Eintrag weiter verarbeiten
Phospho‐tyrosine dependent protein–protein interaction network
Gespeichert in:
| Zeitschriftentitel: | Molecular Systems Biology |
|---|---|
| Personen und Körperschaften: | , , , , , , |
| In: | Molecular Systems Biology, 11, 2015, 3 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Springer Science and Business Media LLC
|
| Schlagwörter: |
| author_facet |
Grossmann, Arndt Benlasfer, Nouhad Birth, Petra Hegele, Anna Wachsmuth, Franziska Apelt, Luise Stelzl, Ulrich Grossmann, Arndt Benlasfer, Nouhad Birth, Petra Hegele, Anna Wachsmuth, Franziska Apelt, Luise Stelzl, Ulrich |
|---|---|
| author |
Grossmann, Arndt Benlasfer, Nouhad Birth, Petra Hegele, Anna Wachsmuth, Franziska Apelt, Luise Stelzl, Ulrich |
| spellingShingle |
Grossmann, Arndt Benlasfer, Nouhad Birth, Petra Hegele, Anna Wachsmuth, Franziska Apelt, Luise Stelzl, Ulrich Molecular Systems Biology Phospho‐tyrosine dependent protein–protein interaction network Applied Mathematics Computational Theory and Mathematics General Agricultural and Biological Sciences General Immunology and Microbiology General Biochemistry, Genetics and Molecular Biology Information Systems |
| author_sort |
grossmann, arndt |
| spelling |
Grossmann, Arndt Benlasfer, Nouhad Birth, Petra Hegele, Anna Wachsmuth, Franziska Apelt, Luise Stelzl, Ulrich 1744-4292 1744-4292 Springer Science and Business Media LLC Applied Mathematics Computational Theory and Mathematics General Agricultural and Biological Sciences General Immunology and Microbiology General Biochemistry, Genetics and Molecular Biology Information Systems http://dx.doi.org/10.15252/msb.20145968 <jats:title>Abstract</jats:title><jats:p>Post‐translational protein modifications, such as tyrosine phosphorylation, regulate protein–protein interactions (<jats:styled-content style="fixed-case">PPI</jats:styled-content>s) critical for signal processing and cellular phenotypes. We extended an established yeast two‐hybrid system employing human protein kinases for the analyses of phospho‐tyrosine (<jats:styled-content style="fixed-case">pY</jats:styled-content>)‐dependent <jats:styled-content style="fixed-case">PPI</jats:styled-content>s in a direct experimental, large‐scale approach. We identified 292 mostly novel <jats:styled-content style="fixed-case">pY</jats:styled-content>‐dependent <jats:styled-content style="fixed-case">PPI</jats:styled-content>s which showed high specificity with respect to kinases and interacting proteins and validated a large fraction in co‐immunoprecipitation experiments from mammalian cells. About one‐sixth of the interactions are mediated by known linear sequence binding motifs while the majority of <jats:styled-content style="fixed-case">pY</jats:styled-content>‐<jats:styled-content style="fixed-case">PPI</jats:styled-content>s are mediated by other linear epitopes or governed by alternative recognition modes. Network analysis revealed that <jats:styled-content style="fixed-case">pY</jats:styled-content>‐mediated recognition events are tied to a highly connected protein module dedicated to signaling and cell growth pathways related to cancer. Using binding assays, protein complementation and phenotypic readouts to characterize the <jats:styled-content style="fixed-case">pY</jats:styled-content>‐dependent interactions of <jats:styled-content style="fixed-case">TSPAN</jats:styled-content>2 (tetraspanin 2) and <jats:styled-content style="fixed-case">GRB</jats:styled-content>2 or <jats:styled-content style="fixed-case">PIK</jats:styled-content>3R3 (p55γ), we exemplarily provide evidence that the two <jats:styled-content style="fixed-case">pY</jats:styled-content>‐dependent <jats:styled-content style="fixed-case">PPI</jats:styled-content>s dictate cellular cancer phenotypes.</jats:p> Phospho‐tyrosine dependent protein–protein interaction network Molecular Systems Biology |
| doi_str_mv |
10.15252/msb.20145968 |
| facet_avail |
Online Free |
| finc_class_facet |
Mathematik Informatik |
| format |
ElectronicArticle |
| fullrecord |
blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTUyNTIvbXNiLjIwMTQ1OTY4 |
| id |
ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTUyNTIvbXNiLjIwMTQ1OTY4 |
| institution |
DE-Gla1 DE-Zi4 DE-15 DE-Pl11 DE-Rs1 DE-105 DE-14 DE-Ch1 DE-L229 DE-D275 DE-Bn3 DE-Brt1 DE-Zwi2 DE-D161 |
