Tyrosine phosphorylation of Grb14 by Tie2
<p>Abstract</p> <p>Background</p> <p>Growth factor receptor bound (Grb) proteins 7, 10 and 14 are a family of structurally related multi-domain adaptor proteins involved in a variety of biological processes. Grb7, 10 and 14 are known to become serine and/or threonine ph...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
| Published: |
BMC
2010-10-01
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| Series: | Cell Communication and Signaling |
| Online Access: | http://www.biosignaling.com/content/8/1/30 |
| _version_ | 1811252602450477056 |
|---|---|
| author | Dumont Daniel J Sturk Celina |
| author_facet | Dumont Daniel J Sturk Celina |
| author_sort | Dumont Daniel J |
| collection | DOAJ |
| description | <p>Abstract</p> <p>Background</p> <p>Growth factor receptor bound (Grb) proteins 7, 10 and 14 are a family of structurally related multi-domain adaptor proteins involved in a variety of biological processes. Grb7, 10 and 14 are known to become serine and/or threonine phosphorylated in response to growth factor (GF) stimulation. Grb7 and 10 have also been shown to become tyrosine phosphorylated under certain conditions. Under experimental conditions Grb7 is tyrosine phosphorylated by the Tie2/Tie-2/Tek angiogenic receptor tyrosine kinase (RTK). Furthermore, Grb14 has also been shown to interact with Tie2, however tyrosine phosphorylation of this Grb family member has yet to be reported.</p> <p>Results</p> <p>Here we report for the first time tyrosine phosphorylation of Grb14. This phosphorylation requires a kinase competent Tie2 as well as intact tyrosines 1100 and 1106 (Y1100 and Y1106) on the receptor. Furthermore, a complete SH2 domain on Grb14 is required for Grb14 tyrosine phosphorylation by Tie2. Grb14 was also able to become tyrosine phosphorylated in primary endothelial cells when treated with a soluble and potent variant of the Tie2 ligand, cartilage oligomeric matrix protein (COMP) Ang1.</p> <p>Conclusion</p> <p>Our results show that Grb14, like its family members Grb7 and Grb10, is able to be tyrosine phosphorylated. Furthermore, our data indicate a role for Grb14 in endothelial signaling downstream of the Tie2 receptor.</p> |
| first_indexed | 2024-04-12T16:38:05Z |
| format | Article |
| id | doaj.art-fb61b4293a80473d84a2f1523601a981 |
| institution | Directory Open Access Journal |
| issn | 1478-811X |
| language | English |
| last_indexed | 2024-04-12T16:38:05Z |
| publishDate | 2010-10-01 |
| publisher | BMC |
| record_format | Article |
| series | Cell Communication and Signaling |
| spelling | doaj.art-fb61b4293a80473d84a2f1523601a9812022-12-22T03:24:56ZengBMCCell Communication and Signaling1478-811X2010-10-01813010.1186/1478-811X-8-30Tyrosine phosphorylation of Grb14 by Tie2Dumont Daniel JSturk Celina<p>Abstract</p> <p>Background</p> <p>Growth factor receptor bound (Grb) proteins 7, 10 and 14 are a family of structurally related multi-domain adaptor proteins involved in a variety of biological processes. Grb7, 10 and 14 are known to become serine and/or threonine phosphorylated in response to growth factor (GF) stimulation. Grb7 and 10 have also been shown to become tyrosine phosphorylated under certain conditions. Under experimental conditions Grb7 is tyrosine phosphorylated by the Tie2/Tie-2/Tek angiogenic receptor tyrosine kinase (RTK). Furthermore, Grb14 has also been shown to interact with Tie2, however tyrosine phosphorylation of this Grb family member has yet to be reported.</p> <p>Results</p> <p>Here we report for the first time tyrosine phosphorylation of Grb14. This phosphorylation requires a kinase competent Tie2 as well as intact tyrosines 1100 and 1106 (Y1100 and Y1106) on the receptor. Furthermore, a complete SH2 domain on Grb14 is required for Grb14 tyrosine phosphorylation by Tie2. Grb14 was also able to become tyrosine phosphorylated in primary endothelial cells when treated with a soluble and potent variant of the Tie2 ligand, cartilage oligomeric matrix protein (COMP) Ang1.</p> <p>Conclusion</p> <p>Our results show that Grb14, like its family members Grb7 and Grb10, is able to be tyrosine phosphorylated. Furthermore, our data indicate a role for Grb14 in endothelial signaling downstream of the Tie2 receptor.</p>http://www.biosignaling.com/content/8/1/30 |
| spellingShingle | Dumont Daniel J Sturk Celina Tyrosine phosphorylation of Grb14 by Tie2 Cell Communication and Signaling |
| title | Tyrosine phosphorylation of Grb14 by Tie2 |
| title_full | Tyrosine phosphorylation of Grb14 by Tie2 |
| title_fullStr | Tyrosine phosphorylation of Grb14 by Tie2 |
| title_full_unstemmed | Tyrosine phosphorylation of Grb14 by Tie2 |
| title_short | Tyrosine phosphorylation of Grb14 by Tie2 |
| title_sort | tyrosine phosphorylation of grb14 by tie2 |
| url | http://www.biosignaling.com/content/8/1/30 |
| work_keys_str_mv | AT dumontdanielj tyrosinephosphorylationofgrb14bytie2 AT sturkcelina tyrosinephosphorylationofgrb14bytie2 |