Membrane Microdomains as Platform to Study Membrane-Associated Events During Oogenesis, Meiotic Maturation, and Fertilization in Xenopus laevis

Sato, Kenichi; Tokmakov, Alexander A.

doi:10.1007/978-1-4939-9009-2_5

Cited by 3 publications

(1 citation statement)

References 25 publications

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“…Membrane nanodomains serve as platforms for regulation of proteins dynamic and cellular signaling [20][21][22] . Several studies have revealed that some PM proteins can move inside and outside the membrane nanodomains to convey signals in response to developmental cues and environmental stimuli 13 .…”

Section: Ser-938 Phosphorylation Enhances Recruitment Of Fls2/bak1 He...mentioning

confidence: 99%

Single-molecule analysis reveals the phosphorylation of FLS2 governs its spatiotemporal dynamics and immunity

Cui,

Qian,

Yin

et al. 2023

Preprint

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SummaryPhosphorylation of receptor-like kinases (RLKs) plays an important role in the regulation of pattern-triggered immunity (PTI).Arabidopsis thalianaFLAGELLIN-SENSITIVE2 (FLS2) is a typical RLK that can sense a conserved 22 amino acid sequence in the N-terminal region of flagellin (flg22) to initiate plant defense pathways. However, the mechanisms underlying the regulation of FLS2 phosphorylation activity at the plasma membrane in response to flg22 remain largely enigmatic. Here, by single-particle tracking, we demonstrated that Ser-938 phosphorylation site affected flg22-induced FLS2 spatiotemporal dynamics and dwell time. Furthermore, using Förster resonance energy transfer-fluorescence lifetime (FRET-FLIM) imaging microscopy coupled with protein proximity indexes (PPI), we revealed that the degree of co-localization of FLS2/FLS2S938D-GFP with AtRem1.3-mCherry increased in response to flg22, whereas FLS2S938A-GFP did not show significant changes, indicating that Ser-938 phosphorylation site facilitates efficient sorting of FLS2 into nanodomains. Importantly, we found that the Ser-938 phosphorylation of FLS2 significantly increased flg22-induced internalization and immune responses. Taken together, these results illustrate that the phosphorylated site of FLS2 regulates the partitioning of FLS2 into functional membrane nanodomains to activate flg22-induced plant immunity.

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Section: Ser-938 Phosphorylation Enhances Recruitment Of Fls2/bak1 He...mentioning

confidence: 99%

Single-molecule analysis reveals the phosphorylation of FLS2 governs its spatiotemporal dynamics and immunity

Cui,

Qian,

Yin

et al. 2023

Preprint

View full text Add to dashboard Cite

show abstract

Uroplakin 1a Knockout Mice Display Marginal Reduction in Fecundity, Decreased Bacterial Clearance Capacity, and Drastic Changes in the Testicular Transcriptome

Munipalli

Yenugu

2022

Reprod. Sci.

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Single-molecule analysis unveils the phosphorylation of FLS2 regulates its spatiotemporal dynamics and immunity

Cui,

Qian,

Yin

et al. 2023

Preprint

View full text Add to dashboard Cite

Phosphorylation of receptor-like kinases (RLKs) plays an important role in the regulation of pattern-triggered immunity (PTI). Arabidopsis thaliana FLAGELLIN-SENSITIVE2 (FLS2) is a typical RLK that can sense a conserved 22 amino acid sequence in the N-terminal region of flagellin (flg22) to initiate plant defense pathways. However, the mechanisms underlying the regulation of FLS2 phosphorylation activity at the plasma membrane in response to flg22 remain largely enigmatic. Here, by single-particle tracking, we demonstrated that Ser-938 phosphorylation site affected flg22-induced FLS2 spatiotemporal dynamics and dwell time. Furthermore, using Förster resonance energy transfer-fluorescence lifetime (FRET-FLIM) imaging microscopy coupled with protein proximity indexes (PPI), we revealed that the degree of co-localization of FLS2/FLS2S938D-GFP with AtRem1.3-mCherry increased in response to flg22, whereas FLS2S938A-GFP did not show significant changes, indicating that Ser-938 phosphorylation site facilitates efficient sorting of FLS2 into nanodomains. Importantly, we found that the Ser-938 phosphorylation of FLS2 significantly increased flg22-induced internalization and immune responses. Taken together, these results illustrate that the phosphorylated site of FLS2 regulates the partitioning of FLS2 into functional membrane nanodomains to activate flg22-induced plant immunity.

show abstract

Membrane Microdomains as Platform to Study Membrane-Associated Events During Oogenesis, Meiotic Maturation, and Fertilization in Xenopus laevis

Cited by 3 publications

References 25 publications

Single-molecule analysis reveals the phosphorylation of FLS2 governs its spatiotemporal dynamics and immunity

Single-molecule analysis reveals the phosphorylation of FLS2 governs its spatiotemporal dynamics and immunity

Uroplakin 1a Knockout Mice Display Marginal Reduction in Fecundity, Decreased Bacterial Clearance Capacity, and Drastic Changes in the Testicular Transcriptome

Single-molecule analysis unveils the phosphorylation of FLS2 regulates its spatiotemporal dynamics and immunity

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