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Autophosphorylation of the two C‐terminal tyrosine residues Tyr1316 and Tyr1322 modulates the activity of the insulin receptor kinase in vitro
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| Zeitschriftentitel: | FEBS Letters |
|---|---|
| Personen und Körperschaften: | , , , |
| In: | FEBS Letters, 479, 2000, 1-2, S. 67-71 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
|
| Schlagwörter: |
| author_facet |
Tennagels, Norbert Bergschneider, Eva Al-Hasani, Hadi Klein, Helmut W Tennagels, Norbert Bergschneider, Eva Al-Hasani, Hadi Klein, Helmut W |
|---|---|
| author |
Tennagels, Norbert Bergschneider, Eva Al-Hasani, Hadi Klein, Helmut W |
| spellingShingle |
Tennagels, Norbert Bergschneider, Eva Al-Hasani, Hadi Klein, Helmut W FEBS Letters Autophosphorylation of the two C‐terminal tyrosine residues Tyr1316 and Tyr1322 modulates the activity of the insulin receptor kinase in vitro Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics |
| author_sort |
tennagels, norbert |
| spelling |
Tennagels, Norbert Bergschneider, Eva Al-Hasani, Hadi Klein, Helmut W 0014-5793 1873-3468 Wiley Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1016/s0014-5793(00)01879-2 <jats:p>Previously, several studies have demonstrated that autophosphorylation of the C‐terminal tyrosine residues (Tyr<jats:sup>1316</jats:sup> and Tyr<jats:sup>1322</jats:sup>) affects the signaling properties of the insulin receptor in vivo. To assess the biochemical consequences of the C‐terminal phosphorylation in vitro, we have constructed, purified and characterized 45 kDa soluble insulin receptor kinase domains (IRKD), either with (IRKD) or without (IRKD‐Y2F) the two C‐terminal tyrosine phosphorylation sites, respectively. According to HPLC phosphopeptide mapping, autophosphorylation of the three tyrosines in the activation loop of the IRKD‐Y2F kinase (Tyr<jats:sup>1146</jats:sup>, Tyr<jats:sup>1150</jats:sup>, and Tyr<jats:sup>1151</jats:sup>) was not affected by the mutation. In addition, the Y2F mutation did not significantly change the <jats:italic>K</jats:italic> <jats:sub>m</jats:sub> values for exogenous substrates. However, the mutation in IRKD‐Y2F resulted in a decrease in the maximum velocities of the phosphotransferase reaction in substrate phosphorylation reactions. Moreover, the exchange of the tyrosines in IRKD‐Y2F led to an increase in the apparent <jats:italic>K</jats:italic> <jats:sub>m</jats:sub> values for ATP, suggesting a cross‐talk of the C‐terminus and the catalytic domain of the enzyme. In addition, as judged by size exclusion chromatography, conformational changes of the enzyme following autophosphorylation were abolished by the removal of the two C‐terminal tyrosines. These data suggest a regulatory role of the two C‐terminal phosphorylation sites in the phosphotransferase activity of the insulin receptor.</jats:p> Autophosphorylation of the two C‐terminal tyrosine residues Tyr<sup>1316</sup> and Tyr<sup>1322</sup> modulates the activity of the insulin receptor kinase in vitro FEBS Letters |
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10.1016/s0014-5793(00)01879-2 |
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Biologie Chemie und Pharmazie Physik |
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FEBS Letters |
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| title |
Autophosphorylation of the two C‐terminal tyrosine residues Tyr1316 and Tyr1322 modulates the activity of the insulin receptor kinase in vitro |
| title_unstemmed |
Autophosphorylation of the two C‐terminal tyrosine residues Tyr1316 and Tyr1322 modulates the activity of the insulin receptor kinase in vitro |
| title_full |
Autophosphorylation of the two C‐terminal tyrosine residues Tyr1316 and Tyr1322 modulates the activity of the insulin receptor kinase in vitro |
| title_fullStr |
Autophosphorylation of the two C‐terminal tyrosine residues Tyr1316 and Tyr1322 modulates the activity of the insulin receptor kinase in vitro |
| title_full_unstemmed |
