Calcineurin B‐like protein CBL 10 directly interacts with AKT 1 and modulates K + homeostasis in Arabidopsis
Potassium transporters and channels play crucial roles in K + uptake and translocation in plant cells. These roles are essential for plant growth and development. AKT 1 is an important K + channel in Arabidopsis roots that is involved in K + uptake. It is known that AKT 1 is activated by a protein k...
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Veröffentlicht in: | The Plant journal : for cell and molecular biology 2013-04, Vol.74 (2), p.258-266 |
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Sprache: | eng |
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Zusammenfassung: | Potassium transporters and channels play crucial roles in K
+
uptake and translocation in plant cells. These roles are essential for plant growth and development.
AKT
1 is an important K
+
channel in Arabidopsis roots that is involved in K
+
uptake. It is known that
AKT
1 is activated by a protein kinase
CIPK
23 interacting with two calcineurin B‐like proteins
CBL
1/
CBL
9. The present study showed that another calcineurin B‐like protein (
CBL
10) may also regulate
AKT
1 activity. The
CBL
10
‐over‐expressing lines showed a phenotype as sensitive as that of the
akt1
mutant under low‐K
+
conditions. In addition, the K
+
content of both
CBL
10
‐over‐expressing lines and
akt1
mutant plants were significantly reduced compared with wild‐type plants. Moreover,
CBL
10 directly interacted with
AKT
1, as verified in yeast two‐hybrid
,
Bi
FC
and co‐immunoprecipitation experiments. The results of electrophysiological analysis in both
Xenopus
oocytes and Arabidopsis root cell protoplasts demonstrated that
CBL
10 impairs
AKT
1‐mediated inward K
+
currents. Furthermore, the results from the yeast two‐hybrid competition assay indicated that
CBL
10 may compete with
CIPK
23 for binding to
AKT
1 and negatively modulate
AKT
1 activity. The present study revealed a
CBL
‐interacting protein kinase‐independent regulatory mechanism of calcineurin B‐like proteins in which
CBL
10 directly regulates
AKT
1 activity and affects ion homeostasis in plant cells. |
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ISSN: | 0960-7412 1365-313X |
DOI: | 10.1111/tpj.12123 |