| imprint |
Springer Science and Business Media LLC, 2015 |
| imprint_str_mv |
Springer Science and Business Media LLC, 2015 |
| issn |
1744-4292 |
| issn_str_mv |
1744-4292 |
| language |
English |
| mega_collection |
Springer Science and Business Media LLC (CrossRef) |
| match_str |
grossmann2015phosphotyrosinedependentproteinproteininteractionnetwork |
| publishDateSort |
2015 |
| publisher |
Springer Science and Business Media LLC |
| recordtype |
ai |
| record_format |
ai |
| series |
Molecular Systems Biology |
| source_id |
49 |
| title |
Phospho‐tyrosine dependent protein–protein interaction network |
| title_unstemmed |
Phospho‐tyrosine dependent protein–protein interaction network |
| title_full |
Phospho‐tyrosine dependent protein–protein interaction network |
| title_fullStr |
Phospho‐tyrosine dependent protein–protein interaction network |
| title_full_unstemmed |
Phospho‐tyrosine dependent protein–protein interaction network |
| title_short |
Phospho‐tyrosine dependent protein–protein interaction network |
| title_sort |
phospho‐tyrosine dependent protein–protein interaction network |
| topic |
Applied Mathematics Computational Theory and Mathematics General Agricultural and Biological Sciences General Immunology and Microbiology General Biochemistry, Genetics and Molecular Biology Information Systems |
| url |
http://dx.doi.org/10.15252/msb.20145968 |
| publishDate |
2015 |
| physical |
|
| description |
<jats:title>Abstract</jats:title><jats:p>Post‐translational protein modifications, such as tyrosine phosphorylation, regulate protein–protein interactions (<jats:styled-content style="fixed-case">PPI</jats:styled-content>s) critical for signal processing and cellular phenotypes. We extended an established yeast two‐hybrid system employing human protein kinases for the analyses of phospho‐tyrosine (<jats:styled-content style="fixed-case">pY</jats:styled-content>)‐dependent <jats:styled-content style="fixed-case">PPI</jats:styled-content>s in a direct experimental, large‐scale approach. We identified 292 mostly novel <jats:styled-content style="fixed-case">pY</jats:styled-content>‐dependent <jats:styled-content style="fixed-case">PPI</jats:styled-content>s which showed high specificity with respect to kinases and interacting proteins and validated a large fraction in co‐immunoprecipitation experiments from mammalian cells. About one‐sixth of the interactions are mediated by known linear sequence binding motifs while the majority of <jats:styled-content style="fixed-case">pY</jats:styled-content>‐<jats:styled-content style="fixed-case">PPI</jats:styled-content>s are mediated by other linear epitopes or governed by alternative recognition modes. Network analysis revealed that <jats:styled-content style="fixed-case">pY</jats:styled-content>‐mediated recognition events are tied to a highly connected protein module dedicated to signaling and cell growth pathways related to cancer. Using binding assays, protein complementation and phenotypic readouts to characterize the <jats:styled-content style="fixed-case">pY</jats:styled-content>‐dependent interactions of <jats:styled-content style="fixed-case">TSPAN</jats:styled-content>2 (tetraspanin 2) and <jats:styled-content style="fixed-case">GRB</jats:styled-content>2 or <jats:styled-content style="fixed-case">PIK</jats:styled-content>3R3 (p55γ), we exemplarily provide evidence that the two <jats:styled-content style="fixed-case">pY</jats:styled-content>‐dependent <jats:styled-content style="fixed-case">PPI</jats:styled-content>s dictate cellular cancer phenotypes.</jats:p> |
| container_issue |
3 |
| container_start_page |
0 |
| container_title |
Molecular Systems Biology |
| container_volume |
11 |
| format_de105 |
Article, E-Article |
| format_de14 |
Article, E-Article |
| format_de15 |
Article, E-Article |
| format_de520 |
Article, E-Article |
| format_de540 |
Article, E-Article |
| format_dech1 |
Article, E-Article |
| format_ded117 |
Article, E-Article |
| format_degla1 |
E-Article |
| format_del152 |
Buch |
| format_del189 |
Article, E-Article |
| format_dezi4 |
Article |
| format_dezwi2 |
Article, E-Article |
| format_finc |
Article, E-Article |
| format_nrw |
Article, E-Article |
| _version_ |
1792348203222302728 |
| geogr_code |
not assigned |
| last_indexed |
2024-03-01T18:07:12.01Z |
| geogr_code_person |
