A Mammalian Adaptor Protein with Conserved Src Homology 2 and Phosphotyrosine-Binding Domains is Related to Shc and is Specifically Expressed in the Brain
The Shc adaptor protein, hereafter referred to as ShcA, possesses two distinct phosphotyrosine-recognition modules, a C-terminal Src homology 2 (SH2) domain and an N-terminal phosphotyrosine-binding (PTB) domain, and is itself phosphorylated on tyrosine in response to many extracellular signals. Pho...
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Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1996-04, Vol.93 (7), p.2729-2734 |
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creator | O'Bryan, John P. Songyang, Zhou Cantley, Lewis Der, Channing J. Pawson, Tony |
description | The Shc adaptor protein, hereafter referred to as ShcA, possesses two distinct phosphotyrosine-recognition modules, a C-terminal Src homology 2 (SH2) domain and an N-terminal phosphotyrosine-binding (PTB) domain, and is itself phosphorylated on tyrosine in response to many extracellular signals. Phosphorylation of human ShcA at Tyr-317 within its central (CH1) region induces binding to the Grb2 SH2 domain and is thereby implicated in activation of the Ras pathway. Two shc-related genes (shcB and shcC) have been identified in the mouse. shcB is closely related to human SCK, while shcC has not yet been found in other organisms. The ShcC protein is predicted to have a C-terminal SH2 domain, a CH1 region with a putative Grb2-binding site, and an N-terminal PTB domain. The ShcC and ShcB SH2 domains bind phosphotyrosine-containing peptides and receptors with a specificity related to, but distinct from, that of the ShcA SH2 domain. The ShcC PTB domain specifically associates in vitro with the autophosphorylated receptors for nerve growth factor and epidermal growth factor. These results indicate that ShcC has functional SH2 and PTB domains. In contrast to shcA, which is widely expressed, shcC RNA and proteins are predominantly expressed in the adult brain. These results suggest that ShcC may mediate signaling from tyrosine kinases in the nervous system, such as receptors for neurotrophins. |
doi_str_mv | 10.1073/pnas.93.7.2729 |
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Phosphorylation of human ShcA at Tyr-317 within its central (CH1) region induces binding to the Grb2 SH2 domain and is thereby implicated in activation of the Ras pathway. Two shc-related genes (shcB and shcC) have been identified in the mouse. shcB is closely related to human SCK, while shcC has not yet been found in other organisms. The ShcC protein is predicted to have a C-terminal SH2 domain, a CH1 region with a putative Grb2-binding site, and an N-terminal PTB domain. The ShcC and ShcB SH2 domains bind phosphotyrosine-containing peptides and receptors with a specificity related to, but distinct from, that of the ShcA SH2 domain. The ShcC PTB domain specifically associates in vitro with the autophosphorylated receptors for nerve growth factor and epidermal growth factor. These results indicate that ShcC has functional SH2 and PTB domains. In contrast to shcA, which is widely expressed, shcC RNA and proteins are predominantly expressed in the adult brain. These results suggest that ShcC may mediate signaling from tyrosine kinases in the nervous system, such as receptors for neurotrophins.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.93.7.2729</identifier><identifier>PMID: 8610109</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>3T3 Cells ; Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Amino acids ; Animals ; Antibodies ; Base Sequence ; Binding Sites ; Biochemistry ; Brain ; Brain - metabolism ; Cell Line ; Cloning, Molecular ; Complementary DNA ; Conserved Sequence ; DNA Primers ; Drosophila ; Drosophila - metabolism ; ErbB Receptors - metabolism ; Female ; Humans ; Mammals ; Mice ; Molecular Sequence Data ; Multigene Family ; Nerve Tissue Proteins - chemistry ; Neuropeptides ; Organ Specificity ; Phosphorylation ; Phosphotyrosine ; Polymerase Chain Reaction ; Protein Biosynthesis ; Proteins ; Proteins - chemistry ; Proteins - metabolism ; Receptors ; Receptors, Nerve Growth Factor - metabolism ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - metabolism ; RNA ; Sequence Homology, Amino Acid ; Shc Signaling Adaptor Proteins ; Src Homology 2 Domain-Containing, Transforming Protein 2 ; Src Homology 2 Domain-Containing, Transforming Protein 3 ; src Homology Domains</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1996-04, Vol.93 (7), p.2729-2734</ispartof><rights>Copyright 1996 National Academy of Sciences</rights><rights>Copyright National Academy of Sciences Apr 2, 1996</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c482t-3840c44b0c0e624b65d28c99ecad536bae45fdd70ae4b3d7b4573604660d03003</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/93/7.