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| | ==The structure of the C-terminal domain of the protein kinase AtSOS2 bound to the calcium sensor AtSOS3== | | ==The structure of the C-terminal domain of the protein kinase AtSOS2 bound to the calcium sensor AtSOS3== |
| - | <StructureSection load='2ehb' size='340' side='right' caption='[[2ehb]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='2ehb' size='340' side='right'caption='[[2ehb]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ehb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EHB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EHB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ehb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EHB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EHB FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SOS3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH]), SOS2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SOS3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH]), SOS2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ehb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ehb OCA], [http://pdbe.org/2ehb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ehb RCSB], [http://www.ebi.ac.uk/pdbsum/2ehb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ehb ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ehb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ehb OCA], [https://pdbe.org/2ehb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ehb RCSB], [https://www.ebi.ac.uk/pdbsum/2ehb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ehb ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CNBL4_ARATH CNBL4_ARATH]] Acts as a calcium sensor involved in the regulatory pathway for the control of intracellular Na(+) and K(+) homeostasis and salt tolerance. Operates in synergy with CIPK24/SOS2 to activate the plasma membrane Na(+)/H(+) antiporter SOS1. May function as positive regulator of salt stress responses. CBL proteins interact with CIPK serine-threonine protein kinases. Binding of a CBL protein to the regulatory NAF domain of a CIPK protein lead to the activation of the kinase in a calcium-dependent manner.<ref>PMID:11006339</ref> <ref>PMID:10725350</ref> <ref>PMID:12034882</ref> [[http://www.uniprot.org/uniprot/CIPKO_ARATH CIPKO_ARATH]] Involved in the regulatory pathway for the control of intracellular Na(+) and K(+) homeostasis and salt tolerance. Activates the vacuolar H(+)/Ca(2+) antiporter CAX1 and operates in synergy with CBL4/SOS3 to activate the plasma membrane Na(+)/H(+) antiporter SOS1. CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner. Phosphorylates CBL1, CBL4 and CBL10.<ref>PMID:10725350</ref> <ref>PMID:12034882</ref> <ref>PMID:14583601</ref> <ref>PMID:22253446</ref> | + | [[https://www.uniprot.org/uniprot/CNBL4_ARATH CNBL4_ARATH]] Acts as a calcium sensor involved in the regulatory pathway for the control of intracellular Na(+) and K(+) homeostasis and salt tolerance. Operates in synergy with CIPK24/SOS2 to activate the plasma membrane Na(+)/H(+) antiporter SOS1. May function as positive regulator of salt stress responses. CBL proteins interact with CIPK serine-threonine protein kinases. Binding of a CBL protein to the regulatory NAF domain of a CIPK protein lead to the activation of the kinase in a calcium-dependent manner.<ref>PMID:11006339</ref> <ref>PMID:10725350</ref> <ref>PMID:12034882</ref> [[https://www.uniprot.org/uniprot/CIPKO_ARATH CIPKO_ARATH]] Involved in the regulatory pathway for the control of intracellular Na(+) and K(+) homeostasis and salt tolerance. Activates the vacuolar H(+)/Ca(2+) antiporter CAX1 and operates in synergy with CBL4/SOS3 to activate the plasma membrane Na(+)/H(+) antiporter SOS1. CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner. Phosphorylates CBL1, CBL4 and CBL10.<ref>PMID:10725350</ref> <ref>PMID:12034882</ref> <ref>PMID:14583601</ref> <ref>PMID:22253446</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Arath]] | | [[Category: Arath]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Non-specific serine/threonine protein kinase]] | | [[Category: Non-specific serine/threonine protein kinase]] |
| | [[Category: Sanchez-Barrena, M J]] | | [[Category: Sanchez-Barrena, M J]] |
| Structural highlights
Function
[CNBL4_ARATH] Acts as a calcium sensor involved in the regulatory pathway for the control of intracellular Na(+) and K(+) homeostasis and salt tolerance. Operates in synergy with CIPK24/SOS2 to activate the plasma membrane Na(+)/H(+) antiporter SOS1. May function as positive regulator of salt stress responses. CBL proteins interact with CIPK serine-threonine protein kinases. Binding of a CBL protein to the regulatory NAF domain of a CIPK protein lead to the activation of the kinase in a calcium-dependent manner.[1] [2] [3] [CIPKO_ARATH] Involved in the regulatory pathway for the control of intracellular Na(+) and K(+) homeostasis and salt tolerance. Activates the vacuolar H(+)/Ca(2+) antiporter CAX1 and operates in synergy with CBL4/SOS3 to activate the plasma membrane Na(+)/H(+) antiporter SOS1. CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner. Phosphorylates CBL1, CBL4 and CBL10.[4] [5] [6] [7]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The plant SOS2 family of protein kinases and their interacting activators, the SOS3 family of calcium-binding proteins, function together in decoding calcium signals elicited by different environmental stimuli. SOS2 is activated by Ca-SOS3 and subsequently phosphorylates the ion transporter SOS1 to bring about cellular ion homeostasis under salt stress. In addition to possessing the kinase activity, members of the SOS2 family of protein kinases can bind to protein phosphatase 2Cs. The crystal structure of the binary complex of Ca-SOS3 with the C-terminal regulatory moiety of SOS2 resolves central questions regarding the dual function of SOS2 as a kinase and a phosphatase-binding protein. A comparison with the structure of unbound SOS3 reveals the basis of the molecular function of this family of kinases and their interacting calcium sensors. Furthermore, our study suggests that the structure of the phosphatase-interaction domain of SOS2 defines a scaffold module conserved from yeast to human.
