All autophosphorylation sites of epidermal growth factor (EGF) receptor and HER2/neu are located in their carboxyl-terminal tails. Identification of a novel site in EGF receptor
Activation of the epidermal growth factor (EGF) receptor kinase leads to autophosphorylation and to the phosphorylation of various cellular substrates. The three known autophosphorylation sites of EGF receptor are located at the carboxyl-terminal tail where they probably act to compete with and thus...
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| Veröffentlicht in: | The Journal of biological chemistry 1989-06, Vol.264 (18), p.10667-10671 |
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| container_title | The Journal of biological chemistry |
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| creator | MARGOLIS, B. L LAX, I KRIS, R DOMBALAGIAN, M HONEGGER, A. M HOWK, R GIVOL, D ULLRICH, A SCHLESSINGER, J |
| description | Activation of the epidermal growth factor (EGF) receptor kinase leads to autophosphorylation and to the phosphorylation of
various cellular substrates. The three known autophosphorylation sites of EGF receptor are located at the carboxyl-terminal
tail where they probably act to compete with and thus modulate substrate phosphorylation. Mutational analysis and microsequencing
techniques have been used to localize and identify new autophosphorylation site(s) of the EGF receptor. We have compared the
phosphopeptide maps of human EGF receptor, and two deletion mutants lacking 63 and 126 amino acids from the carboxyl-terminal
tail with the phosphopeptide maps of HER/neu and a chimeric EGF receptor containing the carboxyl-terminal tail of HER2/neu.
HER2/neu is highly homologous to the EGF receptor, and it probably functions as a growth factor receptor for as yet unidentified
growth factor. On the basis of this analysis, we have concluded that all autophosphorylation sites of EGF receptor and HER2/neu
are located in their carboxyl-terminal tails. Utilizing the EGF receptors with carboxyl-terminal deletions, we were also able
to identify tyr1086 as an additional autophosphorylation site of EGF receptor. Direct microsequencing of a phosphorylated
tryptic peptide from the human EGF receptor confirmed this assignment. |
| format | Article |
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various cellular substrates. The three known autophosphorylation sites of EGF receptor are located at the carboxyl-terminal
tail where they probably act to compete with and thus modulate substrate phosphorylation. Mutational analysis and microsequencing
techniques have been used to localize and identify new autophosphorylation site(s) of the EGF receptor. We have compared the
phosphopeptide maps of human EGF receptor, and two deletion mutants lacking 63 and 126 amino acids from the carboxyl-terminal
tail with the phosphopeptide maps of HER/neu and a chimeric EGF receptor containing the carboxyl-terminal tail of HER2/neu.
HER2/neu is highly homologous to the EGF receptor, and it probably functions as a growth factor receptor for as yet unidentified
growth factor. On the basis of this analysis, we have concluded that all autophosphorylation sites of EGF receptor and HER2/neu
are located in their carboxyl-terminal tails. Utilizing the EGF receptors with carboxyl-terminal deletions, we were also able
to identify tyr1086 as an additional autophosphorylation site of EGF receptor. Direct microsequencing of a phosphorylated
tryptic peptide from the human EGF receptor confirmed this assignment.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>PMID: 2543678</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Animals ; Biological and medical sciences ; C-terminus ; Cell receptors ; Cell structures and functions ; Cells, Cultured ; Chimera ; Chromosome Deletion ; Enzyme Activation ; ErbB Receptors - genetics ; ErbB Receptors - metabolism ; Fundamental and applied biological sciences. Psychology ; Genes ; HER/neu protein ; Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors ; Humans ; Mice ; Molecular and cellular biology ; Molecular Sequence Data ; Mutation ; neu ; Peptide Mapping ; Phosphopeptides - isolation & purification ; Phosphorylation ; Protein-Tyrosine Kinases - metabolism ; Transfection</subject><ispartof>The Journal of biological chemistry, 1989-06, Vol.264 (18), p.10667-10671</ispartof><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,782,786</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19419989$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2543678$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>MARGOLIS, B. L</creatorcontrib><creatorcontrib>LAX, I</creatorcontrib><creatorcontrib>KRIS, R</creatorcontrib><creatorcontrib>DOMBALAGIAN, M</creatorcontrib><creatorcontrib>HONEGGER, A. M</creatorcontrib><creatorcontrib>HOWK, R</creatorcontrib><creatorcontrib>GIVOL, D</creatorcontrib><creatorcontrib>ULLRICH, A</creatorcontrib><creatorcontrib>SCHLESSINGER, J</creatorcontrib><title>All autophosphorylation sites of epidermal growth factor (EGF) receptor and HER2/neu are located in their carboxyl-terminal tails. Identification of a novel site in EGF receptor</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Activation of the epidermal growth factor (EGF) receptor kinase leads to autophosphorylation and to the phosphorylation of
various cellular substrates. The three known autophosphorylation sites of EGF receptor are located at the carboxyl-terminal
tail where they probably act to compete with and thus modulate substrate phosphorylation. Mutational analysis and microsequencing
techniques have been used to localize and identify new autophosphorylation site(s) of the EGF receptor. We have compared the
phosphopeptide maps of human EGF receptor, and two deletion mutants lacking 63 and 126 amino acids from the carboxyl-terminal
tail with the phosphopeptide maps of HER/neu and a chimeric EGF receptor containing the carboxyl-terminal tail of HER2/neu.
HER2/neu is highly homologous to the EGF receptor, and it probably functions as a growth factor receptor for as yet unidentified
growth factor. On the basis of this analysis, we have concluded that all autophosphorylation sites of EGF receptor and HER2/neu
are located in their carboxyl-terminal tails. Utilizing the EGF receptors with carboxyl-terminal deletions, we were also able
to identify tyr1086 as an additional autophosphorylation site of EGF receptor. Direct microsequencing of a phosphorylated
tryptic peptide from the human EGF receptor confirmed this assignment.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>C-terminus</subject><subject>Cell receptors</subject><subject>Cell structures and functions</subject><subject>Cells, Cultured</subject><subject>Chimera</subject><subject>Chromosome Deletion</subject><subject>Enzyme Activation</subject><subject>ErbB Receptors - genetics</subject><subject>ErbB Receptors - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes</subject><subject>HER/neu protein</subject><subject>Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors</subject><subject>Humans</subject><subject>Mice</subject><subject>Molecular and cellular biology</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>neu</subject><subject>Peptide Mapping</subject><subject>Phosphopeptides - isolation & purification</subject><subject>Phosphorylation</subject><subject>Protein-Tyrosine Kinases - metabolism</subject><subject>Transfection</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kNtKxDAQhosouh4eQciFil5Um6bNNpci6wEEQRS8K9N0aiNpUpNU3cfyDY3u4sAwM8zH_w-zkcxoVrGUlfRlM5llWU5TkZfVTrLr_VsWoxB0O9nOy4LxeTVLvi-1JjAFO_bWx3RLDUFZQ7wK6IntCI6qRTeAJq_OfoaedCCDdeR0cXN9RhxKHH9HMC25XTzmFwYnAg6JthICtkQZEnpUjkhwjf1a6jREOWWiYACl_Tm5a9EE1Sm5co6eQIz9QP13xK9AtPp32k-2OtAeD9Z1L3m-Xjxd3ab3Dzd3V5f3aZ8LHtIyl1VVCmANspZlRVFy5JxWceCStZ0AQcvY5XKOWcEY7eYZK6TsRNNKIZHtJScr3dHZ9wl9qAflJWoNBu3ka1oyyhinETxcg1MzYFuPTg3glvX6x3F_vN6Dl6A7B0Yq_49RUVAhKhG5oxXXq9f-UzmsG2Vlj0Od86KmVU0zzufsB8UglA4</recordid><startdate>19890625</startdate><enddate>19890625</enddate><creator>MARGOLIS, B. 