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dc.contributor.authorAl-Younis, Inas
dc.contributor.authorWong, Aloysius
dc.contributor.authorLemtiri-Chlieh, Fouad
dc.contributor.authorSchmöckel, Sandra
dc.contributor.authorTester, Mark A.
dc.contributor.authorGehring, Christoph A
dc.contributor.authorDonaldson, Lara
dc.date.accessioned2018-12-05T08:03:56Z
dc.date.available2018-12-05T08:03:56Z
dc.date.issued2018-11-13
dc.identifier.citationAl-Younis I, Wong A, Lemtiri-Chlieh F, Schmöckel S, Tester M, et al. (2018) The Arabidopsis thaliana K+-Uptake Permease 5 (AtKUP5) Contains a Functional Cytosolic Adenylate Cyclase Essential for K+ Transport. Frontiers in Plant Science 9. Available: http://dx.doi.org/10.3389/fpls.2018.01645.
dc.identifier.issn1664-462X
dc.identifier.doi10.3389/fpls.2018.01645
dc.identifier.urihttp://hdl.handle.net/10754/630171
dc.description.abstractPotassium (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.
dc.description.sponsorshipThis project was funded by King Abdullah University of Science and Technology. AW was supported by National Natural Science Foundation of China (Grant No. 31850410470) and Zhejiang Provincial Natural Science Foundation of China (Grant No. Q19C130001). LD was supported by the National Research Foundation (Grant Nos. 91453 and 106972).
dc.publisherFrontiers Media SA
dc.relation.urlhttps://www.frontiersin.org/articles/10.3389/fpls.2018.01645
dc.rightsThis is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectAdenylate cyclase
dc.subjectArabidopsis thaliana
dc.subjectcAMP
dc.subjectsecond messenger
dc.subjectK+ Transport
dc.subjectCyaa
dc.subjectAtkup5
dc.subjectTrk1 Trk2
dc.titleThe Arabidopsis thaliana K+-Uptake Permease 5 (AtKUP5) Contains a Functional Cytosolic Adenylate Cyclase Essential for K+ Transport
dc.typeArticle
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.contributor.departmentBioscience Program
dc.contributor.departmentDesert Agriculture Initiative
dc.contributor.departmentPlant Science
dc.identifier.journalFrontiers in Plant Science
dc.eprint.versionPublisher's Version/PDF
dc.contributor.institutionCollege of Science and Technology, Wenzhou-Kean University, Wenzhou, China.
dc.contributor.institutionDepartment of Molecular and Cell Biology, University of Cape Town, Cape Town, South Africa.
kaust.personAl-Younis, Inas
kaust.personLemtiri-Chlieh, Fouad
kaust.personSchmöckel, Sandra
kaust.personTester, Mark A.
kaust.personGehring, Christoph A.
refterms.dateFOA2018-12-05T10:47:07Z


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This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
Except where otherwise noted, this item's license is described as This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.