Calcium is the molecular switch shifting the phytosulfokine receptor 1 (PSKR1) from kinase to guanylate cyclase activity
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International Conference on Arabidopsis Research (ICAR)
2016
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author | Muleya, Victor Wheeler, J. I. Freihat, L. Thomas, L. Marondedze, C. Manallack, D. T. Ruzvidzo, O. Kwezi, L. Gehring, C. Irving, H. R. |
author_facet | Muleya, Victor Wheeler, J. I. Freihat, L. Thomas, L. Marondedze, C. Manallack, D. T. Ruzvidzo, O. Kwezi, L. Gehring, C. Irving, H. R. |
author_sort | Muleya, Victor |
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description | Conference presentation |
format | Presentation |
id | ir-11408-1691 |
institution | My University |
language | English |
publishDate | 2016 |
publisher | International Conference on Arabidopsis Research (ICAR) |
record_format | dspace |
spelling | ir-11408-16912022-10-15T20:41:04Z Calcium is the molecular switch shifting the phytosulfokine receptor 1 (PSKR1) from kinase to guanylate cyclase activity Muleya, Victor Wheeler, J. I. Freihat, L. Thomas, L. Marondedze, C. Manallack, D. T. Ruzvidzo, O. Kwezi, L. Gehring, C. Irving, H. R. Calcium, Molecular switch, Phytosulfokine receptor, Guanylate cyclase Conference presentation Many plant responses are mediated by interactions between intracellular calcium and the second messenger cGMP formed by guanylate cyclases (GCs). Previously we identified a novel class of receptor-GCs containing the GC catalytic center embedded within the kinase domain and showed that the recombinant cytoplasmic domain of phytosulfokine receptor AtPSKR1 has both guanylate cyclase and kinase activity in vitro (Kwezi et al. 2011 J Biol Chem 286: 22580-8). We now show that physiological increases in calcium levels enhance GC activity of AtPSKR1 whereas these calcium levels reversibly inhibit kinase activity. In addition PSKR1 kinase activity is reduced in the presence of the GC product cGMP. Recombinant AtPSKR1 can undergo in vitro autophosphorylation and we have confirmed it has 14 phosphorylation sites in its cytoplasmic domain including 8 serine, 3 threonine and 3 tyrosine residues. Three phospho-serine residues at the juxta-membrane position were mutated to either mimic phosphorylation on or off states. Kinase activity was enhanced in the on mutant and suppressed in the off mutant while GC activity was unaffected suggesting calcium acts as a molecular switch of PSKR1- mediated signalling that can be modulated by the phosphorylation state. The challenge now lies in understanding how molecular interactions between the GC and kinase domains are capitalized on in the plant. 2016-07-18T10:03:24Z 2016-07-18T10:03:24Z 2013 Presentation arabidopsisresearch.org/images/ICAR/24th_ICAR_ProgramAbstractBook.pdf en 24th International Conference on Arabidopsis Research (ICAR);24–28 June 2013, Sydney, Australia open International Conference on Arabidopsis Research (ICAR) |
spellingShingle | Calcium, Molecular switch, Phytosulfokine receptor, Guanylate cyclase Muleya, Victor Wheeler, J. I. Freihat, L. Thomas, L. Marondedze, C. Manallack, D. T. Ruzvidzo, O. Kwezi, L. Gehring, C. Irving, H. R. Calcium is the molecular switch shifting the phytosulfokine receptor 1 (PSKR1) from kinase to guanylate cyclase activity |
title | Calcium is the molecular switch shifting the phytosulfokine receptor 1 (PSKR1) from kinase to guanylate cyclase activity |
title_full | Calcium is the molecular switch shifting the phytosulfokine receptor 1 (PSKR1) from kinase to guanylate cyclase activity |
title_fullStr | Calcium is the molecular switch shifting the phytosulfokine receptor 1 (PSKR1) from kinase to guanylate cyclase activity |
title_full_unstemmed | Calcium is the molecular switch shifting the phytosulfokine receptor 1 (PSKR1) from kinase to guanylate cyclase activity |
title_short | Calcium is the molecular switch shifting the phytosulfokine receptor 1 (PSKR1) from kinase to guanylate cyclase activity |
title_sort | calcium is the molecular switch shifting the phytosulfokine receptor 1 (pskr1) from kinase to guanylate cyclase activity |
topic | Calcium, Molecular switch, Phytosulfokine receptor, Guanylate cyclase |
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