Tyrosine phosphorylation of the orphan receptor ESDN/DCBLD2 serves as a scaffold for the signaling adaptor CrkL
•Functional proteomics identifies ESDN as a novel CrkL-SH2 binding protein.•Fyn and other tyrosine kinases induce the binding of ESDN to both the CrkL and Fyn SH2 domains.•Mass spectrometry-based identification of regulated tyrosine phosphorylation sites on ESDN. A quantitative proteomics screen to...
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| Veröffentlicht in: | FEBS letters 2013-08, Vol.587 (15), p.2313-2318 |
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| creator | Aten, Tyler M. Redmond, Miranda M. Weaver, Sheila O. Love, Collin C. Joy, Ryan M. Lapp, Aliya S. Rivera, Osvaldo D. Hinkle, Karen L. Ballif, Bryan A. |
| description | •Functional proteomics identifies ESDN as a novel CrkL-SH2 binding protein.•Fyn and other tyrosine kinases induce the binding of ESDN to both the CrkL and Fyn SH2 domains.•Mass spectrometry-based identification of regulated tyrosine phosphorylation sites on ESDN.
A quantitative proteomics screen to identify substrates of the Src family of tyrosine kinases (SFKs) whose phosphorylation promotes CrkL-SH2 binding identified the known Crk-associated substrate (Cas) of Src as well as the orphan receptor endothelial and smooth muscle cell-derived neuropilin-like protein (ESDN). Mutagenesis analysis of ESDN’s seven intracellular tyrosines in YxxP motifs found several contribute to the binding of ESDN to the SH2 domains of both CrkCT10 regulator of kinase Crk-Like (CrkL) and a representative SFK Fyn. Quantitative mass spectrometry showed that at least three of these (Y565, Y621 and Y750), as well as non-YxxP Y715, are reversibly phosphorylated. SFK activity was shown to be sufficient, but not required for the interaction between ESDN and the CrkL-SH2 domain. Finally, antibody-mediated ESDN clustering induces ESDN tyrosine phosphorylation and CrkL-SH2 binding.
CrkL-SH2physically interacts with ESDN and CAS by pull down (View interaction)
CrkL-SH2physically interacts with ESDN by pull down (View Interaction: 1, 2)
Fyn-SH2physically interacts with ESDN by pull down (View interaction) |
| doi_str_mv | 10.1016/j.febslet.2013.05.064 |
| format | Article |
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A quantitative proteomics screen to identify substrates of the Src family of tyrosine kinases (SFKs) whose phosphorylation promotes CrkL-SH2 binding identified the known Crk-associated substrate (Cas) of Src as well as the orphan receptor endothelial and smooth muscle cell-derived neuropilin-like protein (ESDN). Mutagenesis analysis of ESDN’s seven intracellular tyrosines in YxxP motifs found several contribute to the binding of ESDN to the SH2 domains of both CrkCT10 regulator of kinase Crk-Like (CrkL) and a representative SFK Fyn. Quantitative mass spectrometry showed that at least three of these (Y565, Y621 and Y750), as well as non-YxxP Y715, are reversibly phosphorylated. SFK activity was shown to be sufficient, but not required for the interaction between ESDN and the CrkL-SH2 domain. Finally, antibody-mediated ESDN clustering induces ESDN tyrosine phosphorylation and CrkL-SH2 binding.
