Structural and functional dissection of the cytoplasmic domain of the transmembrane adaptor protein SIT (SHP2-interacting transmembrane adaptor protein)

0191221 - UMG-J 20010292 RIV DE eng J - Journal Article
Pfrepper, K. I. - Marie-Cardine, A. - Simeoni, L. - Kuramitsu, Y. - Leo, A. - Špička, Jiří - Hilgert, Ivan - Scherer, J. - Schraven, B.
Structural and functional dissection of the cytoplasmic domain of the transmembrane adaptor protein SIT (SHP2-interacting transmembrane adaptor protein).
European Journal of Immunology. Roč. 31, č. 6 (2001), s. 1825-1836. ISSN 0014-2980. E-ISSN 1521-4141
R&D Projects: GA ČR GA204/99/0367
Institutional research plan: CEZ:AV0Z5052915
Keywords : receptor * adaptor protein * signaling
Subject RIV: EB - Genetics ; Molecular Biology
Impact factor: 4.990, year: 2001

Transmembrane adaptor protein SIT interacts with SHP2 butalso with Grb2 via two consensus YxN motifs. However, mutation of both Grb2-binding sites does not influence the inhibitory function of SIT. In contrast, mutation of the tyrosine-based signaling motif Y (168) ASV completely abrogates the ability of SIT to inhibit T cell activation. Co-precipitation experiments revealed that the tyrosine kinase p50(csk) could represent the negative regulatory effector molecule that binds to this motif.
Permanent Link: http://hdl.handle.net/11104/0086978