Daughter of Sevenless Is a Substrate of the Phosphotyrosine Phosphatase Corkscrew and Functions during Sevenless Signaling
The SH2 domain–containing phosphotyrosine phosphatase Corkscrew (CSW) is an essential component of the signaling pathway initiated by the activation of the sevenless receptor tyrosine kinase (SEV) during Drosophila eye development. We have used genetic and biochemical approaches to identify a substr...
Gespeichert in:
| Veröffentlicht in: | Cell 1996-06, Vol.85 (6), p.899-909 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 909 |
|---|---|
| container_issue | 6 |
| container_start_page | 899 |
| container_title | Cell |
| container_volume | 85 |
| creator | Herbst, Ronald Carroll, Pamela M Allard, John D Schilling, James Raabe, Thomas Simon, Michael A |
| description | The SH2 domain–containing phosphotyrosine phosphatase Corkscrew (CSW) is an essential component of the signaling pathway initiated by the activation of the
sevenless receptor tyrosine kinase (SEV) during Drosophila eye development. We have used genetic and biochemical approaches to identify a substrate for CSW. Expression of a catalytically inactive CSW was used to trap CSW in a complex with a 115 kDa tyrosine-phosphorylated substrate. This substrate was purified and identified as the product of the
daughter of sevenless (
dos) gene. Mutations of
dos were identified in a screen for dominant mutations which enhance the phenotype caused by overexpression of inactive CSW during photoreceptor development. Analysis of
dos mutations indicates that DOS is a positive component of the SEV signaling pathway and suggests that DOS dephosphorylation by CSW may be a key event during signaling by SEV. |
| doi_str_mv | 10.1016/S0092-8674(00)81273-8 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_78138237</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0092867400812738</els_id><sourcerecordid>15665772</sourcerecordid><originalsourceid>FETCH-LOGICAL-c504t-dafa3eb0d63e4bea47c5ab2ed08de12f34200f96e6510a978bf24184b406eb4d3</originalsourceid><addsrcrecordid>eNqFUcFuEzEUtBCohMInVPIJwWHh2eu1nRNCgUKlSiAFzpbXfpsYNnawvUXl69k0oeLW09N7M_NGmiHkgsEbBky-XQMseaOlEq8AXmvGVdvoR2TBYKkawRR_TBb3lKfkWSk_AEB3XXdGzrTUrNViQf58sNNmWzHTNNA13mAcsRR6Vail66kvNduKB6xukX7dprLfpnqbUwnx326rLUhXKf8sLuNvaqOnl1N0NaRYqJ9yiJv_Xq_DJtpxvj0nTwY7Fnxxmufk--XHb6vPzfWXT1er99eN60DUxtvBttiDly2KHq1QrrM9Rw_aI-NDKzjAsJQoOwZ2qXQ_cMG06AVI7IVvz8nL4999Tr8mLNXsQnE4jjZimopRhyh4qx4ksk7KTik-E7sj0c1BlIyD2eews_nWMDCHcsxdOeaQvAEwd-UYPesuTgZTv0N_rzq1MePvjjjOcdwEzKa4gNGhDxldNT6FBxz-AmtLoT8</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>15665772</pqid></control><display><type>article</type><title>Daughter of Sevenless Is a Substrate of the Phosphotyrosine Phosphatase Corkscrew and Functions during Sevenless Signaling</title><source>MEDLINE</source><source>Cell Press Free Archives</source><source>Elsevier ScienceDirect Journals</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><creator>Herbst, Ronald ; Carroll, Pamela M ; Allard, John D ; Schilling, James ; Raabe, Thomas ; Simon, Michael A</creator><creatorcontrib>Herbst, Ronald ; Carroll, Pamela M ; Allard, John D ; Schilling, James ; Raabe, Thomas ; Simon, Michael A</creatorcontrib><description>The SH2 domain–containing phosphotyrosine phosphatase Corkscrew (CSW) is an essential component of the signaling pathway initiated by the activation of the
sevenless receptor tyrosine kinase (SEV) during Drosophila eye development. We have used genetic and biochemical approaches to identify a substrate for CSW. Expression of a catalytically inactive CSW was used to trap CSW in a complex with a 115 kDa tyrosine-phosphorylated substrate. This substrate was purified and identified as the product of the