not assigned |
| openURL |
url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=Phospho%E2%80%90tyrosine+dependent+protein%E2%80%93protein+interaction+network&rft.date=2015-03-01&genre=article&issn=1744-4292&volume=11&issue=3&jtitle=Molecular+Systems+Biology&atitle=Phospho%E2%80%90tyrosine+dependent+protein%E2%80%93protein+interaction+network&aulast=Stelzl&aufirst=Ulrich&rft_id=info%3Adoi%2F10.15252%2Fmsb.20145968&rft.language%5B0%5D=eng |
| SOLR | |
| _version_ | 1792348203222302728 |
| author | Grossmann, Arndt, Benlasfer, Nouhad, Birth, Petra, Hegele, Anna, Wachsmuth, Franziska, Apelt, Luise, Stelzl, Ulrich |
| author_facet | Grossmann, Arndt, Benlasfer, Nouhad, Birth, Petra, Hegele, Anna, Wachsmuth, Franziska, Apelt, Luise, Stelzl, Ulrich, Grossmann, Arndt, Benlasfer, Nouhad, Birth, Petra, Hegele, Anna, Wachsmuth, Franziska, Apelt, Luise, Stelzl, Ulrich |
| author_sort | grossmann, arndt |
| container_issue | 3 |
| container_start_page | 0 |
| container_title | Molecular Systems Biology |
| container_volume | 11 |
| description | <jats:title>Abstract</jats:title><jats:p>Post‐translational protein modifications, such as tyrosine phosphorylation, regulate protein–protein interactions (<jats:styled-content style="fixed-case">PPI</jats:styled-content>s) critical for signal processing and cellular phenotypes. We extended an established yeast two‐hybrid system employing human protein kinases for the analyses of phospho‐tyrosine (<jats:styled-content style="fixed-case">pY</jats:styled-content>)‐dependent <jats:styled-content style="fixed-case">PPI</jats:styled-content>s in a direct experimental, large‐scale approach. We identified 292 mostly novel <jats:styled-content style="fixed-case">pY</jats:styled-content>‐dependent <jats:styled-content style="fixed-case">PPI</jats:styled-content>s which showed high specificity with respect to kinases and interacting proteins and validated a large fraction in co‐immunoprecipitation experiments from mammalian cells. About one‐sixth of the interactions are mediated by known linear sequence binding motifs while the majority of <jats:styled-content style="fixed-case">pY</jats:styled-content>‐<jats:styled-content style="fixed-case">PPI</jats:styled-content>s are mediated by other linear epitopes or governed by alternative recognition modes. Network analysis revealed that <jats:styled-content style="fixed-case">pY</jats:styled-content>‐mediated recognition events are tied to a highly connected protein module dedicated to signaling and cell growth pathways related to cancer. Using binding assays, protein complementation and phenotypic readouts to characterize the <jats:styled-content style="fixed-case">pY</jats:styled-content>‐dependent interactions of <jats:styled-content style="fixed-case">TSPAN</jats:styled-content>2 (tetraspanin 2) and <jats:styled-content style="fixed-case">GRB</jats:styled-content>2 or <jats:styled-content style="fixed-case">PIK</jats:styled-content>3R3 (p55γ), we exemplarily provide evidence that the two <jats:styled-content style="fixed-case">pY</jats:styled-content>‐dependent <jats:styled-content style="fixed-case">PPI</jats:styled-content>s dictate cellular cancer phenotypes.</jats:p> |
| doi_str_mv | 10.15252/msb.20145968 |
| facet_avail | Online, Free |
| finc_class_facet | Mathematik, Informatik |
| format | ElectronicArticle |
| format_de105 | Article, E-Article |
| format_de14 | Article, E-Article |
| format_de15 | Article, E-Article |
| format_de520 | Article, E-Article |
| format_de540 | Article, E-Article |
| format_dech1 | Article, E-Article |
| format_ded117 | Article, E-Article |
| format_degla1 | E-Article |
| format_del152 | Buch |
| format_del189 | Article, E-Article |
| format_dezi4 | Article |
| format_dezwi2 | Article, E-Article |
| format_finc | Article, E-Article |
| format_nrw | Article, E-Article |
| geogr_code | not assigned |
| geogr_code_person | not assigned |
| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTUyNTIvbXNiLjIwMTQ1OTY4 |
| imprint | Springer Science and Business Media LLC, 2015 |
| imprint_str_mv | Springer Science and Business Media LLC, 2015 |
| institution | DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161 |
| issn | 1744-4292 |
| issn_str_mv | 1744-4292 |
| language | English |
| last_indexed | 2024-03-01T18:07:12.01Z |
