Identification and Characterization of S2V, a Novel Putative Siglec That Contains Two V Set Ig-like Domains and Recruits Protein-tyrosine Phosphatases SHPs*
Identification and Characterization of S2V, a Novel Putative Siglec That Contains Two V Set Ig-like Domains and Recruits Protein-tyrosine Phosphatases SHPs*
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S2V 的鉴定和表征，S2V 是一种新型推定 Siglec，包含两个 V 组 Ig 样结构域并招募蛋白酪氨酸磷酸酶 SHP*
DOI：
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发表时间：
2001
影响因子：
4.8
通讯作者：
S. Shen
中科院分区：
文献类型：
--
作者：
Zhenbao Yu;Ching;M. Maoui;D. Banville;S. Shen
We describe the molecular cloning and characterization of S2V, a novel sialic acid binding immunoglobulin-like lectin. The cDNA of S2V encodes a type 1 transmembrane protein with four extracellular immunoglobulin-like (Ig-like) domains and a cytoplasmic tail bearing a typical immunoreceptor tyrosine-based inhibitory motif (ITIM) and an ITIM-like motif. A unique feature of S2V is the presence of two V-set Ig-like domains responsible for the binding to sialic acid, whereas all other known siglecs possess only one. S2V is predominantly expressed in macrophage. In vivo S2V was tyrosine-phosphorylated when co-expressed with exogenous c-Src kinase. Upon tyrosine phosphorylation, S2V recruits both Src homology 2 (SH2) domain-containing protein-tyrosine phosphatases SHP-1 and SHP-2, two important inhibitory regulators of immunoreceptor signal transduction. These findings suggest that S2V is involved in the negative regulation of the signaling in macrophage by functioning as an inhibitory receptor. When expressed in COS-7 cells, S2V was able to mediate sialic acid-dependent binding to human red blood cells, suggesting that S2V may function through cell-cell interaction.
影响因子：
56.9
作者：
DOODY, GM;JUSTEMENT, LB;FEARON, DT
通讯作者：
FEARON, DT
蛋白酪氨酸磷酸酶 1C 中主要酪氨酸磷酸化位点的磷酸化和鉴定。
DOI：
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发表时间：
1994
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Bouchard,P;Zhao,Z;Banville,D;Dumas,F;Fischer,EH;Shen,SH
通讯作者：
Shen,SH