A nuclear role for Atg8-family proteins

Jacomin, Anne-Claire; Petridi, Stavroula; Monaco, Marisa Di; Nezis, Ioannis P.

doi:10.1080/15548627.2020.1794356

Cited by 4 publications

(5 citation statements)

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“…These results were in accordance with previous research, demonstrating that most ATGs are upregulated by nitrogen starvation, and that plant autophagy plays an important role in nutrient recycling under conditions of nitrogen and carbon starvation (Wang et al, 2019; Zhen et al, 2021). This was consistent with the fact that the activation of proteins in the ATG8 family enhances tolerance to abiotic stresses, including heat, nitrogen, carbon, and drought stress (Zhou et al, 2013; Jacomin et al, 2020; Bao et al, 2020). Further analysis of autophagosome accumulation activity showed that ATG8aOX considerably enhanced autophagosomes in the gpa1-4 mutant background under low nitrate conditions.…”

Section: Discussionsupporting

confidence: 86%

“…Because the functions of different members of ATG8-like proteins are redundant (Bu et al, 2020; Jacomin et al, 2020), we overexpressed AtATG8a in the WT background to generate transgenic lines, such as ATG8aOX #3, #5, and #7, to identify the functions of AtATG8a under low-nitrogen conditions (Supplemental Fig. S2C).…”

Section: Resultsmentioning

confidence: 99%

“…ATG8 and ATG12 belong to the ubiquitin-like conjugation system, of which ATG8 is crucial for membrane scaffold formation, elongation, and expansion during autophagosome generation (Marshall et al, 2019; Wesch et al, 2020; Johansen et al, 2020). Overexpression of AtATG8f and GmATG8c enhances tolerance to both nitrogen and carbon starvation in Arabidopsis (Jacomin et al, 2020). Moreover, interactions with ATG8 are important for regulating autophagy.…”

Section: Introductionmentioning

confidence: 99%

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Heterotrimeric G protein α subunit (GPA1) regulates the response to low-nitrogen stress in Arabidopsis by interacting with AtNRT1.4 and AtATG8a

Luo

et al. 2022

Preprint

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Efficient nitrogen absorption and utilization are important factors for higher plants to increase yield and reduce eutrophication (caused by excessive use of nitrogen fertilizers). Heterotrimeric G proteins participate in the pathway regulating nitrogen absorption and utilization in plants. However, the regulatory mechanism remains largely obscured. In this study, our results revealed that mutant gpa1-4 was tolerant to low-nitrogen stress in Arabidopsis. AtGPA1 was shown to directly interact with a nitrate transporter (AtNRT1.4) and a key autophagy-related protein (AtATG8a) on the plasma membrane. GUS staining and subcellular localization showed that AtGPA1 and AtNRT1.4 were co-expressed in roots and leaf veins and on the plasma membrane. Under low-nitrate conditions, the single mutant gpa1-4 and NRT1.4RNAi plants (AtNRT1.4RNA interference plants) and the double mutant NRT1.4RNAi/gpa1-4 plants (AtNRT1.4RNA interference plants on a gpa1-4 background) were healthier than the wild type plants. Moreover, the phenotype of the double mutant NRT1.4RNAi/gpa1-4 plants was closer to that of the NRT1.4RNAi plants compared to that of the gpa1-4 mutants. The results of the nitrate efflux rate assay in roots were consistent with the phenotypic changes under low-nitrogen conditions. These results indicated that AtGPA1 is an upstream factor that regulated the response to low-nitrogen stress through interaction with AtNRT1.4. In addition, we found that transgenic plants overexpressing AtATG8a were more tolerant to low-nitrogen stress, and their phenotype was similar to that of gpa1-4 mutants and double mutant ATG8aOX/gpa1-4 plants. Our findings may provide a new model for improving nitrogen-use efficiency through genetical modification to boost crop yields.

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Section: Discussionsupporting

confidence: 86%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Heterotrimeric G protein α subunit (GPA1) regulates the response to low-nitrogen stress in Arabidopsis by interacting with AtNRT1.4 and AtATG8a

Luo

et al. 2022

Preprint

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“…The latter was for instance found in the nuclei of all neurons in postmortem human brains 21 , and in cell cultures where a report suggested that it could shuttle in and out to regulate the expression of synapsin 98 . Interestingly in this context, recent report has also shown that ATG8 is present both in lysosomes and in the nucleus where it can regulate gene expression in association with transcription factors 71,99 . Such lysosomal-nuclear connections open the possibility of trapping molecules in the nucleus in abnormal conditions.…”

Section: Discussionmentioning

confidence: 97%

Pallidin function in drosophila surface glia regulates sleep and is dependent on amino acid availability