Autophosphorylation of the two C‐terminal tyrosine residues Tyr1316 and Tyr1322 modulates the activity of the insulin receptor kinase in vitro |
| title_short |
Autophosphorylation of the two C‐terminal tyrosine residues Tyr1316 and Tyr1322 modulates the activity of the insulin receptor kinase in vitro |
| title_sort |
autophosphorylation of the two c‐terminal tyrosine residues tyr<sup>1316</sup> and tyr<sup>1322</sup> modulates the activity of the insulin receptor kinase in vitro |
| topic |
Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics |
| url |
http://dx.doi.org/10.1016/s0014-5793(00)01879-2 |
| publishDate |
2000 |
| physical |
67-71 |
| description |
<jats:p>Previously, several studies have demonstrated that autophosphorylation of the C‐terminal tyrosine residues (Tyr<jats:sup>1316</jats:sup> and Tyr<jats:sup>1322</jats:sup>) affects the signaling properties of the insulin receptor in vivo. To assess the biochemical consequences of the C‐terminal phosphorylation in vitro, we have constructed, purified and characterized 45 kDa soluble insulin receptor kinase domains (IRKD), either with (IRKD) or without (IRKD‐Y2F) the two C‐terminal tyrosine phosphorylation sites, respectively. According to HPLC phosphopeptide mapping, autophosphorylation of the three tyrosines in the activation loop of the IRKD‐Y2F kinase (Tyr<jats:sup>1146</jats:sup>, Tyr<jats:sup>1150</jats:sup>, and Tyr<jats:sup>1151</jats:sup>) was not affected by the mutation. In addition, the Y2F mutation did not significantly change the <jats:italic>K</jats:italic>
<jats:sub>m</jats:sub> values for exogenous substrates. However, the mutation in IRKD‐Y2F resulted in a decrease in the maximum velocities of the phosphotransferase reaction in substrate phosphorylation reactions. Moreover, the exchange of the tyrosines in IRKD‐Y2F led to an increase in the apparent <jats:italic>K</jats:italic>
<jats:sub>m</jats:sub> values for ATP, suggesting a cross‐talk of the C‐terminus and the catalytic domain of the enzyme. In addition, as judged by size exclusion chromatography, conformational changes of the enzyme following autophosphorylation were abolished by the removal of the two C‐terminal tyrosines. These data suggest a regulatory role of the two C‐terminal phosphorylation sites in the phosphotransferase activity of the insulin receptor.</jats:p> |
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| author | Tennagels, Norbert, Bergschneider, Eva, Al-Hasani, Hadi, Klein, Helmut W |
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| description | <jats:p>Previously, several studies have demonstrated that autophosphorylation of the C‐terminal tyrosine residues (Tyr<jats:sup>1316</jats:sup> and Tyr<jats:sup>1322</jats:sup>) affects the signaling properties of the insulin receptor in vivo. To assess the biochemical consequences of the C‐terminal phosphorylation in vitro, we have constructed, purified and characterized 45 kDa soluble insulin receptor kinase domains (IRKD), either with (IRKD) or without (IRKD‐Y2F) the two C‐terminal tyrosine phosphorylation sites, respectively. According to HPLC phosphopeptide mapping, autophosphorylation of the three tyrosines in the activation loop of the IRKD‐Y2F kinase (Tyr<jats:sup>1146</jats:sup>, Tyr<jats:sup>1150</jats:sup>, and Tyr<jats:sup>1151</jats:sup>) was not affected by the mutation. In addition, the Y2F mutation did not significantly change the <jats:italic>K</jats:italic> <jats:sub>m</jats:sub> values for exogenous substrates. However, the mutation in IRKD‐Y2F resulted in a decrease in the maximum velocities of the phosphotransferase reaction in substrate phosphorylation reactions. Moreover, the exchange of the tyrosines in IRKD‐Y2F led to an increase in the apparent <jats:italic>K</jats:italic> <jats:sub>m</jats:sub> values for ATP, suggesting a cross‐talk of the C‐terminus and the catalytic domain of the enzyme. In addition, as judged by size exclusion chromatography, conformational changes of the enzyme following autophosphorylation were abolished by the removal of the two C‐terminal tyrosines. These data suggest a regulatory role of the two C‐terminal phosphorylation sites in the phosphotransferase activity of the insulin receptor.</jats:p> |
