GTP binding to the ROC domain of DAP-kinase regulates its function through intramolecular signalling
Death-associated protein kinase (DAPk) was recently suggested by sequence homology to be a member of the ROCO family of proteins. Here, we show that DAPk has a functional ROC (Ras of complex proteins) domain that mediates homo-oligomerization and GTP binding through a defined P-loop motif. Upon bind...
| Main Authors: | , , , , , , , |
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| Format: | Journal Article |
| Published: |
2011
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| Online Access: | http://hdl.handle.net/20.500.11937/47501 |
| _version_ | 1848757849871613952 |
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| author | Carlessi, Rodrigo Levin-Salomon, V. Ciprut, S. Bialik, S. Berissi, H. Albeck, S. Peleg, Y. Kimchi, A. |
| author_facet | Carlessi, Rodrigo Levin-Salomon, V. Ciprut, S. Bialik, S. Berissi, H. Albeck, S. Peleg, Y. Kimchi, A. |
| author_sort | Carlessi, Rodrigo |
| building | Curtin Institutional Repository |
| collection | Online Access |
| description | Death-associated protein kinase (DAPk) was recently suggested by sequence homology to be a member of the ROCO family of proteins. Here, we show that DAPk has a functional ROC (Ras of complex proteins) domain that mediates homo-oligomerization and GTP binding through a defined P-loop motif. Upon binding to GTP, the ROC domain negatively regulates the catalytic activity of DAPk and its cellular effects. Mechanistically, GTP binding enhances an inhibitory autophosphorylation at a distal site that suppresses kinase activity. This study presents a new mechanism of intramolecular signal transduction, by which GTP binding operates in cis to affect the catalytic activity of a distal domain in the protein. © 2011 European Molecular Biology Organization. |
| first_indexed | 2025-11-14T09:34:38Z |
| format | Journal Article |
| id | curtin-20.500.11937-47501 |
| institution | Curtin University Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-14T09:34:38Z |
| publishDate | 2011 |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | curtin-20.500.11937-475012023-02-22T06:24:18Z GTP binding to the ROC domain of DAP-kinase regulates its function through intramolecular signalling Carlessi, Rodrigo Levin-Salomon, V. Ciprut, S. Bialik, S. Berissi, H. Albeck, S. Peleg, Y. Kimchi, A. Death-associated protein kinase (DAPk) was recently suggested by sequence homology to be a member of the ROCO family of proteins. Here, we show that DAPk has a functional ROC (Ras of complex proteins) domain that mediates homo-oligomerization and GTP binding through a defined P-loop motif. Upon binding to GTP, the ROC domain negatively regulates the catalytic activity of DAPk and its cellular effects. Mechanistically, GTP binding enhances an inhibitory autophosphorylation at a distal site that suppresses kinase activity. This study presents a new mechanism of intramolecular signal transduction, by which GTP binding operates in cis to affect the catalytic activity of a distal domain in the protein. © 2011 European Molecular Biology Organization. 2011 Journal Article http://hdl.handle.net/20.500.11937/47501 10.1038/embor.2011.126 unknown |
| spellingShingle | Carlessi, Rodrigo Levin-Salomon, V. Ciprut, S. Bialik, S. Berissi, H. Albeck, S. Peleg, Y. Kimchi, A. GTP binding to the ROC domain of DAP-kinase regulates its function through intramolecular signalling |
| title | GTP binding to the ROC domain of DAP-kinase regulates its function through intramolecular signalling |
| title_full | GTP binding to the ROC domain of DAP-kinase regulates its function through intramolecular signalling |
| title_fullStr | GTP binding to the ROC domain of DAP-kinase regulates its function through intramolecular signalling |
| title_full_unstemmed | GTP binding to the ROC domain of DAP-kinase regulates its function through intramolecular signalling |
| title_short | GTP binding to the ROC domain of DAP-kinase regulates its function through intramolecular signalling |
| title_sort | gtp binding to the roc domain of dap-kinase regulates its function through intramolecular signalling |
| url | http://hdl.handle.net/20.500.11937/47501 |