Physical association between Src homology 3 elements and the protein product of the c-cbl proto-oncogene
To investigate the nature of proteins recognized by Src homology 3 (SH3) domains, a cDNA expression library was prepared from macrophages and screened with a probe representing the three SH3 domains of p47nck. Two clones were isolated, and one, designated SAKAP I (for Src A box Nck-associated protei...
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| Veröffentlicht in: | The Journal of biological chemistry 1994-07, Vol.269 (26), p.17363-17366 |
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| container_issue | 26 |
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| container_title | The Journal of biological chemistry |
| container_volume | 269 |
| creator | RIVERO-LEZCANO, O. M SAMESHIMA, J. H MARCILLA, A ROBBINS, K. C |
| description | To investigate the nature of proteins recognized by Src homology 3 (SH3) domains, a cDNA expression library was prepared from
macrophages and screened with a probe representing the three SH3 domains of p47nck. Two clones were isolated, and one, designated
SAKAP I (for Src A box Nck-associated protein I), contained the carboxyl-terminal half of the cbl proto-oncogene product.
Studies in vitro demonstrated reactivity between SAKAP I and SH3 domains derived from a variety of molecules. Wide variations
in this assay suggested a high degree of specificity inherent in SAKAP I binding. Moreover, it was possible to demonstrate
an in vivo association between p47nck and p120c-cbl in HL60 cells. These findings suggest that proteins containing SH3 elements
regulate Cbl function. |
| doi_str_mv | 10.1016/s0021-9258(17)32443-2 |
| format | Article |
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macrophages and screened with a probe representing the three SH3 domains of p47nck. Two clones were isolated, and one, designated
SAKAP I (for Src A box Nck-associated protein I), contained the carboxyl-terminal half of the cbl proto-oncogene product.
Studies in vitro demonstrated reactivity between SAKAP I and SH3 domains derived from a variety of molecules. Wide variations
in this assay suggested a high degree of specificity inherent in SAKAP I binding. Moreover, it was possible to demonstrate
an in vivo association between p47nck and p120c-cbl in HL60 cells. These findings suggest that proteins containing SH3 elements
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macrophages and screened with a probe representing the three SH3 domains of p47nck. Two clones were isolated, and one, designated
SAKAP I (for Src A box Nck-associated protein I), contained the carboxyl-terminal half of the cbl proto-oncogene product.
Studies in vitro demonstrated reactivity between SAKAP I and SH3 domains derived from a variety of molecules. Wide variations
in this assay suggested a high degree of specificity inherent in SAKAP I binding. Moreover, it was possible to demonstrate
an in vivo association between p47nck and p120c-cbl in HL60 cells. These findings suggest that proteins containing SH3 elements
regulate Cbl function.</description><subject>Adaptor Proteins, Signal Transducing</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Cell Line</subject><subject>Cell physiology</subject><subject>Cloning, Molecular</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Mice</subject><subject>Molecular and cellular biology</subject><subject>Oncogene Proteins - genetics</subject><subject>Oncogene Proteins - metabolism</subject><subject>Proto-Oncogene Proteins - genetics</subject><subject>Proto-Oncogene Proteins - metabolism</subject><subject>Proto-Oncogene Proteins c-cbl</subject><subject>Proto-Oncogene Proteins pp60(c-src) - genetics</subject><subject>Proto-Oncogene Proteins pp60(c-src) - metabolism</subject><subject>Signal transduction</subject><subject>Ubiquitin-Protein Ligases</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUV1r3DAQFKUhvSb9CQE9lNI8ONGnJT2GkKaFQANJoG9CltdnFVtKLB_h_n3ky3H0rQvLIs3sDswgdEbJBSW0vsyEMFoZJvV3qs45E4JX7ANaUaJ5xSX98xGtDpRP6HPOf0kpYegxOlaSKm7UCvX3_TYH7wbsck4-uDmkiBuYXwEifpg87tOYhrTeYo5hgBHinLGLLZ57wM9TmiHEZbYbP-PU7b595ZthB6YqRZ_WEOEUHXVuyPBlP0_Q04-bx-uf1d3v21_XV3eVF4yySred9G3nBeVSgXCqMdo3rZLaOEZAK0lELYguT6eUNqxY0UoqfeOMNl7wE_Tt_W6Rf9lAnu0YsodhcBHSJltVSyW0MP8l0loJxsVyUb4T_ZRynqCzz1MY3bS1lNglCvuw-GwXny1VdheFZWXvbC-waUZoD1t77wv-dY-7XALoJhd9yAdasUOaf2l9WPevYQLbhOR7GC2rTekiyWvO3wCvYpzK</recordid><startdate>19940701</startdate><enddate>19940701</enddate><creator>RIVERO-LEZCANO, O. 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Psychology</topic><topic>Mice</topic><topic>Molecular and cellular biology</topic><topic>Oncogene Proteins - genetics</topic><topic>Oncogene Proteins - metabolism</topic><topic>Proto-Oncogene Proteins - genetics</topic><topic>Proto-Oncogene Proteins - metabolism</topic><topic>Proto-Oncogene Proteins c-cbl</topic><topic>Proto-Oncogene Proteins pp60(c-src) - genetics</topic><topic>Proto-Oncogene Proteins pp60(c-src) - metabolism</topic><topic>Signal transduction</topic><topic>Ubiquitin-Protein Ligases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>RIVERO-LEZCANO, O. M</creatorcontrib><creatorcontrib>SAMESHIMA, J. H</creatorcontrib><creatorcontrib>MARCILLA, A</creatorcontrib><creatorcontrib>ROBBINS, K. 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C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Physical association between Src homology 3 elements and the protein product of the c-cbl proto-oncogene</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1994-07-01</date><risdate>1994</risdate><volume>269</volume><issue>26</issue><spage>17363</spage><epage>17366</epage><pages>17363-17366</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>To investigate the nature of proteins recognized by Src homology 3 (SH3) domains, a cDNA expression library was prepared from
macrophages and screened with a probe representing the three SH3 domains of p47nck. Two clones were isolated, and one, designated
SAKAP I (for Src A box Nck-associated protein I), contained the carboxyl-terminal half of the cbl proto-oncogene product.
Studies in vitro demonstrated reactivity between SAKAP I and SH3 domains derived from a variety of molecules. Wide variations
in this assay suggested a high degree of specificity inherent in SAKAP I binding. Moreover, it was possible to demonstrate
an in vivo association between p47nck and p120c-cbl in HL60 cells. These findings suggest that proteins containing SH3 elements
regulate Cbl function.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>7517397</pmid><doi>10.1016/s0021-9258(17)32443-2</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1994-07, Vol.269 (26), p.17363-17366 |
| issn | 0021-9258 1083-351X |
| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Adaptor Proteins, Signal Transducing Animals Binding Sites Biological and medical sciences Cell Line Cell physiology Cloning, Molecular Fundamental and applied biological sciences. Psychology Mice Molecular and cellular biology Oncogene Proteins - genetics Oncogene Proteins - metabolism Proto-Oncogene Proteins - genetics Proto-Oncogene Proteins - metabolism Proto-Oncogene Proteins c-cbl Proto-Oncogene Proteins pp60(c-src) - genetics Proto-Oncogene Proteins pp60(c-src) - metabolism Signal transduction Ubiquitin-Protein Ligases |
| title | Physical association between Src homology 3 elements and the protein product of the c-cbl proto-oncogene |
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