Plant 14-3-3 proteins catch up with their mammalian orthologs

Oecking, Claudia; Jaspert, Nina

doi:10.1016/j.pbi.2009.08.003

Cited by 85 publications

(63 citation statements)

References 51 publications

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“…14 14-3-3s generally interact specifically with phosphorylated proteins to control their function by changing their localization, activity or stability. [15][16][17][18] We demonstrated that 14-3-3 stabilizes ACS proteins via 2 distinct mechanisms. First, 14-3-3 binds directly to ACS proteins to reduce their turnover via an ETO1/ EOL-independent mechanism.…”

mentioning

confidence: 83%

ACC synthase and its cognate E3 ligase are inversely regulated by light

Yoon

Kieber

2013

Plant Signaling & Behavior

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mentioning

confidence: 83%

ACC synthase and its cognate E3 ligase are inversely regulated by light

Yoon

Kieber

2013

Plant Signaling & Behavior

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“…Inhibition of MSL10's cell deathpromoting activity by phosphorylation was relieved when the soluble N-terminal domain was expressed alone (compare Figures 5 and 6). Perhaps dephosphorylation of the MSL10 N-terminal domain activates its cell death-promoting activity by favoring a structural rearrangement or the removal of a phospho-binding protein (Oecking and Jaspert, 2009;Bozoky et al, 2013;Yamada et al, 2013). According to this explanation, the active conformation would be favored when the soluble N-terminal domain is expressed in the absence of the rest of MSL10.…”

Section: How Does Dephosphorylation Of the Msl10 N-terminal Domain Trmentioning

confidence: 99%

Arabidopsis MSL10 Has a Regulated Cell Death Signaling Activity That Is Separable from Its Mechanosensitive Ion Channel Activity

et al. 2014

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Members of the MscS superfamily of mechanosensitive ion channels function as osmotic safety valves, releasing osmolytes under increased membrane tension. MscS homologs exhibit diverse topology and domain structure, and it has been proposed that the more complex members of the family might have novel regulatory mechanisms or molecular functions. Here, we present a study of MscS-Like (MSL)10 from Arabidopsis thaliana that supports these ideas. High-level expression of MSL10-GFP in Arabidopsis induced small stature, hydrogen peroxide accumulation, ectopic cell death, and reactive oxygen species-and cell death-associated gene expression. Phosphomimetic mutations in the MSL10 N-terminal domain prevented these phenotypes. The phosphorylation state of MSL10 also regulated its ability to induce cell death when transiently expressed in Nicotiana benthamiana leaves but did not affect subcellular localization, assembly, or channel behavior. Finally, the N-terminal domain of MSL10 was sufficient to induce cell death in tobacco, independent of phosphorylation state. We conclude that the plant-specific N-terminal domain of MSL10 is capable of inducing cell death, this activity is regulated by phosphorylation, and MSL10 has two separable activities-one as an ion channel and one as an inducer of cell death. These findings further our understanding of the evolution and significance of mechanosensitive ion channels.

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“…General Regulatory Factor/14-3-3 proteins are highly conserved in eukaryotes and function in almost all aspects of plant growth and development, including abiotic and biotic stress responses, stomatal opening, primary metabolism, hormone signaling, growth, and cell division (reviewed in Oecking and Jaspert, 2009;Denison et al, 2011;Tseng et al, 2012). The Arabidopsis genome encodes 13 14-3-3 proteins that interact with various target proteins, including kinases, transcription factors, structural proteins, ion channels, and other enzymes (Denison et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

Inhibition of the Arabidopsis Salt Overly Sensitive Pathway by 14-3-3 Proteins

et al. 2014

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The Salt Overly Sensitive (SOS) pathway regulates intracellular sodium ion (Na+) homeostasis and salt tolerance in plants. Until recently, little was known about the mechanisms that inhibit the SOS pathway when plants are grown in the absence of salt stress. In this study, we report that the Arabidopsis thaliana 14-3-3 proteins λ and κ interact with SOS2 and repress its kinase activity. Growth in the presence of salt decreases the interaction between SOS2 and the 14-3-3 proteins, leading to kinase activation in planta. 14-3-3 λ interacts with the SOS2 junction domain, which is important for its kinase activity. A phosphorylation site (Ser-294) is identified within this domain by mass spectrometry. Mutation of Ser-294 to Ala or Asp does not affect SOS2 kinase activity in the absence of the 14-3-3 proteins. However, in the presence of 14-3-3 proteins, the inhibition of SOS2 activity is decreased by the Ser-to-Ala mutation and enhanced by the Ser-to-Asp exchange. These results identify 14-3-3 λ and κ as important regulators of salt tolerance. The inhibition of SOS2 mediated by the binding of 14-3-3 proteins represents a novel mechanism that confers basal repression of the SOS pathway in the absence of salt stress.

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Plant 14-3-3 proteins catch up with their mammalian orthologs

Cited by 85 publications

References 51 publications

ACC synthase and its cognate E3 ligase are inversely regulated by light

ACC synthase and its cognate E3 ligase are inversely regulated by light

Arabidopsis MSL10 Has a Regulated Cell Death Signaling Activity That Is Separable from Its Mechanosensitive Ion Channel Activity

Inhibition of the Arabidopsis Salt Overly Sensitive Pathway by 14-3-3 Proteins

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