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Transmembrane adapters: attractants for cytoplasmic effectors
Author(s) -
Lindquist Jonathan A.,
Simeoni Luca,
Schraven Burkhart
Publication year - 2003
Publication title -
immunological reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.839
H-Index - 223
eISSN - 1600-065X
pISSN - 0105-2896
DOI - 10.1034/j.1600-065x.2003.00007.x
Subject(s) - transmembrane protein , effector , signal transducing adaptor protein , microbiology and biotechnology , biology , phosphoprotein , phosphorylation , cytoplasm , transmembrane domain , linker , adapter (computing) , fusion protein , kinase , biochemistry , receptor , recombinant dna , engineering , computer science , gene , electrical engineering , operating system
Summary: 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.