A Drosophila Protein-tyrosine Phosphatase Associates with an Adapter Protein Required for Axonal Guidance
We have used the yeast two-hybrid system to isolate a novel Drosophila adapter protein, which interacts with the Drosophila protein-tyrosine phosphatase (PTP) dPTP61F. Absence of this protein in Drosophila causes the mutant photoreceptor axon phenotype dreadlocks (dock) (Garrity, P. A., Rao, Y., Sal...
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| Veröffentlicht in: | The Journal of biological chemistry 1996-07, Vol.271 (29), p.17002-17005 |
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| creator | Clemens, James C. Ursuliak, Zenovia Clemens, Kristina K. Price, James V. Dixon, Jack E. |
| description | We have used the yeast two-hybrid system to isolate a novel Drosophila adapter protein, which interacts with the Drosophila protein-tyrosine phosphatase (PTP) dPTP61F. Absence of this protein in Drosophila causes the mutant photoreceptor axon phenotype dreadlocks (dock) (Garrity, P. A., Rao, Y., Salecker, I., and Zipursky, S. L. (1996) Cell 85, 639-650). Dock is similar to the mammalian oncoprotein Nck and contains three Src homology 3 (SH3) domains and one Src homology 2 (SH2) domain. The interaction of dPTP61F with Dock was confirmed in vivo by immune precipitation experiments. A sequence containing five PXXP motifs from the non-catalytic domain of the PTP is sufficient for interaction with Dock. This suggests that binding to the PTP is mediated by one or more of the SH3 domains of Dock. Immune precipitations of Dock also co-precipitate two tyrosine-phosphorylated proteins having molecular masses of 190 and 145 kDa. Interactions between Dock and these tyrosine-phosphorylated proteins are likely mediated by the Dock SH2 domain. These findings identify potential signal-transducing partners of Dock and propose a role for dPTP61F and the unidentified phosphoproteins in axonal guidance. |
| doi_str_mv | 10.1074/jbc.271.29.17002 |
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Absence of this protein in Drosophila causes the mutant photoreceptor axon phenotype dreadlocks (dock) (Garrity, P. A., Rao, Y., Salecker, I., and Zipursky, S. L. (1996) Cell 85, 639-650). Dock is similar to the mammalian oncoprotein Nck and contains three Src homology 3 (SH3) domains and one Src homology 2 (SH2) domain. The interaction of dPTP61F with Dock was confirmed in vivo by immune precipitation experiments. A sequence containing five PXXP motifs from the non-catalytic domain of the PTP is sufficient for interaction with Dock. This suggests that binding to the PTP is mediated by one or more of the SH3 domains of Dock. Immune precipitations of Dock also co-precipitate two tyrosine-phosphorylated proteins having molecular masses of 190 and 145 kDa. Interactions between Dock and these tyrosine-phosphorylated proteins are likely mediated by the Dock SH2 domain. These findings identify potential signal-transducing partners of Dock and propose a role for dPTP61F and the unidentified phosphoproteins in axonal guidance.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.271.29.17002</identifier><identifier>PMID: 8663600</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; ANIMAL PROTEINS ; Animals ; Axons - physiology ; BINDING ; CELLS ; CELLULE ; CELULAS ; Consensus Sequence ; DROSOPHILA ; Drosophila melanogaster - genetics ; Drosophila melanogaster - physiology ; Drosophila Proteins ; Embryo, Nonmammalian ; ESTERASAS ; ESTERASE ; ESTERASES ; FOTORECEPTORES ; Gene Expression Regulation, Developmental ; Gene Library ; Humans ; Larva ; Mammals ; MOLECULAR SEQUENCE DATA ; NERF ; Nerve Tissue Proteins - biosynthesis ; Nerve Tissue Proteins - chemistry ; Nerve Tissue Proteins - metabolism ; NERVES ; NERVIOS ; Oncogene Proteins - chemistry ; PHOSPHOPROTEIN PHOSPHATASE ; PHOTORECEPTEUR ; Photoreceptor Cells, Invertebrate - physiology ; PHOTORECEPTORS ; Polymerase Chain Reaction ; Protein Tyrosine Phosphatases - metabolism ; PROTEINAS ; PROTEINE ; PROTEINS ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - chemistry ; Recombinant Proteins - metabolism ; RNA, Messenger - biosynthesis ; Sequence Homology, Amino Acid ; src Homology Domains ; TIROSINA ; Transcription, Genetic ; TYROSINE</subject><ispartof>The Journal of biological chemistry, 1996-07, Vol.271 (29), p.17002-17005</ispartof><rights>1996 © 1996 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8663600$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Clemens, James C.</creatorcontrib><creatorcontrib>Ursuliak, Zenovia</creatorcontrib><creatorcontrib>Clemens, Kristina K.</creatorcontrib><creatorcontrib>Price, James V.</creatorcontrib><creatorcontrib>Dixon, Jack E.