daughter of sevenless (
dos) gene. Mutations of
dos were identified in a screen for dominant mutations which enhance the phenotype caused by overexpression of inactive CSW during photoreceptor development. Analysis of
dos mutations indicates that DOS is a positive component of the SEV signaling pathway and suggests that DOS dephosphorylation by CSW may be a key event during signaling by SEV.</description><identifier>ISSN: 0092-8674</identifier><identifier>EISSN: 1097-4172</identifier><identifier>DOI: 10.1016/S0092-8674(00)81273-8</identifier><identifier>PMID: 8681384</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Drosophila ; Drosophila - enzymology ; Drosophila - growth & development ; Drosophila Proteins ; Eye Proteins - biosynthesis ; Eye Proteins - chemistry ; Eye Proteins - genetics ; Eye Proteins - isolation & purification ; Eye Proteins - metabolism ; Membrane Glycoproteins - biosynthesis ; Membrane Glycoproteins - genetics ; Membrane Glycoproteins - metabolism ; Molecular Sequence Data ; Molecular Weight ; Mutation ; Phosphorylation ; Photoreceptor Cells, Invertebrate - growth & development ; Protein Tyrosine Phosphatases - metabolism ; Protein Tyrosine Phosphatases, Non-Receptor ; Receptor Protein-Tyrosine Kinases - biosynthesis ; Receptor Protein-Tyrosine Kinases - genetics ; Receptor Protein-Tyrosine Kinases - metabolism ; Recombinant Fusion Proteins - metabolism ; Signal Transduction - physiology ; src Homology Domains - physiology ; Substrate Specificity</subject><ispartof>Cell, 1996-06, Vol.85 (6), p.899-909</ispartof><rights>1996 Cell Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c504t-dafa3eb0d63e4bea47c5ab2ed08de12f34200f96e6510a978bf24184b406eb4d3</citedby><cites>FETCH-LOGICAL-c504t-dafa3eb0d63e4bea47c5ab2ed08de12f34200f96e6510a978bf24184b406eb4d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0092867400812738$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8681384$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Herbst, Ronald</creatorcontrib><creatorcontrib>Carroll, Pamela M</creatorcontrib><creatorcontrib>Allard, John D</creatorcontrib><creatorcontrib>Schilling, James</creatorcontrib><creatorcontrib>Raabe, Thomas</creatorcontrib><creatorcontrib>Simon, Michael A</creatorcontrib><title>Daughter of Sevenless Is a Substrate of the Phosphotyrosine Phosphatase Corkscrew and Functions during Sevenless Signaling</title><title>Cell</title><addtitle>Cell</addtitle><description>The SH2 domain–containing phosphotyrosine phosphatase Corkscrew (CSW) is an essential component of the signaling pathway initiated by the activation of the
sevenless receptor tyrosine kinase (SEV) during Drosophila eye development. We have used genetic and biochemical approaches to identify a substrate for CSW. Expression of a catalytically inactive CSW was used to trap CSW in a complex with a 115 kDa tyrosine-phosphorylated substrate. This substrate was purified and identified as the product of the
daughter of sevenless (
dos) gene. Mutations of
dos were identified in a screen for dominant mutations which enhance the phenotype caused by overexpression of inactive CSW during photoreceptor development. Analysis of
