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1.

001-es BibID:BIBFORM020155
Első szerző:Calpe, Silvia
Cím:Identification and characterization of two related murine genes, Eat2a and Eat2b, encoding single SH2-domain adapters / Silvia Calpe, Erika Erdős, Gongxian Liao, Ninghai Wang, Svend Rietdijk, Maria Simarro, Beata Scholtz, Jill Mooney, Chang Hoon Lee, Min Sun Shin, Éva Rajnavölgyi, John Schatzle, Herbert C. Morse III, Cox Terhorst, Arpad Lanyi
Dátum:2006
ISSN:0093-7711
Megjegyzések:Human EAT-2 (SH2D1B) and SLAM-associated protein (SAP) (SH2D1A) are single SH2-domain adapters, which bind to specific tyrosine residues in the cytoplasmic tail of six signaling lymphocytic activation molecule (SLAM) (SLAMF1)-related receptors. Here we report that, unlike in humans, the mouse and rat Eat2 genes are duplicated with an identical genomic organization. The coding regions of the mouse Eat2a and Eat2b genes share 91% identity at the nucleotide level and 84% at the protein level; similarly, segments of introns are highly conserved. Whereas expression of mouse Eat2a mRNA was detected in multiple tissues, Eat2b was only detectable in mouse natural killer cells, CD8(+) stop T cells, and ovaries, suggesting a very restricted tissue expression of the latter. Both the EAT-2A and EAT-2B coimmunoprecipitated with mouse SLAM in transfected cells and augmented tyrosine phosphorylation of the cytoplasmic tail of SLAM. Both EAT-2A and EAT-2B bind to the Src-like kinases Fyn, Hck, Lyn, Lck, and Fgr, as determined by a yeast two-hybrid assay. However, unlike SAP, the EAT-2 proteins bind to their kinase domains and not to the SH3 domain of these kinases. Taken together, the data suggest that both EAT-2A and EAT-2B are adapters that recruit Src kinases to SLAM family receptors using a mechanism that is distinct from that of SAP.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
adapter proteins
EAT-2
SLAM
Src kinases
Megjelenés:Immunogenetics 58 : 1 (2006), p. 15-25. -
További szerzők:Erdős Erika Liao, Gongxian Wang, Ninghai Rietdijk, Svend Simarro, Maria Scholtz Beáta (1967-) (biokémikus, molekuláris biológus) Mooney, Jill Lee, Chang Hoon Shin, Min Sun Rajnavölgyi Éva (1950-) (immunológus) Schatzle, John Morse, Herbert C. III Terhorst, Cox Lányi Árpád (1962-) (biológus, immunológus)
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2.

001-es BibID:BIBFORM005686
Első szerző:Calpe, Silvia
Cím:The SLAM and SAP gene families control innate and adaptive immune responses / Silvia Calpe, Ninghai Wang, Xavier Romero, Scott B. Berger, Arpad Lanyi, Pablo Engel, Cox Terhorst
Dátum:2008
Megjegyzések:The nine SLAM-family genes, SLAMF1-9, a subfamily of the immunoglobulin superfamily, encode differentially expressed cell-surface receptors of hematopoietic cells. Engagement with their ligands, which are predominantly homotypic, leads to distinct signal transduction events, for instance those that occur in the T or NK cell immune synapse. Upon phosphorylation of one or more copies of a unique tyrosine-based signaling motif in their cytoplasmic tails, six of the SLAM receptors recruit the highly specific single SH2-domain adapters SLAM-associated protein (SAP), EAT-2A, and/or EAT-2B. These adapters in turn bind to the tyrosine kinase Fyn and/or other protein tyrosine kinases connecting the receptors to signal transduction networks. Individuals deficient in the SAP gene, SH2D1A, develop an immunodeficiency syndrome: X-linked lympho-proliferative disease. In addition to operating in the immune synapse, SLAM receptors initiate or partake in multiple effector functions of hematopoietic cells, for example, neutrophil and macrophage killing and platelet aggregation. Here we discuss the current understanding of the structure and function of these recently discovered receptors and adapter molecules in the regulation of adaptive and innate immune responses.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Linked Lymphoproliferative-Disease
Lymphocitic Activation Molecule
Epstein-Barr-Virus
Natural-Killer-Cells
Huan NK Cells
Systemic-Lupus-Erythematosus
CD8(+) T-Cells
Common Variable Immunodeficiency
Human B-Lymphocytes
Receptor 2B4 CD244
Megjelenés:Advances in Immunology. - 97 (2008), p. 177-250. -
További szerzők:Wang, Ninghai Romero, Xavier Berger, Scott B. Lányi Árpád (1962-) (biológus, immunológus) Engel, Pablo Terhorst, Cox
Internet cím:elektronikus változat
DOI
elektronikus változat
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3.