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| institution | DE-D275, DE-Bn3, DE-Brt1, DE-D161, DE-Zwi2, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229 |
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| spelling | Tennagels, Norbert Bergschneider, Eva Al-Hasani, Hadi Klein, Helmut W 0014-5793 1873-3468 Wiley Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1016/s0014-5793(00)01879-2 <jats:p>Previously, several studies have demonstrated that autophosphorylation of the C‐terminal tyrosine residues (Tyr<jats:sup>1316</jats:sup> and Tyr<jats:sup>1322</jats:sup>) affects the signaling properties of the insulin receptor in vivo. To assess the biochemical consequences of the C‐terminal phosphorylation in vitro, we have constructed, purified and characterized 45 kDa soluble insulin receptor kinase domains (IRKD), either with (IRKD) or without (IRKD‐Y2F) the two C‐terminal tyrosine phosphorylation sites, respectively. According to HPLC phosphopeptide mapping, autophosphorylation of the three tyrosines in the activation loop of the IRKD‐Y2F kinase (Tyr<jats:sup>1146</jats:sup>, Tyr<jats:sup>1150</jats:sup>, and Tyr<jats:sup>1151</jats:sup>) was not affected by the mutation. In addition, the Y2F mutation did not significantly change the <jats:italic>K</jats:italic> <jats:sub>m</jats:sub> values for exogenous substrates. However, the mutation in IRKD‐Y2F resulted in a decrease in the maximum velocities of the phosphotransferase reaction in substrate phosphorylation reactions. Moreover, the exchange of the tyrosines in IRKD‐Y2F led to an increase in the apparent <jats:italic>K</jats:italic> <jats:sub>m</jats:sub> values for ATP, suggesting a cross‐talk of the C‐terminus and the catalytic domain of the enzyme. In addition, as judged by size exclusion chromatography, conformational changes of the enzyme following autophosphorylation were abolished by the removal of the two C‐terminal tyrosines. These data suggest a regulatory role of the two C‐terminal phosphorylation sites in the phosphotransferase activity of the insulin receptor.</jats:p> Autophosphorylation of the two C‐terminal tyrosine residues Tyr<sup>1316</sup> and Tyr<sup>1322</sup> modulates the activity of the insulin receptor kinase in vitro FEBS Letters |
| spellingShingle | Tennagels, Norbert, Bergschneider, Eva, Al-Hasani, Hadi, Klein, Helmut W, FEBS Letters, Autophosphorylation of the two C‐terminal tyrosine residues Tyr1316 and Tyr1322 modulates the activity of the insulin receptor kinase in vitro, Cell Biology, Genetics, Molecular Biology, Biochemistry, Structural Biology, Biophysics |
| title | Autophosphorylation of the two C‐terminal tyrosine residues Tyr1316 and Tyr1322 modulates the activity of the insulin receptor kinase in vitro |
| title_full | Autophosphorylation of the two C‐terminal tyrosine residues Tyr1316 and Tyr1322 modulates the activity of the insulin receptor kinase in vitro |
| title_fullStr | Autophosphorylation of the two C‐terminal tyrosine residues Tyr1316 and Tyr1322 modulates the activity of the insulin receptor kinase in vitro |
| title_full_unstemmed | Autophosphorylation of the two C‐terminal tyrosine residues Tyr1316 and Tyr1322 modulates the activity of the insulin receptor kinase in vitro |
| title_short | Autophosphorylation of the two C‐terminal tyrosine residues Tyr1316 and Tyr1322 modulates the activity of the insulin receptor kinase in vitro |
| title_sort | autophosphorylation of the two c‐terminal tyrosine residues tyr<sup>1316</sup> and tyr<sup>1322</sup> modulates the activity of the insulin receptor kinase in vitro |
| title_unstemmed | Autophosphorylation of the two C‐terminal tyrosine residues Tyr1316 and Tyr1322 modulates the activity of the insulin receptor kinase in vitro |
| topic | Cell Biology, Genetics, Molecular Biology, Biochemistry, Structural Biology, Biophysics |
| url | http://dx.doi.org/10.1016/s0014-5793(00)01879-2 |