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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
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elektronikus változat
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3.

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
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