</creatorcontrib><title>A Drosophila Protein-tyrosine Phosphatase Associates with an Adapter Protein Required for Axonal Guidance</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>We have used the yeast two-hybrid system to isolate a novel Drosophila adapter protein, which interacts with the Drosophila protein-tyrosine phosphatase (PTP) dPTP61F. Absence of this protein in Drosophila causes the mutant photoreceptor axon phenotype dreadlocks (dock) (Garrity, P. A., Rao, Y., Salecker, I., and Zipursky, S. L. (1996) Cell 85, 639-650). Dock is similar to the mammalian oncoprotein Nck and contains three Src homology 3 (SH3) domains and one Src homology 2 (SH2) domain. The interaction of dPTP61F with Dock was confirmed in vivo by immune precipitation experiments. A sequence containing five PXXP motifs from the non-catalytic domain of the PTP is sufficient for interaction with Dock. This suggests that binding to the PTP is mediated by one or more of the SH3 domains of Dock. Immune precipitations of Dock also co-precipitate two tyrosine-phosphorylated proteins having molecular masses of 190 and 145 kDa. Interactions between Dock and these tyrosine-phosphorylated proteins are likely mediated by the Dock SH2 domain. These findings identify potential signal-transducing partners of Dock and propose a role for dPTP61F and the unidentified phosphoproteins in axonal guidance.</description><subject>Adaptor Proteins, Signal Transducing</subject><subject>Amino Acid Sequence</subject><subject>ANIMAL PROTEINS</subject><subject>Animals</subject><subject>Axons - physiology</subject><subject>BINDING</subject><subject>CELLS</subject><subject>CELLULE</subject><subject>CELULAS</subject><subject>Consensus Sequence</subject><subject>DROSOPHILA</subject><subject>Drosophila melanogaster - genetics</subject><subject>Drosophila melanogaster - physiology</subject><subject>Drosophila Proteins</subject><subject>Embryo, Nonmammalian</subject><subject>ESTERASAS</subject><subject>ESTERASE</subject><subject>ESTERASES</subject><subject>FOTORECEPTORES</subject><subject>Gene Expression Regulation, Developmental</subject><subject>Gene Library</subject><subject>Humans</subject><subject>Larva</subject><subject>Mammals</subject><subject>MOLECULAR SEQUENCE DATA</subject><subject>NERF</subject><subject>Nerve Tissue Proteins - biosynthesis</subject><subject>Nerve Tissue Proteins - chemistry</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>NERVES</subject><subject>NERVIOS</subject><subject>Oncogene Proteins - chemistry</subject><subject>PHOSPHOPROTEIN PHOSPHATASE</subject><subject>PHOTORECEPTEUR</subject><subject>Photoreceptor Cells, Invertebrate - physiology</subject><subject>PHOTORECEPTORS</subject><subject>Polymerase Chain Reaction</subject><subject>Protein Tyrosine Phosphatases - metabolism</subject><subject>PROTEINAS</subject><subject>PROTEINE</subject><subject>PROTEINS</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - metabolism</subject><subject>RNA, Messenger - biosynthesis</subject><subject>Sequence Homology, Amino Acid</subject><subject>src Homology Domains</subject><subject>TIROSINA</subject><subject>Transcription, Genetic</subject><subject>TYROSINE</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkUFv1DAQhS1EVbaFOxckHxC3LHa8TmJuUUsLUqVWhUrcrIk9aVxl49R2KP33uN1FqHMZad7Mk943hLznbM1Zvfl815l1WfN1qda8Zqx8RVacNaIQkv96TVZ5wgtVyuYNOYrxjuXaKH5IDpuqEhVjK-Jaehp89PPgRqBXwSd0U5Ee88xNSK8GH-cBEkSkbYzeOEgY6YNLA4WJthbmhOHfHb3G-8UFtLT3gbZ__AQjPV-chcngW3LQwxjx3b4fk5uzrz9PvhUXl-ffT9qLAgVrUlF2SkqUwlYdGMllLS0HaZit-lJVYGXPzIYZ7BshKkCwSrAO-kyjQtGDEMfk0853Dv5-wZj01kWD4wgT-iXquuG1kPXT4of94tJt0eo5uC2ER71nk_WPO31wt8NDjqU7582AW52J61LpZ-L_bXrwGm6Di_rmB1eqZpI3z_qXnY459G-HQUfjMAOx2dIkbb3TnOmnd-r8zpfmfwGp_I_y</recordid><startdate>19960719</startdate><enddate>19960719</enddate><creator>Clemens, James C.</creator><creator>Ursuliak, Zenovia</creator><creator>Clemens, Kristina K.</creator><creator>Price, James V.</creator><creator>Dixon, Jack E.</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>19960719</creationdate><title>A Drosophila Protein-tyrosine Phosphatase Associates with an Adapter Protein Required for Axonal Guidance</title><author>Clemens, James C. ; Ursuliak, Zenovia ; Clemens, Kristina K. ; Price, James V. ; Dixon, Jack E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-e308t-2b955e53d6bac51575d1a5c0d6f296ad5f0c40cef8336aead930baf1076e3fa33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Adaptor Proteins, Signal Transducing</topic><topic>Amino Acid Sequence</topic><topic>ANIMAL PROTEINS</topic><topic>Animals</topic><topic>Axons - physiology</topic><topic>BINDING</topic><topic>CELLS</topic><topic>CELLULE</topic><topic>CELULAS</topic><topic>Consensus