| match_str | grossmann2015phosphotyrosinedependentproteinproteininteractionnetwork |
| mega_collection | Springer Science and Business Media LLC (CrossRef) |
| physical | |
| publishDate | 2015 |
| publishDateSort | 2015 |
| publisher | Springer Science and Business Media LLC |
| record_format | ai |
| recordtype | ai |
| series | Molecular Systems Biology |
| source_id | 49 |
| spelling | Grossmann, Arndt Benlasfer, Nouhad Birth, Petra Hegele, Anna Wachsmuth, Franziska Apelt, Luise Stelzl, Ulrich 1744-4292 1744-4292 Springer Science and Business Media LLC Applied Mathematics Computational Theory and Mathematics General Agricultural and Biological Sciences General Immunology and Microbiology General Biochemistry, Genetics and Molecular Biology Information Systems http://dx.doi.org/10.15252/msb.20145968 <jats:title>Abstract</jats:title><jats:p>Post‐translational protein modifications, such as tyrosine phosphorylation, regulate protein–protein interactions (<jats:styled-content style="fixed-case">PPI</jats:styled-content>s) critical for signal processing and cellular phenotypes. We extended an established yeast two‐hybrid system employing human protein kinases for the analyses of phospho‐tyrosine (<jats:styled-content style="fixed-case">pY</jats:styled-content>)‐dependent <jats:styled-content style="fixed-case">PPI</jats:styled-content>s in a direct experimental, large‐scale approach. We identified 292 mostly novel <jats:styled-content style="fixed-case">pY</jats:styled-content>‐dependent <jats:styled-content style="fixed-case">PPI</jats:styled-content>s which showed high specificity with respect to kinases and interacting proteins and validated a large fraction in co‐immunoprecipitation experiments from mammalian cells. About one‐sixth of the interactions are mediated by known linear sequence binding motifs while the majority of <jats:styled-content style="fixed-case">pY</jats:styled-content>‐<jats:styled-content style="fixed-case">PPI</jats:styled-content>s are mediated by other linear epitopes or governed by alternative recognition modes. Network analysis revealed that <jats:styled-content style="fixed-case">pY</jats:styled-content>‐mediated recognition events are tied to a highly connected protein module dedicated to signaling and cell growth pathways related to cancer. Using binding assays, protein complementation and phenotypic readouts to characterize the <jats:styled-content style="fixed-case">pY</jats:styled-content>‐dependent interactions of <jats:styled-content style="fixed-case">TSPAN</jats:styled-content>2 (tetraspanin 2) and <jats:styled-content style="fixed-case">GRB</jats:styled-content>2 or <jats:styled-content style="fixed-case">PIK</jats:styled-content>3R3 (p55γ), we exemplarily provide evidence that the two <jats:styled-content style="fixed-case">pY</jats:styled-content>‐dependent <jats:styled-content style="fixed-case">PPI</jats:styled-content>s dictate cellular cancer phenotypes.</jats:p> Phospho‐tyrosine dependent protein–protein interaction network Molecular Systems Biology |
| spellingShingle | Grossmann, Arndt, Benlasfer, Nouhad, Birth, Petra, Hegele, Anna, Wachsmuth, Franziska, Apelt, Luise, Stelzl, Ulrich, Molecular Systems Biology, Phospho‐tyrosine dependent protein–protein interaction network, Applied Mathematics, Computational Theory and Mathematics, General Agricultural and Biological Sciences, General Immunology and Microbiology, General Biochemistry, Genetics and Molecular Biology, Information Systems |
| title | Phospho‐tyrosine dependent protein–protein interaction network |
| title_full | Phospho‐tyrosine dependent protein–protein interaction network |
| title_fullStr | Phospho‐tyrosine dependent protein–protein interaction network |
| title_full_unstemmed | Phospho‐tyrosine dependent protein–protein interaction network |
| title_short | Phospho‐tyrosine dependent protein–protein interaction network |
| title_sort | phospho‐tyrosine dependent protein–protein interaction network |
| title_unstemmed | Phospho‐tyrosine dependent protein–protein interaction network |
| topic | Applied Mathematics, Computational Theory and Mathematics, General Agricultural and Biological Sciences, General Immunology and Microbiology, General Biochemistry, Genetics and Molecular Biology, Information Systems |
| url | http://dx.doi.org/10.15252/msb.20145968 |