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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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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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