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/39053$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/39053$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,315,729,782,786,805,887,27931,27932,53798,53800,58024,58257</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8610109$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>O'Bryan, John P.</creatorcontrib><creatorcontrib>Songyang, Zhou</creatorcontrib><creatorcontrib>Cantley, Lewis</creatorcontrib><creatorcontrib>Der, Channing J.</creatorcontrib><creatorcontrib>Pawson, Tony</creatorcontrib><title>A Mammalian Adaptor Protein with Conserved Src Homology 2 and Phosphotyrosine-Binding Domains is Related to Shc and is Specifically Expressed in the Brain</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The Shc adaptor protein, hereafter referred to as ShcA, possesses two distinct phosphotyrosine-recognition modules, a C-terminal Src homology 2 (SH2) domain and an N-terminal phosphotyrosine-binding (PTB) domain, and is itself phosphorylated on tyrosine in response to many extracellular signals. Phosphorylation of human ShcA at Tyr-317 within its central (CH1) region induces binding to the Grb2 SH2 domain and is thereby implicated in activation of the Ras pathway. Two shc-related genes (shcB and shcC) have been identified in the mouse. shcB is closely related to human SCK, while shcC has not yet been found in other organisms. The ShcC protein is predicted to have a C-terminal SH2 domain, a CH1 region with a putative Grb2-binding site, and an N-terminal PTB domain. The ShcC and ShcB SH2 domains bind phosphotyrosine-containing peptides and receptors with a specificity related to, but distinct from, that of the ShcA SH2 domain. The ShcC PTB domain specifically associates in vitro with the autophosphorylated receptors for nerve growth factor and epidermal growth factor. These results indicate that ShcC has functional SH2 and PTB domains. In contrast to shcA, which is widely expressed, shcC RNA and proteins are predominantly expressed in the adult brain. These results suggest that ShcC may mediate signaling from tyrosine kinases in the nervous system, such as receptors for neurotrophins.</description><subject>3T3 Cells</subject><subject>Adaptor Proteins, Signal Transducing</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Brain</subject><subject>Brain - metabolism</subject><subject>Cell Line</subject><subject>Cloning, Molecular</subject><subject>Complementary DNA</subject><subject>Conserved Sequence</subject><subject>DNA Primers</subject><subject>Drosophila</subject><subject>Drosophila - metabolism</subject><subject>ErbB Receptors - metabolism</subject><subject>Female</subject><subject>Humans</subject><subject>Mammals</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Multigene Family</subject><subject>Nerve Tissue Proteins - chemistry</subject><subject>Neuropeptides</subject><subject>Organ Specificity</subject><subject>Phosphorylation</subject><subject>Phosphotyrosine</subject><subject>Polymerase Chain Reaction</subject><subject>Protein Biosynthesis</subject><subject>Proteins</subject><subject>Proteins - chemistry</subject><subject>Proteins - metabolism</subject><subject>Receptors</subject><subject>Receptors, Nerve Growth Factor - metabolism</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - metabolism</subject><subject>RNA</subject><subject>Sequence Homology, Amino Acid</subject><subject>Shc Signaling Adaptor Proteins</subject><subject>Src Homology 2 Domain-Containing, Transforming Protein 2</subject><subject>Src Homology 2 Domain-Containing, Transforming Protein 3</subject><subject>src Homology Domains</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kkFv0zAYhiMEGqVw5YCEZHHYLeVL7MSxxKUrgyENMVE4W47jNq4SO7Pdsf6V_do5tFSFAydb_p7Hn-3XSfI6g1kGFL8fjPAzhmd0ltOcPUkmGbAsLQmDp8kEIKdpRXLyPHnh_QYAWFHBWXJWlRlEcJI8zNFX0fei08KgeSOGYB26cTYobdAvHVq0sMYrd6catHQSXdnedna9QzkSpkE3rfVDa8POWa-NSi-0abRZo4-2F9p4pD36rjoRoh0sWrbytxVXl4OSeqWl6LodurwfnPI-QrFpaBW6cNF-mTxbic6rV4dxmvz8dPljcZVef_v8ZTG_TiWp8pDiioAkpAYJqsxJXRZNXknGlBRNgctaKFKsmoZCnNS4oTUpKC6BlCU0gAHwNPmw33fY1r1qpDLBiY4PTvfC7bgVmv9dMbrla3vHMSsZi_r5QXf2dqt84L32UnWdMMpuPaeUUaBk7PPuH3Bjt87Eq_EcMlzmY57TZLaHZHxR79TqeI4M-AjwMXDOMKd8DDwKb09Pf8QPCZ_UR-9P9dQ__1-dr7ZdF9R9iOCbPbjx8Y8cScygwPgRHk_JvA</recordid><startdate>19960402</startdate><enddate>19960402</enddate><creator>O'Bryan, John P.</creator><creator>Songyang, Zhou</creator><creator>Cantley, Lewis</creator><creator>Der, Channing J.