CrkL-SH2physically interacts with ESDN and CAS by pull down (View interaction)
CrkL-SH2physically interacts with ESDN by pull down (View Interaction: 1, 2)
Fyn-SH2physically interacts with ESDN by pull down (View interaction)</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2013.05.064</identifier><identifier>PMID: 23770091</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Adaptor Proteins, Signal Transducing - metabolism ; Amino Acid Sequence ; C-terminal Src kinase ; Cas ; complement C1r/C1s Uegf Bmp1 ; Crk-associated substrate ; CrkCT10 regulator of kinase Crk-Like ; CrkL ; CSK ; CUB ; DCBLD2 ; discoidin CUB and LCCL domain containing 2 ; endothelial and smooth muscle cell-derived neuropilin-like protein ; ESDN ; Functional phosphoproteomics ; Gab1 ; glutathione stransferase ; GRB2-associated-binding protein 1 ; GST ; HEK293 Cells ; Humans ; insulin receptor substrate-1 ; IRS-1 ; liquid chromatography ; Mass spectrometry ; Membrane Proteins - chemistry ; Membrane Proteins - metabolism ; Molecular Sequence Data ; mutagenesis ; Nuclear Proteins - metabolism ; PCR ; Phosphorylation ; phosphotransferases (kinases) ; polymerase chain reaction ; proteomics ; Sequence Homology, Amino Acid ; SFK ; SH2 ; Signal transduction ; SILAC ; smooth muscle ; Src family kinase ; Src family tyrosine kinase ; stable-isotope labeling by amino acids in cell culture ; tyrosine ; Tyrosine - metabolism ; WCE ; whole cell extract</subject><ispartof>FEBS letters, 2013-08, Vol.587 (15), p.2313-2318</ispartof><rights>2013 Federation of European Biochemical Societies</rights><rights>FEBS Letters 587 (2013) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>Copyright © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.</rights><rights>2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. 2013</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5652-825dc634ac975b62c1a4eb5eb45ac0d1e34a9b60cf28418e889d784654299bf53</citedby><cites>FETCH-LOGICAL-c5652-825dc634ac975b62c1a4eb5eb45ac0d1e34a9b60cf28418e889d784654299bf53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2013.05.064$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579313004432$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,776,780,881,1411,1427,3537,27901,27902,45550,45551,46384,46808,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23770091$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Aten, Tyler M.</creatorcontrib><creatorcontrib>Redmond, Miranda M.</creatorcontrib><creatorcontrib>Weaver, Sheila O.</creatorcontrib><creatorcontrib>Love, Collin C.</creatorcontrib><creatorcontrib>Joy, Ryan M.</creatorcontrib><creatorcontrib>Lapp, Aliya S.</creatorcontrib><creatorcontrib>Rivera, Osvaldo D.</creatorcontrib><creatorcontrib>Hinkle, Karen L.</creatorcontrib><creatorcontrib>Ballif, Bryan A.</creatorcontrib><title>Tyrosine phosphorylation of the orphan receptor ESDN/DCBLD2 serves as a scaffold for the signaling adaptor CrkL</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>•Functional proteomics identifies ESDN as a novel CrkL-SH2 binding protein.•Fyn and other tyrosine kinases induce the binding of ESDN to both the CrkL and Fyn SH2 domains.•Mass spectrometry-based identification of regulated tyrosine phosphorylation sites on ESDN.
A quantitative proteomics screen to identify substrates of the Src family of tyrosine kinases (SFKs) whose phosphorylation promotes CrkL-SH2 binding identified the known Crk-associated substrate (Cas) of Src as well as the orphan receptor endothelial and smooth muscle cell-derived neuropilin-like protein (ESDN). Mutagenesis analysis of ESDN’s seven intracellular tyrosines in YxxP motifs found several contribute to the binding of ESDN to the SH2 domains of both CrkCT10 regulator of kinase Crk-Like (CrkL) and a representative SFK Fyn. Quantitative mass spectrometry showed that at least three of these (Y565, Y621 and Y750), as well as non-YxxP Y715, are reversibly phosphorylated. SFK activity was shown to be sufficient, but not required for the interaction between ESDN and the CrkL-SH2 domain. Finally, antibody-mediated ESDN clustering induces ESDN tyrosine phosphorylation and CrkL-SH2 binding.
CrkL-SH2physically interacts with ESDN and CAS by pull down (View interaction)
CrkL-SH2physically interacts with ESDN by pull down (View Interaction: 1, 2)