Hui

Aboudhiaf

Parrot

et al. 2022

Preprint

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The Pallidin protein is a component of a multimeric complex named the Biogenesis of Lysosome-related Organelles Complex-1 (BLOC1) that regulates specific endosomal function and transmembrane protein trafficking in many different cell types. In the brain, defective BLOC1 function has been linked to schizophrenia, a neuropsychiatric disorder with highly prevalent sleep disruptions, and to impaired cognitive abilities in healthy subjects. In animal models, defective BLOC-1 function also impairs behavior, memory, neurotransmission systems and metabolism. This growing body of experimental evidence suggest an involvement of BLOC1 in sleep/wake regulation. Here, we used Drosophila molecular genetics and conditional, cell-type specific knockdown strategy to address this question. We show that down-regulation of a central subunit of BLOC1, Pallidin, in the surface glia, the Drosophila equivalent of the blood brain barrier, is sufficient to reduce, fragment and delay nighttime sleep at the adult stage and in a circadian clock dependent manner. Other members of the BLOC1 complex appear to be involved in this surface glia-dependent sleep regulation. In agreement with a BLOC1 involvement in amino acid transport, down-regulation of the Large neutral Amino acid Transporter 1 (LAT1)-like transporters JhI-21 and minidiscs, phenocopy the down-regulation of pallidin. Similar results were obtained by inhibiting the TOR amino acid signaling pathway. Supplementing food with essential amino acids normalizes the sleep/wake phenotypes of pallidin and JhI-21 down-regulation. Furthermore, we identify a role for pallidin in the subcellular trafficking of JhI-21 in surface glial cells. Finally, we provide evidence that Pallidin function in surface glia is required for GABAergic neurons activation involved in promoting sleep. Taken together, these data identify a novel role for BLOC1 that, through LAT1-like transporters subcellular trafficking modulates essential amino acid availability and GABAergic sleep/wake regulation.

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“…A hallmark of most LC3-interacting proteins is the presence of an LIR motif, which is required for their interaction with LC3 ( Onishi, et al, 2021 ). The requirement for LIR motifs to convey the ability of autophagy-related proteins to interact with LC3 is conserved across the eukaryotes ( Chu, 2019 ; Jacomin, et al, 2020 ). In this study, Cg NIX, Cg FUNDC1, Cg PHB2, Cg Cardiolipin, Cg P62, and Cg OPTN were identified with one or more LIR motifs, indicating their potential interaction with Cg LC3 in oysters.…”

Section: Discussionmentioning

confidence: 99%

LC3-Mediated Mitophagy After CCCP or Vibrio splendidus Exposure in the Pacific Oyster Crassostrea gigas

Sun

Leng

et al. 2022

Front. Cell Dev. Biol.

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Mitochondrial selective autophagy, known as mitophagy, surveils the mitochondrial population by eliminating superfluous and/or impaired organelles to mediate cellular survival and viability in response to injury/trauma and infection. In this study, the components of the mitophagy pathway in the Pacific oyster Crassostrea gigas were screened from NCBI with reference to the protein sequences of the human mitophagy process. A total of 10 mitophagy process–related genes were identified from C. gigas, including NIX, FUNDC1, PHB2, Cardiolipin, P62, VDAC2, MFN2, PARL, MPP, and OPTN. They shared high similarities with their homologs in the human mitophagy pathway and were expressed in various tissues of C. gigas. After CCCP exposure, the fluorescence intensity of the mitochondrial probe JC-1 monomers increased significantly in hemocytes, while the fluorescence intensity of JC-1 aggregates decreased significantly. Meanwhile, the fluorescence of lysosomes was found to be co-localized with that of CgLC3 and mitochondria in CCCP-treated hemocytes. Double- and single-membrane-bound vacuoles resembling autophagic structures were observed in the hemocytes after CCCP exposure. The fluorescence intensity of JC-1 monomers and the abundance of CgLC3Ⅱ in hemocytes both increased after Vibrio splendidus exposure. At the same time, the green signals of CgLC3 were co-localized with red signals of the mitochondria, and the fluorescence intensity of autophagy increased significantly in hemocytes after V. splendidus exposure. The results confirmed the existence of a complete mitophagy pathway in mollusks for the first time, which was helpful for further study on the function of mitochondrial autophagy in mollusks.

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A nuclear role for Atg8-family proteins

Cited by 4 publications

References 1 publication

Heterotrimeric G protein α subunit (GPA1) regulates the response to low-nitrogen stress in Arabidopsis by interacting with AtNRT1.4 and AtATG8a

Heterotrimeric G protein α subunit (GPA1) regulates the response to low-nitrogen stress in Arabidopsis by interacting with AtNRT1.4 and AtATG8a

Pallidin function in drosophila surface glia regulates sleep and is dependent on amino acid availability

LC3-Mediated Mitophagy After CCCP or Vibrio splendidus Exposure in the Pacific Oyster Crassostrea gigas

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