Src Kinase Associates with a Member of a Distinct Subfamily of Protein-Tyrosine Phosphatases Containing an Ezrin-Like Domain
A 6.2-kb full-length clone encoding a distinct protein-tyrosine phosphatase (PTP; EC 3.1.3.48), PTPD1, was isolated from a human skeletal muscle cDNA library. The cDNA encodes a protein of 1174 amino acids with N-terminal sequence homology to the ezrin-band 4.1-merlin-radixin protein family, which a...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1994-08, Vol.91 (16), p.7477-7481 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Møller, N P Møller, K B Lammers, R Kharitonenkov, A Sures, I Ullrich, A |
| description | A 6.2-kb full-length clone encoding a distinct protein-tyrosine phosphatase (PTP; EC 3.1.3.48), PTPD1, was isolated from a human skeletal muscle cDNA library. The cDNA encodes a protein of 1174 amino acids with N-terminal sequence homology to the ezrin-band 4.1-merlin-radixin protein family, which also includes the two PTPs H1 and MEG1. The PTP domain is positioned in the extreme C-terminal part of PTPD1, and there is an intervening sequence of about 580 residues without any apparent homology to known proteins separating the ezrin-like and the PTP domains. Thus, PTPD1 and the closely related, partially characterized, PTPD2 belong to the same family as PTPH1 and PTPMEG1, but because of distinct features constitute a different PTP subfamily. Northern blot analyses indicate that PTPD1 and PTPD2 are expressed in a variety of tissues. In transient coexpression experiments PTPD1 was found to be efficiently phosphorylated by and associated with the src kinase pp60src. |
| doi_str_mv | 10.1073/pnas.91.16.7477 |
| format | Article |
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The cDNA encodes a protein of 1174 amino acids with N-terminal sequence homology to the ezrin-band 4.1-merlin-radixin protein family, which also includes the two PTPs H1 and MEG1. The PTP domain is positioned in the extreme C-terminal part of PTPD1, and there is an intervening sequence of about 580 residues without any apparent homology to known proteins separating the ezrin-like and the PTP domains. Thus, PTPD1 and the closely related, partially characterized, PTPD2 belong to the same family as PTPH1 and PTPMEG1, but because of distinct features constitute a different PTP subfamily. Northern blot analyses indicate that PTPD1 and PTPD2 are expressed in a variety of tissues. 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The cDNA encodes a protein of 1174 amino acids with N-terminal sequence homology to the ezrin-band 4.1-merlin-radixin protein family, which also includes the two PTPs H1 and MEG1. The PTP domain is positioned in the extreme C-terminal part of PTPD1, and there is an intervening sequence of about 580 residues without any apparent homology to known proteins separating the ezrin-like and the PTP domains. Thus, PTPD1 and the closely related, partially characterized, PTPD2 belong to the same family as PTPH1 and PTPMEG1, but because of distinct features constitute a different PTP subfamily. Northern blot analyses indicate that PTPD1 and PTPD2 are expressed in a variety of tissues. In transient coexpression experiments PTPD1 was found to be efficiently phosphorylated by and associated with the src kinase pp60src.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Antibodies</subject><subject>Biochemistry</subject><subject>Cell lines</subject><subject>Cell membranes</subject><subject>Complementary DNA</subject><subject>Cytoskeletal Proteins</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>Fibroblasts</subject><subject>Focal adhesions</subject><subject>Humans</subject><subject>Molecular Sequence Data</subject><subject>Muscles</subject><subject>Muscular system</subject><subject>Phosphatases</subject><subject>Phosphoproteins - genetics</subject><subject>Protein Tyrosine Phosphatase, Non-Receptor Type 3</subject><subject>Protein Tyrosine Phosphatases - genetics</subject><subject>Protein Tyrosine Phosphatases - metabolism</subject><subject>Protein-Tyrosine Kinases - metabolism</subject><subject>Proteins</subject><subject>Proto-Oncogene Proteins pp60(c-src) - metabolism</subject><subject>RNA</subject><subject>RNA, Messenger - analysis</subject><subject>Sequence Homology, Amino Acid</subject><subject>Tissue Distribution</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kUtvEzEUhS0EKqGwZgPIYgGrSf32jMSmSstDBFGpZW15HE_jMGOntoc2iB-Po4SIsmBly-c7R9f3APAcoylGkp6svU7TBk-xmEom5QMwwajBlWANeggmCBFZ1Yywx-BJSiuEUMNrdASOJMeNrNEE_LqMBn52JcXC05SCcTrbBG9dXkINv9ihtRGGrtzPXMrOmwwvx7bTg-s32_eLGLJ1vrraxJCct_BiGdJ6qXMJTHAWfNbOO38NtYfnP2Mh5-67hWdhKO9PwaNO98k-25_H4Nv786vZx2r-9cOn2em8MqxuciVbygiyHe90Yyjr0AIxaTWxlDMkjOTdQtSSYWMklaSmWreCE9kSWmOEKKbH4N0udz22g10Y63PUvVpHN-i4UUE7dV_xbqmuww_FWNldsb_Z22O4GW3KanDJ2L7X3oYxKSkEQZzzAr7-B1yFMfryNUUQpjURUhToZAeZsrEUbXeYAyO17VRtO1UNVliobafF8fLv8Q_8vsSiv9rrW-Mf9V7A2_8Cqhv7Ptu7XMgXO3KVcogHlFDBaRntN09cv-M</recordid><startdate>19940802</startdate><enddate>19940802</enddate><creator>Møller, N