Fyn-SH2physically interacts with ESDN by pull down (View interaction)</description><subject>Adaptor Proteins, Signal Transducing - metabolism</subject><subject>Amino Acid Sequence</subject><subject>C-terminal Src kinase</subject><subject>Cas</subject><subject>complement C1r/C1s Uegf Bmp1</subject><subject>Crk-associated substrate</subject><subject>CrkCT10 regulator of kinase Crk-Like</subject><subject>CrkL</subject><subject>CSK</subject><subject>CUB</subject><subject>DCBLD2</subject><subject>discoidin CUB and LCCL domain containing 2</subject><subject>endothelial and smooth muscle cell-derived neuropilin-like protein</subject><subject>ESDN</subject><subject>Functional phosphoproteomics</subject><subject>Gab1</subject><subject>glutathione stransferase</subject><subject>GRB2-associated-binding protein 1</subject><subject>GST</subject><subject>HEK293 Cells</subject><subject>Humans</subject><subject>insulin receptor substrate-1</subject><subject>IRS-1</subject><subject>liquid chromatography</subject><subject>Mass spectrometry</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - metabolism</subject><subject>Molecular Sequence Data</subject><subject>mutagenesis</subject><subject>Nuclear Proteins - metabolism</subject><subject>PCR</subject><subject>Phosphorylation</subject><subject>phosphotransferases (kinases)</subject><subject>polymerase chain reaction</subject><subject>proteomics</subject><subject>Sequence Homology, Amino Acid</subject><subject>SFK</subject><subject>SH2</subject><subject>Signal transduction</subject><subject>SILAC</subject><subject>smooth muscle</subject><subject>Src family kinase</subject><subject>Src family tyrosine kinase</subject><subject>stable-isotope labeling by amino acids in cell culture</subject><subject>tyrosine</subject><subject>Tyrosine - metabolism</subject><subject>WCE</subject><subject>whole cell extract</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkV9v0zAUxS0EYmXwEUB-5CWZ_ybOC4i13YZUwcPGs-U4N61LGgc7Leq3x6HdBE8g2bKse87x9f0h9JaSnBJaXG3zFurYwZgzQnlOZE4K8QzNqCp5xkWhnqMZIVRksqz4BXoV45aku6LVS3TBeFkSUtEZ8g_H4KPrAQ8bH9MOx86MzvfYt3jcAPZh2JgeB7AwjD7g5f3iy9Vifr1aMBwhHCBikxaO1rSt7xrcJtFkjG7dm871a2wa89s6D99Xr9GL1nQR3pzPS_TtZvkwv8tWX28_zz-tMisLyTLFZGMLLoytSlkXzFIjoJZQC2ksaSikUlUXxLZMCapAqaoplSikYFVVt5Jfog-n3GFf76Cx0I_BdHoIbmfCUXvj9N-V3m302h80L2UlKUsB788Bwf_YQxz1zkULXWd68Puoacm5pFwKkqTyJLVplDFA-_QMJXqCpbf6DEtPsDSROsFKvnd_9vjkeqSTBHcnwU_XwfH_UvXN8prdT-Qn8JQTIgSfvvPxFAVp6AcHQUfroLfQuIR21I13_-j2F9SBvxc</recordid><startdate>20130802</startdate><enddate>20130802</enddate><creator>Aten, Tyler M.</creator><creator>Redmond, Miranda M.</creator><creator>Weaver, Sheila O.</creator><creator>Love, Collin C.</creator><creator>Joy, Ryan M.</creator><creator>Lapp, Aliya S.</creator><creator>Rivera, Osvaldo D.</creator><creator>Hinkle, Karen L.</creator><creator>Ballif, Bryan A.</creator><general>Elsevier B.V</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>7S9</scope><scope>L.6</scope><scope>5PM</scope></search><sort><creationdate>20130802</creationdate><title>Tyrosine phosphorylation of the orphan receptor ESDN/DCBLD2 serves as a scaffold for the signaling adaptor CrkL</title><author>Aten, Tyler M. ; Redmond, Miranda M. ; Weaver, Sheila O. ; Love, Collin C. ; Joy, Ryan M. ; Lapp, Aliya S. ; Rivera, Osvaldo D. ; Hinkle, Karen L. ; Ballif, Bryan A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5652-825dc634ac975b62c1a4eb5eb45ac0d1e34a9b60cf28418e889d784654299bf53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Adaptor Proteins, Signal Transducing - metabolism</topic><topic>Amino Acid Sequence</topic><topic>C-terminal Src kinase</topic><topic>Cas</topic><topic>complement C1r/C1s Uegf Bmp1</topic><topic>Crk-associated substrate</topic><topic>CrkCT10 regulator of kinase Crk-Like</topic><topic>CrkL</topic><topic>CSK</topic><topic>CUB</topic><topic>DCBLD2</topic><topic>discoidin CUB and LCCL domain containing 2</topic><topic>endothelial and smooth muscle cell-derived neuropilin-like protein</topic><topic>ESDN</topic><topic>Functional phosphoproteomics</topic><topic>Gab1</topic><topic>glutathione stransferase</topic><topic>GRB2-associated-binding protein 1</topic><topic>GST</topic><topic>HEK293 Cells</topic><topic>Humans</topic><topic>insulin receptor substrate-1</topic><topic>IRS-1</topic><topic>liquid chromatography</topic><topic>Mass spectrometry</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - metabolism</topic><topic>Molecular Sequence Data</topic><topic>mutagenesis</topic><topic>Nuclear Proteins - metabolism</topic><topic>PCR</topic><topic>Phosphorylation</topic><topic>phosphotransferases (kinases)</topic><topic>polymerase chain reaction</topic><topic>proteomics</topic><topic>Sequence Homology, Amino Acid</topic><topic>SFK</topic><topic>SH2</topic><topic>Signal transduction</topic><topic>SILAC</topic><topic>smooth muscle</topic><topic>Src family kinase</topic><topic>Src family tyrosine kinase</topic><topic>stable-isotope labeling by amino acids in cell culture</topic><topic>tyrosine</topic><topic>Tyrosine - metabolism</topic><topic>WCE</topic><topic>whole cell extract</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Aten, Tyler M.