dos mutations indicates that DOS is a positive component of the SEV signaling pathway and suggests that DOS dephosphorylation by CSW may be a key event during signaling by SEV.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Drosophila</subject><subject>Drosophila - enzymology</subject><subject>Drosophila - growth & development</subject><subject>Drosophila Proteins</subject><subject>Eye Proteins - biosynthesis</subject><subject>Eye Proteins - chemistry</subject><subject>Eye Proteins - genetics</subject><subject>Eye Proteins - isolation & purification</subject><subject>Eye Proteins - metabolism</subject><subject>Membrane Glycoproteins - biosynthesis</subject><subject>Membrane Glycoproteins - genetics</subject><subject>Membrane Glycoproteins - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Mutation</subject><subject>Phosphorylation</subject><subject>Photoreceptor Cells, Invertebrate - growth & development</subject><subject>Protein Tyrosine Phosphatases - metabolism</subject><subject>Protein Tyrosine Phosphatases, Non-Receptor</subject><subject>Receptor Protein-Tyrosine Kinases - biosynthesis</subject><subject>Receptor Protein-Tyrosine Kinases - genetics</subject><subject>Receptor Protein-Tyrosine Kinases - metabolism</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Signal Transduction - physiology</subject><subject>src Homology Domains - physiology</subject><subject>Substrate Specificity</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUcFuEzEUtBCohMInVPIJwWHh2eu1nRNCgUKlSiAFzpbXfpsYNnawvUXl69k0oeLW09N7M_NGmiHkgsEbBky-XQMseaOlEq8AXmvGVdvoR2TBYKkawRR_TBb3lKfkWSk_AEB3XXdGzrTUrNViQf58sNNmWzHTNNA13mAcsRR6Vail66kvNduKB6xukX7dprLfpnqbUwnx326rLUhXKf8sLuNvaqOnl1N0NaRYqJ9yiJv_Xq_DJtpxvj0nTwY7Fnxxmufk--XHb6vPzfWXT1er99eN60DUxtvBttiDly2KHq1QrrM9Rw_aI-NDKzjAsJQoOwZ2qXQ_cMG06AVI7IVvz8nL4999Tr8mLNXsQnE4jjZimopRhyh4qx4ksk7KTik-E7sj0c1BlIyD2eews_nWMDCHcsxdOeaQvAEwd-UYPesuTgZTv0N_rzq1MePvjjjOcdwEzKa4gNGhDxldNT6FBxz-AmtLoT8</recordid><startdate>19960614</startdate><enddate>19960614</enddate><creator>Herbst, Ronald</creator><creator>Carroll, Pamela M</creator><creator>Allard, John D</creator><creator>Schilling, James</creator><creator>Raabe, Thomas</creator><creator>Simon, Michael A</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><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>7SS</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19960614</creationdate><title>Daughter of Sevenless Is a Substrate of the Phosphotyrosine Phosphatase Corkscrew and Functions during Sevenless Signaling</title><author>Herbst, Ronald ; Carroll, Pamela M ; Allard, John D ; Schilling, James ; Raabe, Thomas ; Simon, Michael A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c504t-dafa3eb0d63e4bea47c5ab2ed08de12f34200f96e6510a978bf24184b406eb4d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Drosophila</topic><topic>Drosophila - enzymology</topic><topic>Drosophila - growth & development</topic><topic>Drosophila Proteins</topic><topic>Eye Proteins - biosynthesis</topic><topic>Eye Proteins - chemistry</topic><topic>Eye Proteins - genetics</topic><topic>Eye Proteins - isolation & purification</topic><topic>Eye Proteins - metabolism</topic><topic>Membrane Glycoproteins - biosynthesis</topic><topic>Membrane Glycoproteins - genetics</topic><topic>Membrane Glycoproteins - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Mutation</topic><topic>Phosphorylation</topic><topic>Photoreceptor Cells, Invertebrate - growth & development</topic><topic>Protein Tyrosine Phosphatases - metabolism</topic><topic>Protein Tyrosine Phosphatases, Non-Receptor</topic><topic>Receptor Protein-Tyrosine Kinases - biosynthesis</topic><topic>Receptor Protein-Tyrosine Kinases - genetics</topic><topic>Receptor Protein-Tyrosine Kinases - metabolism</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Signal Transduction - physiology</topic><topic>src Homology Domains - physiology</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Herbst, Ronald</creatorcontrib><creatorcontrib>Carroll, Pamela M</creatorcontrib><creatorcontrib>Allard, John