The Arabidopsis chaperone J3 regulates the plasma membrane H+-ATPase through interaction with the PKS5 Kinase

TY - JOUR

T1 - The Arabidopsis chaperone J3 regulates the plasma membrane H+-ATPase through interaction with the PKS5 Kinase

AU - Yang, Yongqing

AU - Qin, Yunxia

AU - Xie, Changgen

AU - Zhao, Feiyi

AU - Zhao, Jinfeng

AU - Liu, Dafa

AU - Chen, Shouyi

AU - Fuglsang, Anja Thoe

AU - Palmgren, Michael

AU - Schumaker, Karen

AU - Wang Deng, Xing

AU - Guo, Yan

PY - 2010/4

Y1 - 2010/4

N2 - The plasma membrane H+-ATPase (PM H+-ATPase) plays an important role in the regulation of ion and metabolite transport and is involved in physiological processes that include cell growth, intracellular pH, and stomatal regulation. PM H+-ATPase activity is controlled by many factors, including hormones, calcium, light, and environmental stresses like increased soil salinity. We have previously shown that the Arabidopsis thaliana Salt Overly Sensitive2-Like Protein Kinase5 (PKS5) negatively regulates the PM H+-ATPase. Here, we report that a chaperone, J3 (DnaJ homolog 3; heat shock protein 40-like), activates PM H+-ATPase activity by physically interacting with and repressing PKS5 kinase activity. Plants lacking J3 are hypersensitive to salt at high external pH and exhibit decreased PM H+-ATPase activity. J3 functions upstream of PKS5 as double mutants generated using j3-1 and several pks5 mutant alleles with altered kinase activity have levels of PM H+-ATPase activity and responses to salt at alkaline pH similar to their corresponding pks5 mutant. Taken together, our results demonstrate that regulation of PM H+-ATPase activity by J3 takes place via inactivation of the PKS5 kinase.

AB - The plasma membrane H+-ATPase (PM H+-ATPase) plays an important role in the regulation of ion and metabolite transport and is involved in physiological processes that include cell growth, intracellular pH, and stomatal regulation. PM H+-ATPase activity is controlled by many factors, including hormones, calcium, light, and environmental stresses like increased soil salinity. We have previously shown that the Arabidopsis thaliana Salt Overly Sensitive2-Like Protein Kinase5 (PKS5) negatively regulates the PM H+-ATPase. Here, we report that a chaperone, J3 (DnaJ homolog 3; heat shock protein 40-like), activates PM H+-ATPase activity by physically interacting with and repressing PKS5 kinase activity. Plants lacking J3 are hypersensitive to salt at high external pH and exhibit decreased PM H+-ATPase activity. J3 functions upstream of PKS5 as double mutants generated using j3-1 and several pks5 mutant alleles with altered kinase activity have levels of PM H+-ATPase activity and responses to salt at alkaline pH similar to their corresponding pks5 mutant. Taken together, our results demonstrate that regulation of PM H+-ATPase activity by J3 takes place via inactivation of the PKS5 kinase.

U2 - 10.1105/tpc.109.069609

DO - 10.1105/tpc.109.069609

M3 - Journal article

C2 - 20418496

SN - 1040-4651

VL - 22

SP - 1313

EP - 1332

JO - Plant Cell

JF - Plant Cell

IS - 4

ER -