AUTHOR=Al-Younis Inas , Wong Aloysius , Lemtiri-Chlieh Fouad , Schmöckel Sandra , Tester Mark , Gehring Chris , Donaldson Lara TITLE=The Arabidopsis thaliana K+-Uptake Permease 5 (AtKUP5) Contains a Functional Cytosolic Adenylate Cyclase Essential for K+ Transport JOURNAL=Frontiers in Plant Science VOLUME=9 YEAR=2018 URL=https://www.frontiersin.org/journals/plant-science/articles/10.3389/fpls.2018.01645 DOI=10.3389/fpls.2018.01645 ISSN=1664-462X 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.