Lipid flippases in polarized growth

López‐Marqués, Rosa L.

doi:10.1007/s00294-020-01145-0

Cited by 7 publications

(5 citation statements)

References 76 publications

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“…Anionic phospholipids exhibit different subcellular localization patterns and functions in pollen tubes. PS is mainly distributed in the apical vesicle-rich inverted cone zone and apical plasma membrane ( Zhou et al, 2020 ; López-Marqués, 2021 ). Late endosome/multivesicular body-localized PtdIns(3)P is involved in vesicle degradation ( Vermeer et al, 2006 ).…”

Section: Discussionmentioning

confidence: 99%

“…Type IV P-type ATPases (P4-ATPases) are a class of eukaryotic-specific phospholipid flippases that flip aminophospholipids such as phosphatidylcholine, phosphatidylethanolamine, and phosphatidylserine (PS) from the extracellular/luminal leaflet of the plasma membrane/organelles to the cytoplasmic side. This process, which is powered by ATP hydrolysis, establishes and maintains the asymmetric distribution of phospholipids within the plasma membrane ( Roland and Graham, 2014 ; López-Marqués, 2021 ). In addition, P4-ATPases are involved in endosomal trafficking ( Pomorski et al, 2003 ; Poulsen et al, 2008 ; Muthusamy et al, 2009 ).…”

Section: Introductionmentioning

confidence: 99%

“…The catalytic subunit family of Arabidopsis P4-ATPases comprises 12 members, also termed Aminophospholipid ATPases 1–12 (ALA1–ALA12). Arabidopsis ALAs play key roles in many processes, including plant growth and development, reproduction, and responses and resistance to biotic and abiotic stress ( Gomès et al, 2000 ; McDowell et al, 2013 , 2015 , 2018 ; Poulsen et al, 2015 ; Guo et al, 2017 ; Niu et al, 2017 ; Zhang et al, 2020 ; López-Marqués, 2021 ; Wang et al, 2021 ). Six members of the Arabidopsis ALA family are abundantly expressed in pollen.…”

Section: Introductionmentioning

confidence: 99%

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The phospholipid flippase ALA3 regulates pollen tube growth and guidance in Arabidopsis

et al. 2022

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Pollen tube guidance regulates the growth direction and ovule targeting of pollen tubes in pistils, which is crucial for the completion of sexual reproduction in flowering plants. The Arabidopsis (Arabidopsis thaliana) pollen-specific receptor kinase (PRK) family members PRK3 and PRK6 are specifically tip-localized and essential for pollen tube growth and guidance. However, the mechanisms controlling the polar localization of PRKs at the pollen tube tip are unclear. The Arabidopsis P4-ATPase ALA3 helps establish the polar localization of apical phosphatidylserine (PS) in pollen tubes. Here, we discovered that loss of ALA3 function caused pollen tube defects in growth and ovule targeting and significantly affected the polar localization pattern of PRK3 and PRK6. Both PRK3 and PRK6 contain two polybasic clusters in the intracellular juxtamembrane domain, and they bound to PS in vitro. PRK3 and PRK6 with polybasic cluster mutations showed reduced or abolished binding to PS and altered polar localization patterns, and they failed to effectively complement the pollen tube-related phenotypes of prk mutants. These results suggest that ALA3 influences the precise localization of PRK3, PRK6 and other PRKs by regulating the distribution of PS, which plays a key role in regulating pollen tube growth and guidance.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The phospholipid flippase ALA3 regulates pollen tube growth and guidance in Arabidopsis

et al. 2022

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“…Lipid flippases are P4-ATPases, only found in eukaryotes, where they are similar in domain structures from fungi to Humans (reviewed in [12]). These proteins actively transport phospholipids from the external/luminal to cytoplasmic membrane leaflets and play an important role in polarized growth (reviewed in [13]). There are 14 P4-ATPases in Human and only 5 in the yeast S. cerevisiae (Dnf1-3, Drs2, Neo1), with most of them regulated by non-catalytic subunits from the Cdc50/Lem3 family.…”

Section: Introductionmentioning

confidence: 99%

Two distinct lipid transporters together regulate invasive filamentous growth in the human fungal pathogen Candida albicans

et al. 2022

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Flippases transport lipids across the membrane bilayer to generate and maintain asymmetry. The human fungal pathogen Candida albicans has 5 flippases, including Drs2, which is critical for filamentous growth and phosphatidylserine (PS) distribution. Furthermore, a drs2 deletion mutant is hypersensitive to the antifungal drug fluconazole and copper ions. We show here that such a flippase mutant also has an altered distribution of phosphatidylinositol 4-phosphate [PI(4)P] and ergosterol. Analyses of additional lipid transporters, i.e. the flippases Dnf1-3, and all the oxysterol binding protein (Osh) family lipid transfer proteins, i.e. Osh2-4 and Osh7, indicate that they are not critical for filamentous growth. However, deletion of Osh4 alone, which exchanges PI(4)P for sterol, in a drs2 mutant can bypass the requirement for this flippase in invasive filamentous growth. In addition, deletion of the lipid phosphatase Sac1, which dephosphorylates PI(4)P, in a drs2 mutant results in a synthetic growth defect, suggesting that Drs2 and Sac1 function in parallel pathways. Together, our results indicate that a balance between the activities of two putative lipid transporters regulates invasive filamentous growth, via PI(4)P. In contrast, deletion of OSH4 in drs2 does not restore growth on fluconazole, nor on papuamide A, a toxin that binds PS in the outer leaflet of the plasma membrane, suggesting that Drs2 has additional role(s) in plasma membrane organization, independent of Osh4. As we show that C. albicans Drs2 localizes to different structures, including the Spitzenkörper, we investigated if a specific localization of Drs2 is critical for different functions, using a synthetic physical interaction approach to restrict/stabilize Drs2 at the Spitzenkörper. Our results suggest that the localization of Drs2 at the plasma membrane is critical for C. albicans growth on fluconazole and papuamide A, but not for invasive filamentous growth.

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“…Phospholipid flippases may not be essential for cell viability, which might explain why they have not been identified in previous screening approaches for prokaryotic proteins with crucial function for cellular integrity. Flippases have been characterized in eukaryotic cells [3] but the responsible proteins do not seem to have obvious homologs in prokaryotes.…”

Section: Introductionmentioning

confidence: 99%

PplT domain proteins – ubiquitous potential prokaryotic phospholipid translocases

Hauser

Tchoupa

Zabel

et al. 2022

Preprint

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Flippase proteins exchanging phospholipids between the cytoplasmic membrane leaflets have been identified in Eukaryotes but remained largely unknown in Prokaryotes. Only MprF proteins that synthesize aminoacyl phospholipids in some bacteria have been found to contain a domain that translocates the produced lipids. We show here that this domain, which we named 'prokaryotic phospholipid translocator' (PplT), is widespread in Bacteria and Archaea, encoded as a separate protein or fused to different types of enzymes. We also demonstrate that the Escherichia coli PplT protein interacts with many phospholipid-synthetic enzymes and deletion of pplT impaired bacterial growth and membrane fluidity. Thus, PplT domain proteins appear to be general prokaryotic lipid flippases with critical roles in cellular homeostasis.

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Lipid flippases in polarized growth

Cited by 7 publications

References 76 publications

The phospholipid flippase ALA3 regulates pollen tube growth and guidance in Arabidopsis

The phospholipid flippase ALA3 regulates pollen tube growth and guidance in Arabidopsis

Two distinct lipid transporters together regulate invasive filamentous growth in the human fungal pathogen Candida albicans

PplT domain proteins – ubiquitous potential prokaryotic phospholipid translocases

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