001-es BibID:BIBFORM035749
Első szerző:Chan, Betty
Cím:SAP couples Fyn to SLAM immune receptors / Chan Betty, Lanyi Arpad, Song Hyun Kyu, Griesbach Jan, Simarro-Grande Maria, Poy Florence, Howie Duncan, Sumegi Janos, Terhorst Cox, Eck Michael J.
Dátum:2003
ISSN:1465-7392
Megjegyzések:SAP (SLAM-associated protein) is a small lymphocyte-specific signalling molecule that is defective or absent in patients with X-linked lymphoproliferative syndrome (XLP). Consistent with its single src homology 2 (SH2) domain architecture and unusually high affinity for SLAM (also called CD150), SAP has been suggested to function by blocking binding of SHP-2 or other SH2-containing signalling proteins to SLAM receptors. Additionally, SAP has recently been shown to be required for recruitment and activation of the Src-family kinase FynT after SLAM ligation. This signalling 'adaptor' function has been difficult to conceptualize, because unlike typical SH2-adaptor proteins, SAP contains only a single SH2 domain and lacks other recognized protein interaction domains or motifs. Here, we show that the SAP SH2 domain binds to the SH3 domain of FynT and directly couples FynT to SLAM. The crystal structure of a ternary SLAM-SAP-Fyn-SH3 complex reveals that SAP binds the FynT SH3 domain through a surface-surface interaction that does not involve canonical SH3 or SH2 binding interactions. The observed mode of binding to the Fyn-SH3 domain is expected to preclude the auto-inhibited conformation of Fyn, thereby promoting activation of the kinase after recruitment. These findings broaden our understanding of the functional repertoire of SH3 and SH2 domains.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Nature Cell Biology. - 5 : 2 (2003), p. 155-160. -
További szerzők:Lányi Árpád (1962-) (biológus, immunológus) Song, Hyun Kyu Griesbach, Jan Simarro-Grande, Maria Poy, Florence Howie, Duncan Sümegi János Terhorst, Cox Eck, Michael J.
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4.

001-es BibID:BIBFORM028890
Első szerző:Lányi Árpád (biológus, immunológus)
Cím:The homolog of the five SH3-domain protein (HOFI/SH3PXD2B) regulates lamellipodia formation and cell spreading / Lányi Á., Baráth M., Péterfi Z., Bogel G., Orient A., Simon T., Petrovszki E., Kis-Tóth K., Sirokmány G., Rajnavölgyi É., Terhorst C., Buday L., Geiszt M.
Dátum:2011
ISSN:1932-6203
Megjegyzések:Motility of normal and transformed cells within and across tissues requires specialized subcellular structures, e. g. membrane ruffles, lamellipodia and podosomes, which are generated by dynamic rearrangements of the actin cytoskeleton. Because the formation of these sub-cellular structures is complex and relatively poorly understood, we evaluated the role of the adapter protein SH3PXD2B [HOFI, fad49, Tks4], which plays a role in the development of the eye, skeleton and adipose tissue. Surprisingly, we find that SH3PXD2B is requisite for the development of EGF-induced membrane ruffles and lamellipodia, as well as for efficient cellular attachment and spreading of HeLa cells. Furthermore, SH3PXD2B is present in a complex with the non-receptor protein tyrosine kinase Src, phosphorylated by Src, which is consistent with SH3PXD2B accumulating in Src-induced podosomes. Furthermore, SH3PXD2B closely follows the subcellular relocalization of cortactin to Src-induced podosomes, EGF-induced membrane ruffles and lamellipodia. Because SH3PXD2B also forms a complex with the C-terminal region of cortactin, we propose that SH3PXD2B is a scaffold protein that plays a key role in regulating the actin cytoskeleton via Src and cortactin.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
lamellipodia, podosome
scaffold protein
Megjelenés:PLoS One. - 6 : 8 (2011), p. e23653. -
További szerzők:Baráth Mónika (1980-) (Phd hallgató) Péterfi Zalán Bogel Gábor Orient Anna Simon Tünde (1984-) (biokémikus, molekuláris biológus) Petrovszki Enikő Kis-Tóth Katalin (1975-) (immunológus) Sirokmány Gábor Rajnavölgyi Éva (1950-) (immunológus) Terhorst, Cox Buday László Geiszt Miklós
Pályázati támogatás:TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
Molekuláris immunológia
Internet cím:DOI
Intézményi repozitóriumban (DEA) tárolt változat
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5.

