Lindquist Jonathan A, Simeoni Luca, Schraven Burkhart
Institute of Immunology, Otto-von-Guericke University, Magdeburg, Germany.
Immunol Rev. 2003 Feb;191:165-82. doi: 10.1034/j.1600-065x.2003.00007.x.
Transmembrane adapter proteins (TRAPs) are a relatively new and growing family of proteins that include linker for activation of T cells (LAT), phosphoprotein associated with glycosphingolipid-enriched micro domains (PAG)/C-terminal Src kinase (Csk) binding protein (Cbp), SHP2-interacting transmembrane adapter protein (SIT), T cell receptor interacting molecule (TRIM), and the recently identified non-T cell activation linker (NTAL) and pp30. TRAPs share several common structural features, but more importantly they possess multiple sites of tyrosine phosphorylation, by which they act as scaffolds for recruiting cytosolic adapter and/or effector proteins. The membrane association of TRAPs places them near to the immunoreceptors, a position from which they coordinate and modulate the signals they receive to produce an appropriate cellular response.
跨膜衔接蛋白(TRAPs)是一个相对较新且不断发展的蛋白质家族,其中包括T细胞活化连接蛋白(LAT)、与富含糖鞘脂微结构域相关的磷蛋白(PAG)/C末端Src激酶(Csk)结合蛋白(Cbp)、SHP2相互作用跨膜衔接蛋白(SIT)、T细胞受体相互作用分子(TRIM),以及最近发现的非T细胞活化连接蛋白(NTAL)和pp30。TRAPs具有几个共同的结构特征,但更重要的是,它们拥有多个酪氨酸磷酸化位点,通过这些位点它们充当招募胞质衔接蛋白和/或效应蛋白的支架。TRAPs与膜的结合使它们靠近免疫受体,从这个位置它们协调和调节所接收的信号以产生适当的细胞反应。