Title : PILRalpha, a novel immunoreceptor tyrosine-based inhibitory motif-bearing protein, recruits SHP-1 upon tyrosine phosphorylation and is paired with the truncated counterpart PILRbeta.

Pub. Date : 2000 Feb 11

PMID : 10660620






7 Functional Relationships(s)
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1 PILRalpha, a novel immunoreceptor tyrosine-based inhibitory motif-bearing protein, recruits SHP-1 upon tyrosine phosphorylation and is paired with the truncated counterpart PILRbeta. Tyrosine protein tyrosine phosphatase non-receptor type 6 Homo sapiens
2 PILRalpha, a novel immunoreceptor tyrosine-based inhibitory motif-bearing protein, recruits SHP-1 upon tyrosine phosphorylation and is paired with the truncated counterpart PILRbeta. Tyrosine protein tyrosine phosphatase non-receptor type 6 Homo sapiens
3 SHP-1-mediated dephosphorylation of protein tyrosine residues is central to the regulation of several cell signaling pathways, the specificity of which is dictated by the intrinsic affinity of SH2 domains for the flanking sequences of phosphotyrosine residues. Tyrosine protein tyrosine phosphatase non-receptor type 6 Homo sapiens
4 Substrate trapping in combination with pervanadate treatment of 293T cells confirms that PILRalpha associates with SHP-1 in vivo upon tyrosine phosphorylation. Tyrosine protein tyrosine phosphatase non-receptor type 6 Homo sapiens
5 Mutation of the tyrosine residues in PILRalpha indicates the pivotal role of the Tyr-269 residue in recruiting SHP-1. Tyrosine protein tyrosine phosphatase non-receptor type 6 Homo sapiens
6 Mutation of the tyrosine residues in PILRalpha indicates the pivotal role of the Tyr-269 residue in recruiting SHP-1. Tyrosine protein tyrosine phosphatase non-receptor type 6 Homo sapiens
7 Surface plasmon resonance analysis further suggests that the association between PILRalpha-Tyr-269 and SHP-1 is mediated primarily via the amino-terminal SH2 domain of the latter. Tyrosine protein tyrosine phosphatase non-receptor type 6 Homo sapiens