P</creator><creator>Møller, K B</creator><creator>Lammers, R</creator><creator>Kharitonenkov, A</creator><creator>Sures, I</creator><creator>Ullrich, A</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>19940802</creationdate><title>Src Kinase Associates with a Member of a Distinct Subfamily of Protein-Tyrosine Phosphatases Containing an Ezrin-Like Domain</title><author>Møller, N P ; Møller, K B ; Lammers, R ; Kharitonenkov, A ; Sures, I ; Ullrich, A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c489t-7b3420ef5fa9c34f0d047ea2e35406c75fd68741cc737283aab6527b238100313</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Antibodies</topic><topic>Biochemistry</topic><topic>Cell lines</topic><topic>Cell membranes</topic><topic>Complementary DNA</topic><topic>Cytoskeletal Proteins</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>Fibroblasts</topic><topic>Focal adhesions</topic><topic>Humans</topic><topic>Molecular Sequence Data</topic><topic>Muscles</topic><topic>Muscular system</topic><topic>Phosphatases</topic><topic>Phosphoproteins - genetics</topic><topic>Protein Tyrosine Phosphatase, Non-Receptor Type 3</topic><topic>Protein Tyrosine Phosphatases - genetics</topic><topic>Protein Tyrosine Phosphatases - metabolism</topic><topic>Protein-Tyrosine Kinases - metabolism</topic><topic>Proteins</topic><topic>Proto-Oncogene Proteins pp60(c-src) - metabolism</topic><topic>RNA</topic><topic>RNA, Messenger - analysis</topic><topic>Sequence Homology, Amino Acid</topic><topic>Tissue Distribution</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Møller, N P</creatorcontrib><creatorcontrib>Møller, K B</creatorcontrib><creatorcontrib>Lammers, R</creatorcontrib><creatorcontrib>Kharitonenkov, A</creatorcontrib><creatorcontrib>Sures, I</creatorcontrib><creatorcontrib>Ullrich, A</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>Møller, N P</au><au>Møller, K B</au><au>Lammers, R</au><au>Kharitonenkov, A</au><au>Sures, I</au><au>Ullrich, A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Src Kinase Associates with a Member of a Distinct Subfamily of Protein-Tyrosine Phosphatases Containing an Ezrin-Like Domain</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1994-08-02</date><risdate>1994</risdate><volume>91</volume><issue>16</issue><spage>7477</spage><epage>7481</epage><pages>7477-7481</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>A 6.2-kb full-length clone encoding a distinct protein-tyrosine phosphatase (PTP; EC 3.1.3.48), PTPD1, was isolated from a human skeletal muscle cDNA library. The cDNA encodes a protein of 1174 amino acids with N-terminal sequence homology to the ezrin-band 4.1-merlin-radixin protein family, which also includes the two PTPs H1 and MEG1. The PTP domain is positioned in the extreme C-terminal part of PTPD1, and there is an intervening sequence of about 580 residues without any apparent homology to known proteins separating the ezrin-like and the PTP domains. Thus, PTPD1 and the closely related, partially characterized, PTPD2 belong to the same family as PTPH1 and PTPMEG1, but because of distinct features constitute a different PTP subfamily. Northern blot analyses indicate that PTPD1 and PTPD2 are expressed in a variety of tissues. In transient coexpression experiments PTPD1 was found to be efficiently phosphorylated by and associated with the src kinase pp60src.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>7519780</pmid><doi>10.1073/pnas.91.16.7477</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1994-08, Vol.91 (16), p.7477-7481 |
| issn | 0027-8424 1091-6490 |
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| source | MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry; JSTOR |
| subjects | Amino Acid Sequence Amino acids Antibodies Biochemistry Cell lines Cell membranes Complementary DNA Cytoskeletal Proteins Deoxyribonucleic acid DNA Fibroblasts Focal adhesions Humans Molecular Sequence Data Muscles Muscular system Phosphatases Phosphoproteins - genetics Protein Tyrosine Phosphatase, Non-Receptor Type 3 Protein Tyrosine Phosphatases - genetics Protein Tyrosine Phosphatases - metabolism Protein-Tyrosine Kinases - metabolism Proteins Proto-Oncogene Proteins pp60(c-src) - metabolism RNA RNA, Messenger - analysis Sequence Homology, Amino Acid Tissue Distribution |
| title | Src Kinase Associates with a Member of a Distinct Subfamily of Protein-Tyrosine Phosphatases Containing an Ezrin-Like Domain |
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