2020
DOI: 10.1111/pce.13851
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Phosphorylation influences water and ion channel function of AtPIP2;1

Abstract: The phosphorylation state of two serine residues within the C‐terminal domain of AtPIP2;1 (S280, S283) regulates its plasma membrane localization in response to salt and osmotic stress. Here, we investigated whether the phosphorylation state of S280 and S283 also influence AtPIP2;1 facilitated water and cation transport. A series of single and double S280 and S283 phosphomimic and phosphonull AtPIP2;1 mutants were tested in heterologous systems. In Xenopus laevis oocytes, phosphomimic mutants AtPIP2;1 S280D, S… Show more

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Cited by 50 publications
(63 citation statements)
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“…4B) is an outcome of changes in stomata and/or PD reactions, changes in ion fluxes or pH, and/or other unknown at present mechanisms that shape or block the systemic hydraulic signal and require GLR3.3;GLR3.6. One possible mechanism could be mediated through the function of aquaporins that are actively regulated in plants by phosphorylation, calcium, and/or other reactions (33,(57)(58)(59)(60). If for example a particular signal such as wounding would trigger a GLR3.3;GLR3.6-dependent signaling mechanism that will cause the simultaneous closure of aquaporins in cells, at and around the vascular bundle, this process could cause an increase in hydraulic pressure in the xylem vessels; because the pressure that is usually relieved from the xylem column into neighboring cells will now cease to be relieved.…”
Section: Discussionmentioning
confidence: 99%
“…4B) is an outcome of changes in stomata and/or PD reactions, changes in ion fluxes or pH, and/or other unknown at present mechanisms that shape or block the systemic hydraulic signal and require GLR3.3;GLR3.6. One possible mechanism could be mediated through the function of aquaporins that are actively regulated in plants by phosphorylation, calcium, and/or other reactions (33,(57)(58)(59)(60). If for example a particular signal such as wounding would trigger a GLR3.3;GLR3.6-dependent signaling mechanism that will cause the simultaneous closure of aquaporins in cells, at and around the vascular bundle, this process could cause an increase in hydraulic pressure in the xylem vessels; because the pressure that is usually relieved from the xylem column into neighboring cells will now cease to be relieved.…”
Section: Discussionmentioning
confidence: 99%
“…None of the three NtPIP1s examined here enhanced permeability to water, but were permeable to H 2 O 2 (NtPIP1;1t) or BA (NtPIP1;5s) (Table 1). As permeability to H 2 O 2 and BA was not predicted for these PIP1s by Ahmed et al (2020), subtle sequence differences or pore dynamics of these isoforms clearly can modify an AQP’s preferential transport to a given substrate (Qiu et al 2020). Various PIP1 and 2 isoforms from other species are permeable to BA (e.g.…”
Section: Discussionmentioning
confidence: 99%
“…The phosphorylation of PIP channels is considered as the key mechanism for cell water flow regulation in response to environmental clues [43]. The phosphorylation of two serine residues on AtPIP2.1 was recently demonstrated to regulate the activity of this channel to shift between passage of water and ions [44]. Higher water absorption of rice grown in ammonium is connected with up-regulation of aquaporin genes [4,6].…”
Section: Discussionmentioning
confidence: 99%