1. Molecular Cloning of the cDNA Encoding pp36, a Tyrosine-phosphorylated Adaptor Protein Selectively Expressed by T Cells and Natural Killer Cells
- Author
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Weber, John R, Ørstavik, Sigurd, Torgersen, Knut Martin, Danbolt, Niels Christian, Berg, Siri F, Ryan, James C, Taskén, Kjetil, Imboden, John B, and Vaage, John T
- Subjects
Biotechnology ,Adaptor Proteins ,Signal Transducing ,Amino Acid Sequence ,Animals ,Cells ,Cultured ,Cloning ,Molecular ,Deoxyuridine ,GRB2 Adaptor Protein ,Humans ,Isoenzymes ,Killer Cells ,Natural ,Molecular Sequence Data ,Peptide Fragments ,Phospholipase C gamma ,Phosphoproteins ,Propanolamines ,Proteins ,RNA ,Messenger ,Rats ,Recombinant Proteins ,Sequence Analysis ,DNA ,T-Lymphocytes ,Thymus Gland ,Type C Phospholipases ,src Homology Domains ,Medical and Health Sciences ,Immunology - Abstract
Activation of T and natural killer (NK) cells leads to the tyrosine phosphorylation of pp36 and to its association with several signaling molecules, including phospholipase Cgamma-1 and Grb2. Microsequencing of peptides derived from purified rat pp36 protein led to the cloning, in rat and man, of cDNA encoding a T- and NK cell-specific protein with several putative Src homology 2 domain-binding motifs. A rabbit antiserum directed against a peptide sequence from the cloned rat molecule recognized tyrosine phosphorylated pp36 from pervanadate-treated rat thymocytes. When expressed in 293T human fibroblast cells and tyrosine-phosphorylated, pp36 associated with phospholipase Cgamma-1 and Grb2. Studies with GST-Grb2 fusion proteins demonstrated that the association was specific for the Src homology 2 domain of Grb-2. Molecular cloning of the gene encoding pp36 should facilitate studies examining the role of this adaptor protein in proximal signaling events during T and NK cell activation.
- Published
- 1998