</creator><creator>Pawson, Tony</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><general>National Academy of Sciences</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19960402</creationdate><title>A Mammalian Adaptor Protein with Conserved Src Homology 2 and Phosphotyrosine-Binding Domains is Related to Shc and is Specifically Expressed in the Brain</title><author>O'Bryan, John P. ; Songyang, Zhou ; Cantley, Lewis ; Der, Channing J. ; Pawson, Tony</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c482t-3840c44b0c0e624b65d28c99ecad536bae45fdd70ae4b3d7b4573604660d03003</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>3T3 Cells</topic><topic>Adaptor Proteins, Signal Transducing</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Antibodies</topic><topic>Base Sequence</topic><topic>Binding Sites</topic><topic>Biochemistry</topic><topic>Brain</topic><topic>Brain - metabolism</topic><topic>Cell Line</topic><topic>Cloning, Molecular</topic><topic>Complementary DNA</topic><topic>Conserved Sequence</topic><topic>DNA Primers</topic><topic>Drosophila</topic><topic>Drosophila - metabolism</topic><topic>ErbB Receptors - metabolism</topic><topic>Female</topic><topic>Humans</topic><topic>Mammals</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Multigene Family</topic><topic>Nerve Tissue Proteins - chemistry</topic><topic>Neuropeptides</topic><topic>Organ Specificity</topic><topic>Phosphorylation</topic><topic>Phosphotyrosine</topic><topic>Polymerase Chain Reaction</topic><topic>Protein Biosynthesis</topic><topic>Proteins</topic><topic>Proteins - chemistry</topic><topic>Proteins - metabolism</topic><topic>Receptors</topic><topic>Receptors, Nerve Growth Factor - metabolism</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - metabolism</topic><topic>RNA</topic><topic>Sequence Homology, Amino Acid</topic><topic>Shc Signaling Adaptor Proteins</topic><topic>Src Homology 2 Domain-Containing, Transforming Protein 2</topic><topic>Src Homology 2 Domain-Containing, Transforming Protein 3</topic><topic>src Homology Domains</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>O'Bryan, John P.</creatorcontrib><creatorcontrib>Songyang, Zhou</creatorcontrib><creatorcontrib>Cantley, Lewis</creatorcontrib><creatorcontrib>Der, Channing J.</creatorcontrib><creatorcontrib>Pawson, Tony</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>O'Bryan, John P.</au><au>Songyang, Zhou</au><au>Cantley, Lewis</au><au>Der, Channing J.</au><au>Pawson, Tony</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Mammalian Adaptor Protein with Conserved Src Homology 2 and Phosphotyrosine-Binding Domains is Related to Shc and is Specifically Expressed in the Brain</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1996-04-02</date><risdate>1996</risdate><volume>93</volume><issue>7</issue><spage>2729</spage><epage>2734</epage><pages>2729-2734</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>The Shc adaptor protein, hereafter referred to as ShcA, possesses two distinct phosphotyrosine-recognition modules, a C-terminal Src homology 2 (SH2) domain and an N-terminal phosphotyrosine-binding (PTB) domain, and is itself phosphorylated on tyrosine in response to many extracellular signals. Phosphorylation of human ShcA at Tyr-317 within its central (CH1) region induces binding to the Grb2 SH2 domain and is thereby implicated in activation of the Ras pathway. Two shc-related genes (shcB and shcC) have been identified in the mouse. shcB is closely related to human SCK, while shcC has not yet been found in other organisms. The ShcC protein is predicted to have a C-terminal SH2 domain, a CH1 region with a putative Grb2-binding site, and an N-terminal PTB domain. The ShcC and ShcB SH2 domains bind phosphotyrosine-containing peptides and receptors with a specificity related to, but distinct from, that of the ShcA SH2 domain. The ShcC PTB domain specifically associates in vitro with the autophosphorylated receptors for nerve growth factor and epidermal growth factor. These results indicate that ShcC has functional SH2 and PTB domains. In contrast to shcA, which is widely expressed, shcC RNA and proteins are predominantly expressed in the adult brain. These results suggest that ShcC may mediate signaling from tyrosine kinases in the nervous system, such as receptors for neurotrophins.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>8610109</pmid><doi>10.1073/pnas.93.7.2729</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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source | MEDLINE; JSTOR Archive Collection A-Z Listing; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
subjects | 3T3 Cells Adaptor Proteins, Signal Transducing Amino Acid Sequence Amino acids Animals Antibodies Base Sequence Binding Sites Biochemistry Brain Brain - metabolism Cell Line Cloning, Molecular Complementary DNA Conserved Sequence DNA Primers Drosophila Drosophila - metabolism ErbB Receptors - metabolism Female Humans Mammals Mice Molecular Sequence Data Multigene Family Nerve Tissue Proteins - chemistry Neuropeptides Organ Specificity Phosphorylation Phosphotyrosine Polymerase Chain Reaction Protein Biosynthesis Proteins Proteins - chemistry Proteins - metabolism Receptors Receptors, Nerve Growth Factor - metabolism Recombinant Proteins - biosynthesis Recombinant Proteins - metabolism RNA Sequence Homology, Amino Acid Shc Signaling Adaptor Proteins Src Homology 2 Domain-Containing, Transforming Protein 2 Src Homology 2 Domain-Containing, Transforming Protein 3 src Homology Domains |
title | A Mammalian Adaptor Protein with Conserved Src Homology 2 and Phosphotyrosine-Binding Domains is Related to Shc and is Specifically Expressed in the Brain |
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