Molecular cloning of the cDNA encoding pp36, a tyrosine-phosphorylated adaptor protein selectively expressed by T cells and natural killer cells
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 cD...
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| Veröffentlicht in: | The Journal of experimental medicine 1998-04, Vol.187 (7), p.1157-1161 |
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| container_title | The Journal of experimental medicine |
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| creator | Weber, J R Orstavik, S Torgersen, K M Danbolt, N C Berg, S F Ryan, J C Taskén, K Imboden, J B Vaage, J T |
| description | 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. |
| doi_str_mv | 10.1084/jem.187.7.1157 |
| format | Article |
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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. 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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.</description><subject>Adaptor Proteins, Signal Transducing</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Brief Definitive Report</subject><subject>Cells, Cultured</subject><subject>Cloning, Molecular</subject><subject>Deoxyuridine - analogs & derivatives</subject><subject>Deoxyuridine - chemistry</subject><subject>GRB2 Adaptor Protein</subject><subject>Humans</subject><subject>Isoenzymes - metabolism</subject><subject>Killer Cells, Natural - immunology</subject><subject>Molecular Sequence Data</subject><subject>Peptide Fragments - immunology</subject><subject>Phospholipase C gamma</subject><subject>Phosphoproteins - chemistry</subject><subject>Propanolamines - chemistry</subject><subject>Proteins - metabolism</subject><subject>Rats</subject><subject>Recombinant Proteins - immunology</subject><subject>RNA, Messenger - metabolism</subject><subject>Sequence Analysis, DNA</subject><subject>src Homology Domains - genetics</subject><subject>T-Lymphocytes - immunology</subject><subject>Thymus Gland - physiology</subject><subject>Type C Phospholipases - metabolism</subject><issn>0022-1007</issn><issn>1540-9538</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtv1DAUhS0EKkNhyw7JK1Yk-JXY2SBV5SkV2JS1ZTt3OikeO9hORf4FPxkPM6pgheQrS77nHp3rD6HnlLSUKPH6FvYtVbKVLaWdfIA2tBOkGTquHqINIYw1lBD5GD3J-ZYQKkTXn6GzoWMD53yDfn2OHtziTcLOxzCFGxy3uOwAu7dfLjAEF8fD4zzz_hU2uKwp5ilAM-9irpVWbwqM2IxmLjHhOcUCU8AZqm2Z7sCvGH7OCXKuKrvia-zA-4xNGHEwZUnG4--T95COjafo0db4DM9O9zn69v7d9eXH5urrh0-XF1eNE7QvDTXGddDZgdhBDWzLOyLsFrh1XAxGMNXZUYIdlWUWjOkJ5zAwwnvGlVKc8XP05ug7L3YPo4NQahQ9p2lv0qqjmfS_nTDt9E2804zRekg1eHkySPHHArno_ZQPK5gAcclaDlIKJel_hbQXVPI_kdqj0NU_zgm292ko0QfYusLWFbaW-gC7Drz4e4d7-Yku_w0_Mqk2</recordid><startdate>19980406</startdate><enddate>19980406</enddate><creator>Weber, J R</creator><creator>Orstavik, S</creator><creator>Torgersen, K M</creator><creator>Danbolt, N C</creator><creator>Berg, S F</creator><creator>Ryan, J C</creator><creator>Taskén, K</creator><creator>Imboden, J B</creator><creator>Vaage, J T</creator><general>The Rockefeller University Press</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7T5</scope><scope>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19980406</creationdate><title>Molecular cloning of the cDNA encoding pp36, a tyrosine-phosphorylated adaptor protein selectively expressed by T cells and natural killer cells</title><author>Weber, J R ; 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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.</abstract><cop>United States</cop><pub>The Rockefeller University Press</pub><pmid>9529333</pmid><doi>10.1084/jem.187.7.1157</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adaptor Proteins, Signal Transducing Amino Acid Sequence Animals Brief Definitive Report Cells, Cultured Cloning, Molecular Deoxyuridine - analogs & derivatives Deoxyuridine - chemistry GRB2 Adaptor Protein Humans Isoenzymes - metabolism Killer Cells, Natural - immunology Molecular Sequence Data Peptide Fragments - immunology Phospholipase C gamma Phosphoproteins - chemistry Propanolamines - chemistry Proteins - metabolism Rats Recombinant Proteins - immunology RNA, Messenger - metabolism Sequence Analysis, DNA src Homology Domains - genetics T-Lymphocytes - immunology Thymus Gland - physiology Type C Phospholipases - metabolism |
| title | Molecular cloning of the cDNA encoding pp36, a tyrosine-phosphorylated adaptor protein selectively expressed by T cells and natural killer cells |
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