001-es BibID:BIBFORM065580
Első szerző:Morra, Massimo
Cím:Characterization of SH2D1A Missense Mutations Identified in X-linked Lymphoproliferative Disease Patients / Massimo Morra, Maria Simarro-Grande, Margarita Martin, Alice Siau-In Chen, Arpad Lanyi, Olin Silander, Silvia Calpe, Jack Davis, Tony Pawson, Michael J. Eck, Janos Sumegi, Pablo Engel, Shun-Cheng Li, Cox Terhorsta
Dátum:2001
ISSN:0021-9258 1083-351X
Megjegyzések:X-linked lymphoproliferative disease (XLP) is a primary immunodeficiency characterized by extreme susceptibility to Epstein-Barr virus. The XLP disease gene product SH2D1A (SAP) interacts via its SH2 domain with a motif (TIYXXV) present in the cytoplasmic tail of the cell-surface receptors CD150/SLAM, CD84, CD229/Ly-9, and CD244/2B4. Characteristically, the SH2D1A three-pronged interaction with Tyr(281) of CD150 can occur in absence of phosphorylation. Here we analyze the effect of SH2D1A protein missense mutations identified in 10 XLP families. Two sets of mutants were found: (i) mutants with a marked decreased protein half-life (e.g. Y7C, S28R, Q99P, P101L, V102G, and X129R) and (ii) mutants with structural changes that differently affect the interaction with the four receptors. In the second group, mutations that disrupt the interaction between the SH2D1A hydrophobic cleft and Val +3 of its binding motif (e.g. T68I) and mutations that interfere with the SH2D1A phosphotyrosine-binding pocket (e.g. C42W) abrogated SH2D1A binding to all four receptors. Surprisingly, a mutation in SH2D1A able to interfere with Thr -2 of the CD150 binding motif (mutant T53I) severely impaired non-phosphotyrosine interactions while preserving unaffected the binding of SH2D1A to phosphorylated CD150. Mutant T53I, however, did not bind to CD229 and CD224, suggesting that SH2D1A controls several critical signaling pathways in T and natural killer cells. Because no correlation is present between identified types of mutations and XLP patient clinical presentation, additional unidentified genetic or environmental factors must play a strong role in XLP disease manifestations.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal Of Biological Chemistry 276 : 39 (2001), p. 36809-36816. -
További szerzők:Simarro-Grande, Maria Martin, Margarita Chen, Alice Siau-In Lányi Árpád (1962-) (biológus, immunológus) Silander, Olin Calpe, Silvia Davis, Jack Pawson, Tony Eck, Michael J. Sümegi János Engel, Pablo Li, Shun-Cheng Terhorst, Cox
Pályázati támogatás:PO1-AI-35714
Egyéb
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6.

001-es BibID:BIBFORM086897
Első szerző:Réthi Bence (biológus, immunológus)
Cím:CD150 (SLAM) modulates TLR and CD40 pathways in monocyte-derived dendritic cells / Réthi Bence, Gogolák Péter, Rajnavölgyi Éva, Terhorst C., Lányi Árpád
Dátum:2005
ISSN:1521-6616
Tárgyszavak:Orvostudományok Klinikai orvostudományok idézhető absztrakt
folyóiratcikk
Megjelenés:Clinical Immunology. - 115 : Suppl1 (2005), p. S26-S26. -
További szerzők:Gogolák Péter (1968-) (biológus, immunológus) Rajnavölgyi Éva (1950-) (immunológus) Terhorst, Cox Lányi Árpád (1962-) (biológus, immunológus)
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7.

