A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion
A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion
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DOI：
10.1093/emboj/17.24.7320
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发表时间：
1998-12-15
期刊：
影响因子：
11.4
通讯作者：
Reinherz, EL
中科院分区：
文献类型：
--
作者：
Li, J;Nishizawa, K;Reinherz, EL
通过相互作用陷阱克隆方法鉴定了人CD 2胞质尾结合蛋白，称为CD 2BP 1。CD 2BP 1的表达仅限于造血组织，在T和自然杀伤（NK）细胞中突出，长（CD 2BP 1 L）和短（CD 2BP 1 S）变体由可变RNA剪接产生。两种CD 2BP 1分子均与粟酒裂殖酵母cdc 15同源，并且包括螺旋结构域、可变长度的插入PEST序列和C-末端SH 3结构域。尽管CD 2BP 1 SH 3结构域直接结合CD 2序列KGPPLPRPRV（氨基酸300-309），但其结合被CD 2BP 1 N-末端区段显著增强。在配体诱导的表面CD 2分子聚集后，CD 2BP 1从胞浆重新分布到表面膜区室，与CD 2共定位。反过来，CD 2BP 1下调CD 2刺激的粘附，这显然是通过蛋白酪氨酸磷酸酶（PTP）-PEST与CD 2的偶联。
A human CD2 cytoplasmic tail-binding protein, termed CD2BP1, was identified by an interaction trap cloning method. Expression of CD2BP1 is restricted to hematopoietic tissue, being prominent in T and natural killer (NK) cells, with long (CD2BP1L) and short (CD2BP1S) variants arising by alternative RNA splicing. Both CD2BP1 molecules are homologous to Schizosaccharomyces pombe cdc15, and include a helical domain, variable length intervening PEST sequence and C-terminal SH3 domain. Although the CD2BP1 SH3 domain binds directly to the CD2 sequence, KGPPLPRPRV (amino acids 300-309), its association is augmented markedly by the CD2BP1 N-terminal segment. Upon ligand-induced clustering of surface CD2 molecules, CD2BP1 redistributes from a cytosolic to a surface membrane compartment, co-localizing with CD2, In turn, CD2-stimulated adhesion is down-regulated by CD2BP1, apparently through coupling of the protein tyrosine phosphatase (PTP)-PEST to CD2, These findings offer the first molecular view into the control processes for T cell adhesion.