5aar

From Proteopedia

(Difference between revisions)

Revision as of 04:48, 25 May 2023

Structure of the ankyrin domain of an Arabidopsis Thaliana potassium channel

Structural highlights

5aar is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AKT1_ARATH Highly selective inward-rectifying potassium channel that mediate potassium uptake by plant roots in response to low K(+) conditions, by a calcium-, CBL-, and CIPK-dependent pathway. Positively regulated by phosphorylation by CIPK23. Negatively regulated by a kinase-independent regulatory mechanism involving a competing direct binding of CBL10. Involved in the stomatal regulation by monitoring the turgor pressure in guard cells. Assuming opened or closed conformations in response to the voltage difference across the membrane, the channel is activated by hyperpolarization. May interact with the cytoskeleton or with regulatory proteins.^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

Plant growth largely depends on the maintenance of adequate intracellular levels of potassium (K(+)). The families of 10 Calcineurin B-Like (CBL) calcium sensors and 26 CBL-Interacting Protein Kinases (CIPKs) of Arabidopsis (Arabidopsis thaliana) decode the calcium signals elicited by environmental inputs to regulate different ion channels and transporters involved in the control of K(+) fluxes by phosphorylation-dependent and -independent events. However, the detailed molecular mechanisms governing target specificity require investigation. Here, we show that the physical interaction between CIPK23 and the noncanonical ankyrin domain in the cytosolic side of the inward-rectifier K(+) channel AKT1 regulates kinase docking and channel activation. Point mutations on this domain specifically alter binding to CIPK23, enhancing or impairing the ability of CIPK23 to regulate channel activity. Our data demonstrate the relevance of this protein-protein interaction that contributes to the formation of a complex between CIPK23/CBL1 and AKT1 in the membrane for the proper regulation of K(+) transport.

Recognition and Activation of the Plant AKT1 Potassium Channel by the Kinase CIPK23.,Sanchez-Barrena MJ, Chaves-Sanjuan A, Raddatz N, Mendoza I, Cortes A, Gago F, Gonzalez-Rubio JM, Benavente JL, Quintero FJ, Pardo JM, Albert A Plant Physiol. 2020 Apr;182(4):2143-2153. doi: 10.1104/pp.19.01084. Epub 2020 Feb, 3. PMID:32015077^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Pilot G, Gaymard F, Mouline K, Cherel I, Sentenac H. Regulated expression of Arabidopsis shaker K+ channel genes involved in K+ uptake and distribution in the plant. Plant Mol Biol. 2003 Mar;51(5):773-87. PMID:12678562
↑ Xu J, Li HD, Chen LQ, Wang Y, Liu LL, He L, Wu WH. A protein kinase, interacting with two calcineurin B-like proteins, regulates K+ transporter AKT1 in Arabidopsis. Cell. 2006 Jun 30;125(7):1347-60. PMID:16814720 doi:http://dx.doi.org/S0092-8674(06)00769-0
↑ Li L, Kim BG, Cheong YH, Pandey GK, Luan S. A Ca(2)+ signaling pathway regulates a K(+) channel for low-K response in Arabidopsis. Proc Natl Acad Sci U S A. 2006 Aug 15;103(33):12625-30. Epub 2006 Aug 8. PMID:16895985 doi:http://dx.doi.org/0605129103
↑ Lee SC, Lan WZ, Kim BG, Li L, Cheong YH, Pandey GK, Lu G, Buchanan BB, Luan S. A protein phosphorylation/dephosphorylation network regulates a plant potassium channel. Proc Natl Acad Sci U S A. 2007 Oct 2;104(40):15959-64. Epub 2007 Sep 26. PMID:17898163 doi:http://dx.doi.org/0707912104
↑ Hirsch RE, Lewis BD, Spalding EP, Sussman MR. A role for the AKT1 potassium channel in plant nutrition. Science. 1998 May 8;280(5365):918-21. PMID:9572739
↑ Sanchez-Barrena MJ, Chaves-Sanjuan A, Raddatz N, Mendoza I, Cortes A, Gago F, Gonzalez-Rubio JM, Benavente JL, Quintero FJ, Pardo JM, Albert A. Recognition and Activation of the Plant AKT1 Potassium Channel by the Kinase CIPK23. Plant Physiol. 2020 Apr;182(4):2143-2153. doi: 10.1104/pp.19.01084. Epub 2020 Feb, 3. PMID:32015077 doi:http://dx.doi.org/10.1104/pp.19.01084

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5aar"

Categories: Arabidopsis thaliana | Large Structures | Albert A | Chaves-Sanjuan A | Sanchez-Barrena MJ

@@ Line 3: / Line 3: @@
 <StructureSection load='5aar' size='340' side='right'caption='[[5aar]], [[Resolution|resolution]] 1.87&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5aar]] is a 1 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=5AAR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5AAR FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5aar]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AAR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AAR FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5aar FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aar OCA], [http://pdbe.org/5aar PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aar RCSB], [http://www.ebi.ac.uk/pdbsum/5aar PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5aar 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=5aar FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aar OCA], [https://pdbe.org/5aar PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5aar RCSB], [https://www.ebi.ac.uk/pdbsum/5aar PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5aar ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/AKT1_ARATH AKT1_ARATH]] Highly selective inward-rectifying potassium channel that mediate potassium uptake by plant roots in response to low K(+) conditions, by a calcium-, CBL-, and CIPK-dependent pathway. Positively regulated by phosphorylation by CIPK23. Negatively regulated by a kinase-independent regulatory mechanism involving a competing direct binding of CBL10. Involved in the stomatal regulation by monitoring the turgor pressure in guard cells. Assuming opened or closed conformations in response to the voltage difference across the membrane, the channel is activated by hyperpolarization. May interact with the cytoskeleton or with regulatory proteins.<ref>PMID:12678562</ref> <ref>PMID:16814720</ref> <ref>PMID:16895985</ref> <ref>PMID:17898163</ref> <ref>PMID:9572739</ref>
+[https://www.uniprot.org/uniprot/AKT1_ARATH AKT1_ARATH] Highly selective inward-rectifying potassium channel that mediate potassium uptake by plant roots in response to low K(+) conditions, by a calcium-, CBL-, and CIPK-dependent pathway. Positively regulated by phosphorylation by CIPK23. Negatively regulated by a kinase-independent regulatory mechanism involving a competing direct binding of CBL10. Involved in the stomatal regulation by monitoring the turgor pressure in guard cells. Assuming opened or closed conformations in response to the voltage difference across the membrane, the channel is activated by hyperpolarization. May interact with the cytoskeleton or with regulatory proteins.<ref>PMID:12678562</ref> <ref>PMID:16814720</ref> <ref>PMID:16895985</ref> <ref>PMID:17898163</ref> <ref>PMID:9572739</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 18: / Line 18: @@
 </div>
 <div class="pdbe-citations 5aar" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Potassium channel 3D structures|Potassium channel 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Arath]]
+[[Category: Arabidopsis thaliana]]
 [[Category: Large Structures]]
-[[Category: Albert, A]]
+[[Category: Albert A]]
-[[Category: Chaves-Sanjuan, A]]
+[[Category: Chaves-Sanjuan A]]
-[[Category: Sanchez-Barrena, M J]]
+[[Category: Sanchez-Barrena MJ]]
-[[Category: Abiotic stress]]
-[[Category: Ankyrin]]
-[[Category: Ion homeostasis]]
-[[Category: Transport protein]]

5aar

From Proteopedia

Revision as of 04:48, 25 May 2023

Structure of the ankyrin domain of an Arabidopsis Thaliana potassium channel

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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