001-es BibID:BIBFORM019938
Első szerző:Réthi Bence (biológus, immunológus)
Cím:SLAM/SLAM interactions inhibit CD40-induced production of inflammatory cytokines in monocyte-derived dendritic cells / Bence Réthi, Péter Gogolák, Istvan Szatmari, Ágota Veres, Erika Erdős, Laszlo Nagy, Éva Rajnavölgyi, Cox Terhorst, Árpád Lányi
Dátum:2006
ISSN:0006-4971
Megjegyzések:Signaling lymphocyte activation molecule (SLAM, CD150, or SLAMF1) is a self-ligand receptor on the surface of activated T- and B-lymphocytes, macrophages, and dendritic cells (DCs). Here we examine the effect of SLAM/SLAM interactions on CD40L-induced CD40 signaling pathways in human DCs. CD40L-expressing L929 cells induced DCs to produce interleukin-6 (IL-6), tumor necrosis factor-alpha (TNF-alpha), and IL-12, which was strongly inhibited by coexpression of SLAM on the surface of the L929 cells. Similarly, transfection of DCs with SLAM strongly reduced CD40L-induced IL-12 production. Furthermore, the negative effect of SLAM/SLAM interactions on CD40L-induced DC activation was also detected in the presence of lipopolysaccharide (LPS). LPS-Induced IL-12 secretion, however, was not inhibited by SLAM engagement. CD40L-activated DCs affected by exposure to SLAM/SLAM engagement were impaired in their ability to induce differentiation of naive T lymphocytes into interferon-gamma (IFN-gamma)-producing T-helper 1 (Th1) effector cells. These inhibitory effects were not the result of a general unresponsiveness of DCs to CD40L, as SLAM/SLAM interactions did not prevent CD40L-induced up-regulation of CD83, CD86, or human leukocyte antigen (HLA)-DQ on the surface of DCs. Taken together, the results indicate that SLAM/SLAM interactions inhibit CD40-induced signal transduction in monocyte-derived dendritic cells, an effect that was not detectable in earlier studies using anti-SLAM monoclonal antibodies.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
linked lymphoproliferative-disease
lymphocytic activation molecule
controls T-cell
measles virus
differential expression
immune-responses
encoding gene
CD150 SLAM
in-vitro
SAP
Megjelenés:Blood. - 107 : 7 (2006), p. 2821-2829. -
További szerzők:Gogolák Péter (1968-) (biológus, immunológus) Szatmári István (1971-) (biológus) Veres Ágota (laboráns) Erdős Erika Nagy László (1966-) (molekuláris sejtbiológus, biokémikus) Rajnavölgyi Éva (1950-) (immunológus) Terhorst, Cox Lányi Árpád (1962-) (biológus, immunológus)
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8.

001-es BibID:BIBFORM035748
Első szerző:Simarro, Maria
Cím:SAP increases FynT kinase activity and is required for phosphorylation of SLAM and Ly9 / Simarro M., Lanyi A., Howie D., Poy F., Bruggeman J., Choi M., Sumegi J., Eck M. J., Terhorst C.
Dátum:2004
ISSN:1471-4906
Megjegyzések:The free Src homology 2 (SH2) domain protein SAP, encoded by the X-linked lymphoproliferative disease gene SH2D1A, controls signal transduction initiated by engagement of the SLAM-related receptors in T and NK cells. Here we demonstrate that SAP is required for phosphorylation of both SLAM and Ly9 in thymocytes and peripheral T cells. Furthermore, in vitro protein interaction studies and yeast two-hybrid analyses indicated that SAP binds directly to FynT and Lck. While SAP bound to both the SH3 domain and to the kinase domain of FynT, SAP bound solely to the kinase domain of Lck. The existence of a strong interaction between SAP and the SH3 domain of FynT prompted us to study the role of SAP in modulating the activity of FynT. In vitro addition of SAP to the autoinhibited form of FynT caused a large increase in FynT catalytic activity. By contrast, the SAP mutant R78E, which is unable to bind to the FynT SH3 domain, did not increase FynT activity and also displayed a reduced adaptor function upon transfection into T cells. Our results demonstrate that SAP is an adaptor that bridges SLAM and Ly9 with Src-like protein tyrosine kinases (PTKs), and has the ability to activate FynT.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
signal transduction
Src
T-lymphocyte
X-linked lymphoproliferative disease
Megjelenés:Trends In Immunology. - 16 : 5 (2004), p. 727-736. -
További szerzők:Lányi Árpád (1962-) (biológus, immunológus) Howie, Duncan Poy, Florence Bruggeman, Joost Choi, Michelle Sümegi János Eck, Michael J. Terhorst, Cox
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