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Regulation of Trk‐dependent potassium transport by the calcineurin pathway involves the Hal5 kinase
Author(s) -
Casado Carlos,
Yenush Lynne,
Melero Carmen,
del Carmen Ruiz María,
Serrano Raquel,
Pérez-Valle Jorge,
Ariño Joaquín,
Ramos José
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.04.042
Subject(s) - calcineurin , phosphatase , potassium , kinase , microbiology and biotechnology , biochemistry , saccharomyces cerevisiae , chemistry , protein kinase a , biology , enzyme , gene , transplantation , medicine , organic chemistry
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.