Molecular chaperone J3 regulates plasma membrane H + -ATPase activity through PKS5 interaction
Plasma membrane H + -ATPase plays an important role in maintaining plant ion balance in response to salt-alkali stress. Therefore, elucidating the regulation mechanism of plasma membrane H + -ATPase activity is essential for us to understand the response of plants to salt-alkali stress. Previous studies have found that Arabidopsis protein kinase PKS5 inhibits plasma membrane H + -ATPase activity, thereby negatively regulating the plant's salt-alkali stress response. In 2010, Guo Yan's laboratory at the Beijing Institute of Life Sciences reported in Plant Cell that a molecular chaperone J3 can activate PM-H + -ATPase and inhibit the activity of PKS5. When the plant lacks J3, it is super sensitive to external salt-alkali stress, and the activity of PM-H + ATPase also decreases. In-situ measurements were performed on the roots of living Arabidopsis using non-invasive microtesting techniques, confirming the difference in proton efflux (H + efflux) regulated by different genes, illustrating the interaction between proteins. This study found that molecular chaperone J3 can interact with PKS5 and inhibit PKS5 kinase activity, thereby positively regulating plasma membrane H + -ATPase activity and plant response to saline-alkali stress. This study identified the components of a new PKS5 signal transduction pathway that are regulating the activity of PM-H + -ATPase. The phosphorylation state of PM-H + -ATPase is very important for Arabidopsis to respond to environmental stimuli. These works revealed that the molecular chaperone protein J3 in Arabidopsis is involved in regulating the activity of PM H + -ATPase and the mechanism of plant salt-alkali stress response by inhibiting the activity of protein kinase PKS5. Keywords: non-damaging micro-measurement technology (MIFE), plasma membrane H + ATPase (PM-H + ATPase), PKS5, J3, proton flux References: Yang Y, Qin Y et al. Plant Cell, 2010 , 22: 1313-1332.
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