Sequence</topic><topic>DROSOPHILA</topic><topic>Drosophila melanogaster - genetics</topic><topic>Drosophila melanogaster - physiology</topic><topic>Drosophila Proteins</topic><topic>Embryo, Nonmammalian</topic><topic>ESTERASAS</topic><topic>ESTERASE</topic><topic>ESTERASES</topic><topic>FOTORECEPTORES</topic><topic>Gene Expression Regulation, Developmental</topic><topic>Gene Library</topic><topic>Humans</topic><topic>Larva</topic><topic>Mammals</topic><topic>MOLECULAR SEQUENCE DATA</topic><topic>NERF</topic><topic>Nerve Tissue Proteins - biosynthesis</topic><topic>Nerve Tissue Proteins - chemistry</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>NERVES</topic><topic>NERVIOS</topic><topic>Oncogene Proteins - chemistry</topic><topic>PHOSPHOPROTEIN PHOSPHATASE</topic><topic>PHOTORECEPTEUR</topic><topic>Photoreceptor Cells, Invertebrate - physiology</topic><topic>PHOTORECEPTORS</topic><topic>Polymerase Chain Reaction</topic><topic>Protein Tyrosine Phosphatases - metabolism</topic><topic>PROTEINAS</topic><topic>PROTEINE</topic><topic>PROTEINS</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - metabolism</topic><topic>RNA, Messenger - biosynthesis</topic><topic>Sequence Homology, Amino Acid</topic><topic>src Homology Domains</topic><topic>TIROSINA</topic><topic>Transcription, Genetic</topic><topic>TYROSINE</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Clemens, James C.</creatorcontrib><creatorcontrib>Ursuliak, Zenovia</creatorcontrib><creatorcontrib>Clemens, Kristina K.</creatorcontrib><creatorcontrib>Price, James V.</creatorcontrib><creatorcontrib>Dixon, Jack E.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Clemens, James C.</au><au>Ursuliak, Zenovia</au><au>Clemens, Kristina K.</au><au>Price, James V.</au><au>Dixon, Jack E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Drosophila Protein-tyrosine Phosphatase Associates with an Adapter Protein Required for Axonal Guidance</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1996-07-19</date><risdate>1996</risdate><volume>271</volume><issue>29</issue><spage>17002</spage><epage>17005</epage><pages>17002-17005</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>We have used the yeast two-hybrid system to isolate a novel Drosophila adapter protein, which interacts with the Drosophila protein-tyrosine phosphatase (PTP) dPTP61F. Absence of this protein in Drosophila causes the mutant photoreceptor axon phenotype dreadlocks (dock) (Garrity, P. A., Rao, Y., Salecker, I., and Zipursky, S. L. (1996) Cell 85, 639-650). Dock is similar to the mammalian oncoprotein Nck and contains three Src homology 3 (SH3) domains and one Src homology 2 (SH2) domain. The interaction of dPTP61F with Dock was confirmed in vivo by immune precipitation experiments. A sequence containing five PXXP motifs from the non-catalytic domain of the PTP is sufficient for interaction with Dock. This suggests that binding to the PTP is mediated by one or more of the SH3 domains of Dock. Immune precipitations of Dock also co-precipitate two tyrosine-phosphorylated proteins having molecular masses of 190 and 145 kDa. Interactions between Dock and these tyrosine-phosphorylated proteins are likely mediated by the Dock SH2 domain. These findings identify potential signal-transducing partners of Dock and propose a role for dPTP61F and the unidentified phosphoproteins in axonal guidance.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>8663600</pmid><doi>10.1074/jbc.271.29.17002</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adaptor Proteins, Signal Transducing Amino Acid Sequence ANIMAL PROTEINS Animals Axons - physiology BINDING CELLS CELLULE CELULAS Consensus Sequence DROSOPHILA Drosophila melanogaster - genetics Drosophila melanogaster - physiology Drosophila Proteins Embryo, Nonmammalian ESTERASAS ESTERASE ESTERASES FOTORECEPTORES Gene Expression Regulation, Developmental Gene Library Humans Larva Mammals MOLECULAR SEQUENCE DATA NERF Nerve Tissue Proteins - biosynthesis Nerve Tissue Proteins - chemistry Nerve Tissue Proteins - metabolism NERVES NERVIOS Oncogene Proteins - chemistry PHOSPHOPROTEIN PHOSPHATASE PHOTORECEPTEUR Photoreceptor Cells, Invertebrate - physiology PHOTORECEPTORS Polymerase Chain Reaction Protein Tyrosine Phosphatases - metabolism PROTEINAS PROTEINE PROTEINS Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Recombinant Proteins - metabolism RNA, Messenger - biosynthesis Sequence Homology, Amino Acid src Homology Domains TIROSINA Transcription, Genetic TYROSINE |
| title | A Drosophila Protein-tyrosine Phosphatase Associates with an Adapter Protein Required for Axonal Guidance |
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