The structure of the C-terminal domain of the protein kinase AtSOS2 bound to the calcium sensor AtSOS3.,Sanchez-Barrena MJ, Fujii H, Angulo I, Martinez-Ripoll M, Zhu JK, Albert A Mol Cell. 2007 May 11;26(3):427-35. PMID:17499048[8]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ishitani M, Liu J, Halfter U, Kim CS, Shi W, Zhu JK. SOS3 function in plant salt tolerance requires N-myristoylation and calcium binding. Plant Cell. 2000 Sep;12(9):1667-78. PMID:11006339
- ↑ Halfter U, Ishitani M, Zhu JK. The Arabidopsis SOS2 protein kinase physically interacts with and is activated by the calcium-binding protein SOS3. Proc Natl Acad Sci U S A. 2000 Mar 28;97(7):3735-40. PMID:10725350 doi:http://dx.doi.org/10.1073/pnas.040577697
- ↑ Qiu QS, Guo Y, Dietrich MA, Schumaker KS, Zhu JK. Regulation of SOS1, a plasma membrane Na+/H+ exchanger in Arabidopsis thaliana, by SOS2 and SOS3. Proc Natl Acad Sci U S A. 2002 Jun 11;99(12):8436-41. Epub 2002 May 28. PMID:12034882 doi:http://dx.doi.org/10.1073/pnas.122224699
- ↑ Halfter U, Ishitani M, Zhu JK. The Arabidopsis SOS2 protein kinase physically interacts with and is activated by the calcium-binding protein SOS3. Proc Natl Acad Sci U S A. 2000 Mar 28;97(7):3735-40. PMID:10725350 doi:http://dx.doi.org/10.1073/pnas.040577697
- ↑ Qiu QS, Guo Y, Dietrich MA, Schumaker KS, Zhu JK. Regulation of SOS1, a plasma membrane Na+/H+ exchanger in Arabidopsis thaliana, by SOS2 and SOS3. Proc Natl Acad Sci U S A. 2002 Jun 11;99(12):8436-41. Epub 2002 May 28. PMID:12034882 doi:http://dx.doi.org/10.1073/pnas.122224699
- ↑ Cheng NH, Pittman JK, Zhu JK, Hirschi KD. The protein kinase SOS2 activates the Arabidopsis H(+)/Ca(2+) antiporter CAX1 to integrate calcium transport and salt tolerance. J Biol Chem. 2004 Jan 23;279(4):2922-6. Epub 2003 Oct 28. PMID:14583601 doi:http://dx.doi.org/10.1074/jbc.M309084200
- ↑ Hashimoto K, Eckert C, Anschutz U, Scholz M, Held K, Waadt R, Reyer A, Hippler M, Becker D, Kudla J. Phosphorylation of calcineurin B-like (CBL) calcium sensor proteins by their CBL-interacting protein kinases (CIPKs) is required for full activity of CBL-CIPK complexes toward their target proteins. J Biol Chem. 2012 Mar 9;287(11):7956-68. doi: 10.1074/jbc.M111.279331. Epub 2012 , Jan 17. PMID:22253446 doi:http://dx.doi.org/10.1074/jbc.M111.279331
- ↑ Sanchez-Barrena MJ, Fujii H, Angulo I, Martinez-Ripoll M, Zhu JK, Albert A. The structure of the C-terminal domain of the protein kinase AtSOS2 bound to the calcium sensor AtSOS3. Mol Cell. 2007 May 11;26(3):427-35. PMID:17499048 doi:10.1016/j.molcel.2007.04.013
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