Plasma membrane nano-organization specifies phosphoinositide effects on Rho-GTPases and actin dynamics in tobacco pollen tubes

Fratini, Marta; Krishnamoorthy, Praveen; Stenzel, Irene; Riechmann, Mara; Bacia, Kirsten; Heilmann, Mareike

doi:10.1101/2020.08.12.248419

Cited by 8 publications

(12 citation statements)

References 121 publications

(196 reference statements)

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“…S9). The differences of CARKs' kinase catalytic sites are variable, which is in line with the PI4P5‐kinases that have divergent regulatory effects in tobacco pollen tubes (Fratini et al ., 2020). In view of our results, CARKs have evolutionarily conserved function in regulation of ABA signaling and diverged in adaptation to a changing environment.…”

Section: Discussionmentioning

confidence: 99%

Monomerization of abscisic acid receptors through CARKs‐mediated phosphorylation

Xie

Zhang

et al. 2022

New Phytologist

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Summary Cytosolic ABA Receptor Kinases (CARKs) play a pivotal role in abscisic acid (ABA)‐dependent pathway in response to dehydration, but their regulatory mechanism in ABA signaling remains unexplored. In this study, we showed that CARK4/5 of CARK family physically interacted with ABA receptors (RCARs/PYR1/PYLs), including RCAR3, RCAR11–RCAR14, while CARK2/7/11 only interacted with RCAR11–RCAR14, but not RCAR3. It indicates that the members in CARK family function redundantly and differentially in ABA signaling. RCAR12 can form heterodimer with RCAR3 in vitro and in vivo. Moreover, the members of CARK family can form homodimer or heterodimer in a kinase activity dependent manner. ITC (isothermal titration calorimetry) analysis demonstrated that the phosphorylation of RCAR12 by CARK1 enhanced the ABA binding affinity. The phosphor‐mimic RCAR12T105D significantly displayed ABA‐induced inhibition of the phosphatase ABI1 (ABA insensitive 1) activity, leading to upregulation of ABA‐responsive genes RD29A and RD29B in cark157:RCAR12T105D transgenic plants, which exhibited ABA hypersensitive phenotype. The transcription factor ABI5 (ABA insensitive 5) activates the transcriptions of CARK1 and CARK3 by binding to ABA‐response elements (ABREs) of their promoters. Collectively, our data imply that the dimeric CARKs phosphorylate homodimer or heterodimer ABA receptors, leading to monomerization for triggering ABA responses in Arabidopsis.

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Section: Discussionmentioning

confidence: 99%

Monomerization of abscisic acid receptors through CARKs‐mediated phosphorylation

Xie

Zhang

et al. 2022

New Phytologist

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“…Cell shrinkage also drove structural reorganization of the membrane by forcing higher lipid packing density (Janmey and Kinnunen, 2006). Recent studies shed light on the importance of spatial reorganization of membrane lipids during development of pollen grains and growth of pollen tubes (Lee et al, 2018; Fratini et al, 2020; Zhou and Dobritsa, 2020). Annexins bind preferentially anionic phospholipids and some members have been shown to associate with the membrane subdomains (Demir et al, 2013; Drücker et al, 2013).…”

Section: Discussionmentioning

confidence: 99%

Arabidopsis annexin 5 controls plasma membrane properties in mature pollen grains

Lichocka

Krzymowska

Górecka

et al. 2021

Preprint

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In Arabidopsis, a dry stigma surface enables a gradual hydration of pollen grains by a controlled release of water. Occasionally the grains may be exposed to extreme precipitations that cause rapid water influx, swelling and eventually lead to pollen membrane (PM) rupture. In metazoans, calcium- and phospholipid-binding proteins, referred to as annexins participate in repair of the plasma membrane damages. It remains unclear, however, how this process is conducted in plants. Here, we examined whether the plant annexin 5 (ANN5), the most abundant member of the annexin family in pollen, is involved in the restoration of PM integrity. We analyzed a cellular dynamics of ANN5 in the pollen grains undergoing in vitro and in vivo hydration. We observed a transient ANN5 association to PM during the in vitro hydration that did not occur in the pollen grains being hydrated on the stigma. To simulate a rainfall, we performed spraying of the pollinated stigma with deionized water that induced ANN5 accumulation at PM. Similarly, calcium or magnesium application affected PM properties and induced ANN5 recruitment to PM. Our data suggest a model, in which ANN5 is involved in the maintenance of membrane integrity in pollen grains exposed to osmotic or ionic imbalances.

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“…PI(4,5)P2 is enriched in nanodomains at the plasma membrane in pollen tubes (Fratini et al, 2020; Kost et al, 1999). These nanodomains contain PIP5K2 and are involved in actin dynamics.…”

Section: Discussionmentioning

confidence: 99%

“…Stt4p and Sac1p together control the PI4P gradient at membrane contact sites (Noack and Jaillais, 2020). A recent preprint shows that PI(4,5)P2 is enriched in nanodomains at the plasma membrane in pollen tubes (Fratini et al, 2020). These nanodomains contain PIP5K2 and are involved in actin dynamics.…”

Section: Formation and Possible Function Of Pi4kα1-containing Nanoclumentioning

confidence: 99%

A nanodomain anchored-scaffolding complex is required for PI4Kα function and localization in plants

Noack

Bayle

Armengot

et al. 2020

Preprint

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Phosphoinositides are low-abundant lipids that participate in the acquisition of membrane identity through their spatiotemporal enrichment in specific compartments. PI4P accumulates at the plant plasma membrane driving its high electrostatic potential, and thereby facilitating interactions with polybasic regions of proteins. PI4Kα1 has been suggested to produce PI4P at the plasma membrane, but how it is recruited to this compartment is unknown. Here, we pin-point the mechanism that tethers PI4Kα1 to the plasma membrane via a nanodomain-anchored scaffolding complex. We identified that PI4Kα1 is part of a heterotetrameric complex composed of proteins from the NO-POLLEN-GERMINATION, EFR3-OF-PLANTS, and HYCCIN families. Comprehensive knock-out and knock-down strategies revealed that subunits of the PI4Kα1 complex are essential for pollen, embryonic and post-embryonic development. We further found that the PI4Kα1 complex is immobilized in plasma membrane nanodomains. Using synthetic mis-targeting strategies, we demonstrate that a combination of lipid anchoring and scaffolding localizes PI4Kα1 to the plasma membrane, which is essential for its function. Together, this work opens new perspectives on the mechanisms and function of plasma membrane nanopatterning by lipid kinases.

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Plasma membrane nano-organization specifies phosphoinositide effects on Rho-GTPases and actin dynamics in tobacco pollen tubes

Cited by 8 publications

References 121 publications

Monomerization of abscisic acid receptors through CARKs‐mediated phosphorylation

Monomerization of abscisic acid receptors through CARKs‐mediated phosphorylation

Arabidopsis annexin 5 controls plasma membrane properties in mature pollen grains

A nanodomain anchored-scaffolding complex is required for PI4Kα function and localization in plants

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