Please use this identifier to cite or link to this item:
https://hdl.handle.net/20.500.12540/53
DC Field | Value | Language |
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dc.contributor.author | Al-Younis, Inas | en_US |
dc.contributor.author | Wong, Aloysius | en_US |
dc.contributor.author | Lemtiri-Chlieh, Fouad | en_US |
dc.contributor.author | Schmöckel, Sandra | en_US |
dc.contributor.author | Tester, Mark | en_US |
dc.contributor.author | Gehring, Chris | en_US |
dc.contributor.author | Donaldson, Lara | en_US |
dc.date.accessioned | 2020-06-19T02:45:25Z | - |
dc.date.available | 2020-06-19T02:45:25Z | - |
dc.date.issued | 2018 | - |
dc.identifier.citation | Al-Younis, I., Wong, A., Lemtiri-Chlieh, F., Schmöckel, S., Tester, M., Gehring, C., & Donaldson, L. (2018). The Arabidopsis thaliana K+-uptake permease 5 (AtKUP5) contains a functional cytosolic adenylate cyclase essential for K+ transport. Frontiers in plant science, 9, 1645. | en_US |
dc.identifier.uri | https://hdl.handle.net/20.500.12540/53 | - |
dc.description.abstract | Potassium (K+) is the most abundant cation in plants, and its uptake and transport are key to growth, development and responses to the environment. Here, we report that Arabidopsis thaliana K+ uptake permease 5 (AtKUP5) contains an adenylate cyclase (AC) catalytic center embedded in its N-terminal cytosolic domain. The purified recombinant AC domain generates cAMP in vitro; and when expressed in Escherichia coli, increases cAMP levels in vivo. Both the AC domain and full length AtKUP5 rescue an AC-deficient E. coli mutant, cyaA, and together these data provide evidence that AtKUP5 functions as an AC. Furthermore, full length AtKUP5 complements the Saccharomyces cerevisiae K+ transport impaired mutant, trk1 trk2, demonstrating its function as a K+ transporter. Surprisingly, a point mutation in the AC center that impairs AC activity, also abolishes complementation of trk1 trk2, suggesting that a functional catalytic AC domain is essential for K+ uptake. AtKUP5-mediated K+ uptake is not affected by cAMP, the catalytic product of the AC, but, interestingly, causes cytosolic cAMP accumulation. These findings are consistent with a role for AtKUP5 as K+ flux sensor, where the flux-dependent cAMP increases modulate downstream components essential for K+ homeostasis, such as cyclic nucleotide gated channels. | en_US |
dc.format.extent | 15 pages | en_US |
dc.format.mimetype | application/pdf | en_US |
dc.language.iso | eng | en_US |
dc.publisher | Frontiers Media S.A. | en_US |
dc.relation.ispartof | Frontiers in Plant Science | en_US |
dc.rights.uri | https://creativecommons.org/licenses/by-nc/4.0/ | - |
dc.subject.lcsh | Arabidopsis Thaliana | en_US |
dc.subject.lcsh | Potassium | en_US |
dc.title | The Arabidopsis thaliana K+-uptake permease 5 (AtKUP5) contains a functional cytosolic adenylate cyclase essential for K+ transport | en_US |
dc.type | Article | en_US |
dc.rights.license | Attribution-NonCommercial 4.0 International (CC BY-NC 4.0) | en_US |
dc.identifier.doi | 10.3389/fpls.2018.01645 | - |
dc.subject.keywords | AtKUP5 | en_US |
dc.subject.keywords | K+ Transport | en_US |
Appears in Collections: | Scholarly Publications |
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File | Description | Size | Format | |
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wku_schlrs_publcn_000029.pdf | 4.6 MB | Adobe PDF | View/Open |
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