Thymocyte activation induces the association of the proto‐oncoprotein c‐cbl and ras GTPase‐ activating protein with CD5
Studies of knockout mice indicate that the glycoprotein CD5, which is expressed on T cells, most thymocytes and a subset of B cells, down‐regulates TCR‐ and B cell receptor (BCR)‐mediated signaling. CD5 is associated with the TCR and BCR, and is phosphorylated on cytoplasmic tyrosine residues follow...
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| Veröffentlicht in: | European journal of immunology 1998-05, Vol.28 (5), p.1617-1625 |
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| creator | Dennehy, Kevin M. Broszeit, Richard Ferris, William F. Beyers, Albert D. |
| description | Studies of knockout mice indicate that the glycoprotein CD5, which is expressed on T cells, most thymocytes and a subset of B cells, down‐regulates TCR‐ and B cell receptor (BCR)‐mediated signaling. CD5 is associated with the TCR and BCR, and is phosphorylated on cytoplasmic tyrosine residues following antigen receptor ligation. Cross‐linking of CD5 or pervanadate stimulation of thymocytes induces the association of a 120‐kDa tyrosine‐phosphorylated protein with CD5. The proto‐oncoprotein c‐cbl associates with CD5 in pervanadate‐stimulated thymocytes, and reprecipitation analysis demonstrates that the major proportion of CD5‐associated pp120 is c‐cbl. The GTPase‐activating protein for ras (ras GAP), which is not tyrosine phosphorylated following CD5 cross‐linking, associates with CD5 in pervanadate‐stimulated thymocytes. Using tyrosine‐phosphorylated peptides we show that ras GAP interacts in an SH2‐mediated manner with the phosphorylated Y429SQP sequence of CD5. Both c‐cbl and ras GAP have been proposed to suppress receptor‐mediated signaling, and may contribute to CD5‐mediated suppression of TCR or BCR signaling. |
| doi_str_mv | 10.1002/(SICI)1521-4141(199805)28:05<1617::AID-IMMU1617>3.0.CO;2-7 |
| format | Article |
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CD5 is associated with the TCR and BCR, and is phosphorylated on cytoplasmic tyrosine residues following antigen receptor ligation. Cross‐linking of CD5 or pervanadate stimulation of thymocytes induces the association of a 120‐kDa tyrosine‐phosphorylated protein with CD5. The proto‐oncoprotein c‐cbl associates with CD5 in pervanadate‐stimulated thymocytes, and reprecipitation analysis demonstrates that the major proportion of CD5‐associated pp120 is c‐cbl. The GTPase‐activating protein for ras (ras GAP), which is not tyrosine phosphorylated following CD5 cross‐linking, associates with CD5 in pervanadate‐stimulated thymocytes. Using tyrosine‐phosphorylated peptides we show that ras GAP interacts in an SH2‐mediated manner with the phosphorylated Y429SQP sequence of CD5. Both c‐cbl and ras GAP have been proposed to suppress receptor‐mediated signaling, and may contribute to CD5‐mediated suppression of TCR or BCR signaling.</description><identifier>ISSN: 0014-2980</identifier><identifier>EISSN: 1521-4141</identifier><identifier>DOI: 10.1002/(SICI)1521-4141(199805)28:05<1617::AID-IMMU1617>3.0.CO;2-7</identifier><identifier>PMID: 9603468</identifier><language>eng</language><publisher>Weinheim: WILEY‐VCH Verlag GmbH</publisher><subject>Amino Acid Sequence ; Animals ; CD5 ; CD5 Antigens - metabolism ; Cell Adhesion Molecules - metabolism ; c‐cbl ; Focal Adhesion Kinase 1 ; Focal Adhesion Protein-Tyrosine Kinases ; GTP Phosphohydrolases - metabolism ; GTPase-Activating Proteins ; Humans ; Lymphocyte Activation ; Mice ; Mice, Knockout ; Molecular Sequence Data ; Phosphopeptides - metabolism ; Phosphorylation ; Protein-Tyrosine Kinases - metabolism ; Proteins - metabolism ; Proto-Oncogene Proteins - metabolism ; Proto-Oncogene Proteins c-cbl ; ras GTPase-Activating Proteins ; ras GTPase‐activating protein ; ras Proteins - metabolism ; Rats ; Rats, Inbred Strains ; src Homology Domains - immunology ; T-Lymphocytes - enzymology ; T-Lymphocytes - immunology ; T-Lymphocytes - metabolism ; Tyrosine - metabolism ; Ubiquitin-Protein Ligases</subject><ispartof>European journal of immunology, 1998-05, Vol.28 (5), p.1617-1625</ispartof><rights>1998 WILEY‐VCH Verlag GmbH, Weinheim, Fed. 