</creatorcontrib><creatorcontrib>Redmond, Miranda M.</creatorcontrib><creatorcontrib>Weaver, Sheila O.</creatorcontrib><creatorcontrib>Love, Collin C.</creatorcontrib><creatorcontrib>Joy, Ryan M.</creatorcontrib><creatorcontrib>Lapp, Aliya S.</creatorcontrib><creatorcontrib>Rivera, Osvaldo D.</creatorcontrib><creatorcontrib>Hinkle, Karen L.</creatorcontrib><creatorcontrib>Ballif, Bryan 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>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Aten, Tyler M.</au><au>Redmond, Miranda M.</au><au>Weaver, Sheila O.</au><au>Love, Collin C.</au><au>Joy, Ryan M.</au><au>Lapp, Aliya S.</au><au>Rivera, Osvaldo D.</au><au>Hinkle, Karen L.</au><au>Ballif, Bryan A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Tyrosine phosphorylation of the orphan receptor ESDN/DCBLD2 serves as a scaffold for the signaling adaptor CrkL</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2013-08-02</date><risdate>2013</risdate><volume>587</volume><issue>15</issue><spage>2313</spage><epage>2318</epage><pages>2313-2318</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>•Functional proteomics identifies ESDN as a novel CrkL-SH2 binding protein.•Fyn and other tyrosine kinases induce the binding of ESDN to both the CrkL and Fyn SH2 domains.•Mass spectrometry-based identification of regulated tyrosine phosphorylation sites on ESDN.
A quantitative proteomics screen to identify substrates of the Src family of tyrosine kinases (SFKs) whose phosphorylation promotes CrkL-SH2 binding identified the known Crk-associated substrate (Cas) of Src as well as the orphan receptor endothelial and smooth muscle cell-derived neuropilin-like protein (ESDN). Mutagenesis analysis of ESDN’s seven intracellular tyrosines in YxxP motifs found several contribute to the binding of ESDN to the SH2 domains of both CrkCT10 regulator of kinase Crk-Like (CrkL) and a representative SFK Fyn. Quantitative mass spectrometry showed that at least three of these (Y565, Y621 and Y750), as well as non-YxxP Y715, are reversibly phosphorylated. SFK activity was shown to be sufficient, but not required for the interaction between ESDN and the CrkL-SH2 domain. Finally, antibody-mediated ESDN clustering induces ESDN tyrosine phosphorylation and CrkL-SH2 binding.
CrkL-SH2physically interacts with ESDN and CAS by pull down (View interaction)
CrkL-SH2physically interacts with ESDN by pull down (View Interaction: 1, 2)
Fyn-SH2physically interacts with ESDN by pull down (View interaction)</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>23770091</pmid><doi>10.1016/j.febslet.2013.05.064</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| source | Wiley Free Content; MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Adaptor Proteins, Signal Transducing - metabolism Amino Acid Sequence C-terminal Src kinase Cas complement C1r/C1s Uegf Bmp1 Crk-associated substrate CrkCT10 regulator of kinase Crk-Like CrkL CSK CUB DCBLD2 discoidin CUB and LCCL domain containing 2 endothelial and smooth muscle cell-derived neuropilin-like protein ESDN Functional phosphoproteomics Gab1 glutathione stransferase GRB2-associated-binding protein 1 GST HEK293 Cells Humans insulin receptor substrate-1 IRS-1 liquid chromatography Mass spectrometry Membrane Proteins - chemistry Membrane Proteins - metabolism Molecular Sequence Data mutagenesis Nuclear Proteins - metabolism PCR Phosphorylation phosphotransferases (kinases) polymerase chain reaction proteomics Sequence Homology, Amino Acid SFK SH2 Signal transduction SILAC smooth muscle Src family kinase Src family tyrosine kinase stable-isotope labeling by amino acids in cell culture tyrosine Tyrosine - metabolism WCE whole cell extract |
| title | Tyrosine phosphorylation of the orphan receptor ESDN/DCBLD2 serves as a scaffold for the signaling adaptor CrkL |
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