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M ; HOWK, R ; GIVOL, D ; ULLRICH, A ; SCHLESSINGER, J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-h296t-52c8859a3be3d304456e66183d36c3df9a9156c32c7e04331f7034ccf9bdc9ce3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>C-terminus</topic><topic>Cell receptors</topic><topic>Cell structures and functions</topic><topic>Cells, Cultured</topic><topic>Chimera</topic><topic>Chromosome Deletion</topic><topic>Enzyme Activation</topic><topic>ErbB Receptors - genetics</topic><topic>ErbB Receptors - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes</topic><topic>HER/neu protein</topic><topic>Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors</topic><topic>Humans</topic><topic>Mice</topic><topic>Molecular and cellular biology</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>neu</topic><topic>Peptide Mapping</topic><topic>Phosphopeptides - isolation & purification</topic><topic>Phosphorylation</topic><topic>Protein-Tyrosine Kinases - metabolism</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>MARGOLIS, B. L</creatorcontrib><creatorcontrib>LAX, I</creatorcontrib><creatorcontrib>KRIS, R</creatorcontrib><creatorcontrib>DOMBALAGIAN, M</creatorcontrib><creatorcontrib>HONEGGER, A. M</creatorcontrib><creatorcontrib>HOWK, R</creatorcontrib><creatorcontrib>GIVOL, D</creatorcontrib><creatorcontrib>ULLRICH, A</creatorcontrib><creatorcontrib>SCHLESSINGER, J</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>MARGOLIS, B. L</au><au>LAX, I</au><au>KRIS, R</au><au>DOMBALAGIAN, M</au><au>HONEGGER, A. M</au><au>HOWK, R</au><au>GIVOL, D</au><au>ULLRICH, A</au><au>SCHLESSINGER, J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>All autophosphorylation sites of epidermal growth factor (EGF) receptor and HER2/neu are located in their carboxyl-terminal tails. Identification of a novel site in EGF receptor</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1989-06-25</date><risdate>1989</risdate><volume>264</volume><issue>18</issue><spage>10667</spage><epage>10671</epage><pages>10667-10671</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Activation of the epidermal growth factor (EGF) receptor kinase leads to autophosphorylation and to the phosphorylation of
various cellular substrates. The three known autophosphorylation sites of EGF receptor are located at the carboxyl-terminal
tail where they probably act to compete with and thus modulate substrate phosphorylation. Mutational analysis and microsequencing
techniques have been used to localize and identify new autophosphorylation site(s) of the EGF receptor. We have compared the
phosphopeptide maps of human EGF receptor, and two deletion mutants lacking 63 and 126 amino acids from the carboxyl-terminal
tail with the phosphopeptide maps of HER/neu and a chimeric EGF receptor containing the carboxyl-terminal tail of HER2/neu.
HER2/neu is highly homologous to the EGF receptor, and it probably functions as a growth factor receptor for as yet unidentified
growth factor. On the basis of this analysis, we have concluded that all autophosphorylation sites of EGF receptor and HER2/neu
are located in their carboxyl-terminal tails. Utilizing the EGF receptors with carboxyl-terminal deletions, we were also able
to identify tyr1086 as an additional autophosphorylation site of EGF receptor. Direct microsequencing of a phosphorylated
tryptic peptide from the human EGF receptor confirmed this assignment.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>2543678</pmid><tpages>5</tpages></addata></record> |
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| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_15313361 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Biological and medical sciences C-terminus Cell receptors Cell structures and functions Cells, Cultured Chimera Chromosome Deletion Enzyme Activation ErbB Receptors - genetics ErbB Receptors - metabolism Fundamental and applied biological sciences. Psychology Genes HER/neu protein Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors Humans Mice Molecular and cellular biology Molecular Sequence Data Mutation neu Peptide Mapping Phosphopeptides - isolation & purification Phosphorylation Protein-Tyrosine Kinases - metabolism Transfection |
| title | All autophosphorylation sites of epidermal growth factor (EGF) receptor and HER2/neu are located in their carboxyl-terminal tails. Identification of a novel site in EGF receptor |
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