D</creatorcontrib><creatorcontrib>Schilling, James</creatorcontrib><creatorcontrib>Raabe, Thomas</creatorcontrib><creatorcontrib>Simon, Michael A</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Herbst, Ronald</au><au>Carroll, Pamela M</au><au>Allard, John D</au><au>Schilling, James</au><au>Raabe, Thomas</au><au>Simon, Michael A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Daughter of Sevenless Is a Substrate of the Phosphotyrosine Phosphatase Corkscrew and Functions during Sevenless Signaling</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>1996-06-14</date><risdate>1996</risdate><volume>85</volume><issue>6</issue><spage>899</spage><epage>909</epage><pages>899-909</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><abstract>The SH2 domain–containing phosphotyrosine phosphatase Corkscrew (CSW) is an essential component of the signaling pathway initiated by the activation of the
sevenless receptor tyrosine kinase (SEV) during Drosophila eye development. We have used genetic and biochemical approaches to identify a substrate for CSW. Expression of a catalytically inactive CSW was used to trap CSW in a complex with a 115 kDa tyrosine-phosphorylated substrate. This substrate was purified and identified as the product of the
daughter of sevenless (
dos) gene. Mutations of
dos were identified in a screen for dominant mutations which enhance the phenotype caused by overexpression of inactive CSW during photoreceptor development. Analysis of
dos mutations indicates that DOS is a positive component of the SEV signaling pathway and suggests that DOS dephosphorylation by CSW may be a key event during signaling by SEV.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>8681384</pmid><doi>10.1016/S0092-8674(00)81273-8</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0092-8674 |
| ispartof | Cell, 1996-06, Vol.85 (6), p.899-909 |
| issn | 0092-8674 1097-4172 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_78138237 |
| source | MEDLINE; Cell Press Free Archives; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Amino Acid Sequence Animals Drosophila Drosophila - enzymology Drosophila - growth & development Drosophila Proteins Eye Proteins - biosynthesis Eye Proteins - chemistry Eye Proteins - genetics Eye Proteins - isolation & purification Eye Proteins - metabolism Membrane Glycoproteins - biosynthesis Membrane Glycoproteins - genetics Membrane Glycoproteins - metabolism Molecular Sequence Data Molecular Weight Mutation Phosphorylation Photoreceptor Cells, Invertebrate - growth & development Protein Tyrosine Phosphatases - metabolism Protein Tyrosine Phosphatases, Non-Receptor Receptor Protein-Tyrosine Kinases - biosynthesis Receptor Protein-Tyrosine Kinases - genetics Receptor Protein-Tyrosine Kinases - metabolism Recombinant Fusion Proteins - metabolism Signal Transduction - physiology src Homology Domains - physiology Substrate Specificity |
| title | Daughter of Sevenless Is a Substrate of the Phosphotyrosine Phosphatase Corkscrew and Functions during Sevenless Signaling |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-16T03%3A08%3A35IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Daughter%20of%20Sevenless%20Is%20a%20Substrate%20of%20the%20Phosphotyrosine%20Phosphatase%20Corkscrew%20and%20Functions%20during%20Sevenless%20Signaling&rft.jtitle=Cell&rft.au=Herbst,%20Ronald&rft.date=1996-06-14&rft.volume=85&rft.issue=6&rft.spage=899&rft.epage=909&rft.pages=899-909&rft.issn=0092-8674&rft.eissn=1097-4172&rft_id=info:doi/10.1016/S0092-8674(00)81273-8&rft_dat=%3Cproquest_cross%3E15665772%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=15665772&rft_id=info:pmid/8681384&rft_els_id=S0092867400812738&rfr_iscdi=true |