces, which maintain these assemblies as principal elements of the membranes, originate from within a microdomain structure, where lipid-lipid, protein-protein, and protein-lipid interactions, as well as sub- and supramembrane (cytoskeletal, extracellular matrix, other cell) effectors, many of them genetically predestined, play equally important roles. The concept of fluidity in the original model now is interpreted as permissiveness of the architecture to continuous, dynamic restructuring of the molecular- and higher-level clusters according to the needs of the cell and as evoked by the environment.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Animals Biophysics Cell Membrane chemistry Chemistry,Physical Diffusion Extracellular Matrix Fluorescence Resonance Energy Transfer Hungary Lipid Bilayers Membrane Fluidity Membrane Lipids Membrane Microdomains Membrane Proteins Microscopy,Electron Models,Biological Motion physiology Proteins Research Signal Transduction Support
Megjelenés:	Proceedings of the National Academy of Sciences of the United States of America. - 100 : 14 (2003), p. 8053-8058. -
További szerzők:	Szöllősi János (1953-) (biofizikus) Matkó János (1952-) (biológus) Nagy Péter (1971-) (biofizikus) Farkas Tamás (1971-) (biológus) Vígh L. Mátyus László (1956-) (biofizikus) Waldmann, Thomas A. Damjanovich Sándor (1936-2017) (biofizikus)
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