Abstract
The phosphatase calcineurin and the kinases Hal4/Hal5 regulate high-affinity potassium uptake in Saccharomyces cerevisiae through the Trk1 transporter. We demonstrate that calcineurin is necessary for high-affinity potassium uptake even in the absence of Na+ stress. HAL5 expression is induced in response to stress in a calcineurin-dependent manner through a newly identified functional CDRE (nt -195/-189). Lack of calcineurin decreases Hal5 protein levels, although with little effect on Trk1 amounts. However, the growth defect of cnb1 cells at K+-limiting conditions can be rescued in part by overexpression of HAL5, and this mutation further aggravates the potassium requirements of a hal4 strain. This suggests that the control exerted by calcineurin on Hal5 expression may be biologically relevant for Trk1 regulation. © 2010 Federation of European Biochemical Societies.
Original language | English |
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Pages (from-to) | 2415-2420 |
Journal | FEBS Letters |
Volume | 584 |
DOIs | |
Publication status | Published - 1 Jun 2010 |
Keywords
- Gene expression
- High-affinity potassium transport
- Saccharomyces cerevisiae
- Trk1