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CD5 is associated with the TCR and BCR, and is phosphorylated on cytoplasmic tyrosine residues following antigen receptor ligation. Cross‐linking of CD5 or pervanadate stimulation of thymocytes induces the association of a 120‐kDa tyrosine‐phosphorylated protein with CD5. The proto‐oncoprotein c‐cbl associates with CD5 in pervanadate‐stimulated thymocytes, and reprecipitation analysis demonstrates that the major proportion of CD5‐associated pp120 is c‐cbl. The GTPase‐activating protein for ras (ras GAP), which is not tyrosine phosphorylated following CD5 cross‐linking, associates with CD5 in pervanadate‐stimulated thymocytes. Using tyrosine‐phosphorylated peptides we show that ras GAP interacts in an SH2‐mediated manner with the phosphorylated Y429SQP sequence of CD5. Both c‐cbl and ras GAP have been proposed to suppress receptor‐mediated signaling, and may contribute to CD5‐mediated suppression of TCR or BCR signaling.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>CD5</subject><subject>CD5 Antigens - metabolism</subject><subject>Cell Adhesion Molecules - metabolism</subject><subject>c‐cbl</subject><subject>Focal Adhesion Kinase 1</subject><subject>Focal Adhesion Protein-Tyrosine Kinases</subject><subject>GTP Phosphohydrolases - metabolism</subject><subject>GTPase-Activating Proteins</subject><subject>Humans</subject><subject>Lymphocyte Activation</subject><subject>Mice</subject><subject>Mice, Knockout</subject><subject>Molecular Sequence Data</subject><subject>Phosphopeptides - metabolism</subject><subject>Phosphorylation</subject><subject>Protein-Tyrosine Kinases - metabolism</subject><subject>Proteins - metabolism</subject><subject>Proto-Oncogene Proteins - metabolism</subject><subject>Proto-Oncogene Proteins c-cbl</subject><subject>ras GTPase-Activating Proteins</subject><subject>ras GTPase‐activating protein</subject><subject>ras Proteins - metabolism</subject><subject>Rats</subject><subject>Rats, Inbred Strains</subject><subject>src Homology Domains - immunology</subject><subject>T-Lymphocytes - enzymology</subject><subject>T-Lymphocytes - immunology</subject><subject>T-Lymphocytes - metabolism</subject><subject>Tyrosine - metabolism</subject><subject>Ubiquitin-Protein Ligases</subject><issn>0014-2980</issn><issn>1521-4141</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc9u1DAQxi0EKtvCIyDlhNpDFv9JYmepkNoUSqRWi8T2woGR7dhsUDYucbbVHirxCH3GPgkO2e4FoV5szzcz34z8Q-iU4CnBmL47_FoW5RFJKYkTkpBDkucCp0dUzHB6TDLCZ7OT8iwuLy-vhugDm-JpMX9PY_4MTXZtz9EEY5LENDS_RPve_8QY51ma76G9PMMsycQE3S2Wm5XTm95EUvf1jexr10Z1W6218VG_DLL3Ttej7uxf6bpzvXv4fe9a7Ya3qdtIh1irJpJtFXXSR-eLL9KbIO582x_RY_Ft3S-j4ix9hV5Y2XjzensfoKtPHxfF5_hifl4WJxexTkTOY6mk5IYIrqSqtFVWW8aosibhNGMVZURiIzQRylBCRUqxtJVWVoZf4JWo2AF6O_qGBX6tje9hVXttmka2xq098FzklOXZk4UkS4I956Hw21ioO-d9Zyxcd_VKdhsgGAaIAANEGGjAQANGiEAFhHPABhAgwiNEYIChmAOFwfzNdou1WplqZ72lFvLfx_xt3ZjNP5OfHPyfuTuN_QHmFb85</recordid><startdate>199805</startdate><enddate>199805</enddate><creator>Dennehy, Kevin M.</creator><creator>Broszeit, Richard</creator><creator>Ferris, William F.</creator><creator>Beyers, Albert D.</creator><general>WILEY‐VCH Verlag GmbH</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>H94</scope><scope>7X8</scope></search><sort><creationdate>199805</creationdate><title>Thymocyte activation induces the association of the proto‐oncoprotein c‐cbl and ras GTPase‐ activating protein with CD5</title><author>Dennehy, Kevin M. ; Broszeit, Richard ; Ferris, William F. ; Beyers, Albert D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4897-abaa7e187babdcfbfcf332bfe47263d231a0e8c18be2128520afdcbfa1417d8d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>CD5</topic><topic>CD5 Antigens - metabolism</topic><topic>Cell Adhesion Molecules - metabolism</topic><topic>c‐cbl</topic><topic>Focal Adhesion Kinase 1</topic><topic>Focal Adhesion Protein-Tyrosine Kinases</topic><topic>GTP Phosphohydrolases - metabolism</topic><topic>GTPase-Activating Proteins</topic><topic>Humans</topic><topic>Lymphocyte Activation</topic><topic>Mice</topic><topic>Mice, Knockout</topic><topic>Molecular Sequence Data</topic><topic>Phosphopeptides - metabolism</topic><topic>Phosphorylation</topic><topic>Protein-Tyrosine Kinases - metabolism</topic><topic>Proteins - metabolism</topic><topic>Proto-Oncogene Proteins - metabolism</topic><topic>Proto-Oncogene Proteins c-cbl</topic><topic>ras GTPase-Activating Proteins</topic><topic>ras GTPase‐activating protein</topic><topic>ras Proteins - metabolism</topic><topic>Rats</topic><topic>Rats, Inbred Strains</topic><topic>src Homology Domains - immunology</topic><topic>T-Lymphocytes - enzymology</topic><topic>T-Lymphocytes - immunology</topic><topic>T-Lymphocytes - metabolism</topic><topic>Tyrosine - metabolism</topic><topic>Ubiquitin-Protein Ligases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dennehy, Kevin M.</creatorcontrib><creatorcontrib>Broszeit, Richard</creatorcontrib><creatorcontrib>Ferris, William F.</creatorcontrib><creatorcontrib>Beyers, Albert D.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dennehy, Kevin M.</au><au>Broszeit, Richard</au><au>Ferris, William F.</au><au>Beyers, Albert D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Thymocyte activation induces the association of the proto‐oncoprotein c‐cbl and ras GTPase‐ activating protein with CD5</atitle><jtitle>European journal of immunology</jtitle><addtitle>Eur J Immunol</addtitle><date>1998-05</date><risdate>1998</risdate><volume>28</volume><issue>5</issue><spage>1617</spage><epage>1625</epage><pages>1617-1625</pages><issn>0014-2980</issn><eissn>1521-4141</eissn><abstract>Studies of knockout mice indicate that the glycoprotein CD5, which is expressed on T cells, most thymocytes and a subset of B cells, down‐regulates TCR‐ and B cell receptor (BCR)‐mediated signaling. CD5 is associated with the TCR and BCR, and is phosphorylated on cytoplasmic tyrosine residues following antigen receptor ligation. Cross‐linking of CD5 or pervanadate stimulation of thymocytes induces the association of a 120‐kDa tyrosine‐phosphorylated protein with CD5. The proto‐oncoprotein c‐cbl associates with CD5 in pervanadate‐stimulated thymocytes, and reprecipitation analysis demonstrates that the major proportion of CD5‐associated pp120 is c‐cbl. The GTPase‐activating protein for ras (ras GAP), which is not tyrosine phosphorylated following CD5 cross‐linking, associates with CD5 in pervanadate‐stimulated thymocytes. Using tyrosine‐phosphorylated peptides we show that ras GAP interacts in an SH2‐mediated manner with the phosphorylated Y429SQP sequence of CD5. Both c‐cbl and ras GAP have been proposed to suppress receptor‐mediated signaling, and may contribute to CD5‐mediated suppression of TCR or BCR signaling.</abstract><cop>Weinheim</cop><pub>WILEY‐VCH Verlag GmbH</pub><pmid>9603468</pmid><doi>10.1002/(SICI)1521-4141(199805)28:05<1617::AID-IMMU1617>3.0.CO;2-7</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | European journal of immunology, 1998-05, Vol.28 (5), p.1617-1625 |
| issn | 0014-2980 1521-4141 |
| language | eng |
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| source | MEDLINE; Wiley Online Library Free Content; Access via Wiley Online Library; EZB-FREE-00999 freely available EZB journals |
| subjects | Amino Acid Sequence Animals CD5 CD5 Antigens - metabolism Cell Adhesion Molecules - metabolism c‐cbl Focal Adhesion Kinase 1 Focal Adhesion Protein-Tyrosine Kinases GTP Phosphohydrolases - metabolism GTPase-Activating Proteins Humans Lymphocyte Activation Mice Mice, Knockout Molecular Sequence Data Phosphopeptides - metabolism Phosphorylation Protein-Tyrosine Kinases - metabolism Proteins - metabolism Proto-Oncogene Proteins - metabolism Proto-Oncogene Proteins c-cbl ras GTPase-Activating Proteins ras GTPase‐activating protein ras Proteins - metabolism Rats Rats, Inbred Strains src Homology Domains - immunology T-Lymphocytes - enzymology T-Lymphocytes - immunology T-Lymphocytes - metabolism Tyrosine - metabolism Ubiquitin-Protein Ligases |
| title | Thymocyte activation induces the association of the proto‐oncoprotein c‐cbl and ras GTPase‐ activating protein with CD5 |
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