Disruption of the plant-specific CFS1 gene impairs autophagosome turnover and triggers EDS1-dependent cell death

Sutipatanasomboon, Arpaporn; Herberth, Stefanie; Alwood, Ellen G.; Häweker, Heidrun; Müller, Boje; Shahriari, Mojgan; Zienert, Anke Y.; Marin, Birger; Robatzek, Silke; Praefcke, Gerrit J. K.; Ayscough, Kathryn R.; Hülskamp, Martin; Schellmann, Swen

doi:10.1038/s41598-017-08577-8

Cited by 28 publications

(31 citation statements)

References 69 publications

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“…A plant-specific ESCRT component, FREE1 (FYVE domain protein required for endosomal sorting 1), was reported to directly interact with the autophagy regulator SH3P2 and to play a role in autophagosome-vacuole fusion in Arabidopsis (Zhuang et al, 2013;Gao et al, 2015). Arabidopsis CFS1 (Cell death related endosomal FYVE/SYLF protein 1), a FYVE and SYLF domaincontaining protein unique to plants that co-localizes and interacts with PI3P and the ESCRT-I component ELCH, is enriched in the autophagosome membrane and participates in autophagosome turnover (Sutipatanasomboon et al, 2017).…”

Section: Autophagy In Plants the Molecular Mechanism Of Autophagymentioning

confidence: 99%

Autophagy: An Intracellular Degradation Pathway Regulating Plant Survival and Stress Response

et al. 2020

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Autophagy is an intracellular process that facilitates the bulk degradation of cytoplasmic materials by the vacuole or lysosome in eukaryotes. This conserved process is achieved through the coordination of different autophagy-related genes (ATGs). Autophagy is essential for recycling cytoplasmic material and eliminating damaged or dysfunctional cell constituents, such as proteins, aggregates or even entire organelles. Plant autophagy is necessary for maintaining cellular homeostasis under normal conditions and is upregulated during abiotic and biotic stress to prolong cell life. In this review, we present recent advances on our understanding of the molecular mechanisms of autophagy in plants and how autophagy contributes to plant development and plants' adaptation to the environment.

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Section: Autophagy In Plants the Molecular Mechanism Of Autophagymentioning

confidence: 99%

Autophagy: An Intracellular Degradation Pathway Regulating Plant Survival and Stress Response

et al. 2020

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“…The SYLF domain is named "SYLF" on the basis of its representative members (SH3YL1, Ysc84p/Lsb4p, Lsb3p, and plant FYVE protein), and comprises a segment of ≈220 residues shown to be a lipid-binding module. Both the FYVE and the SYLF domain of AtFYVE2 also referred as CFS1 (CELL DEATH RELATED ENDOSOMAL FYVE/SYLF PROTEIN 1), were shown to bind to PtdIns3P (Sutipatanasomboon et al 2017). A subgroup of proteins from class II including PpFYVE2…”

Section: Structural Annotation Of Ppfyve and Ppphox Genesmentioning

confidence: 99%

“…and AtFYVE2, exhibit a P(S/T)XP motif which is known from yeast and mammals to mediate binding to the Vps23/TSG101 subunit of the endosomal sorting complex required for transport (ESCRT)-I. AtFYVE2 is the only characterized protein from this class, and is involved in fusion events between autophagosomes and ESCRT-positive late endosomes (LEs), affecting autophagosome degradation and protein homeostasis (Sutipatanasomboon et al 2017). The class III FYVE is represented by a single member in all species studied, except for G. max which has two members.…”

Section: Structural Annotation Of Ppfyve and Ppphox Genesmentioning

confidence: 99%

Evolutionary insights into FYVE and PHOX effector proteins from the moss Physcomitrella patens

Patrícia

Fortes

Suárez

et al. 2020

Planta

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Phosphatidylinositol 3-phosphate (PtdIns3P) is one of the five different phosphoinositides (PPIs) species in plant cells, which regulate several aspects of plant growth and development, as well as responses to biotic and abiotic stresses. The mechanistic insights underlying PtdIns3P mode of action, specifically through PtdIns3P-binding effectors such as FYVE and PHOX proteins have been partially explored in plants with main focus on Arabidopsis thaliana. Additionally, they have been underexplored in other plant organisms such as bryophytes, the earliest diverging group of terrestrial flora. In this study, we searched for genes coding for FYVE and PHOX domains containing sequences from different photosynthetic organisms in order to gather evolutionary insights on these PPI binding domains, followed by an in silico characterization of the FYVE and PHOX gene family in the moss Physcomitrella patens. Phylogenetic analysis showed that PpFYVE proteins can be grouped in 7 subclasses, with an additional subclass whose FYVE domain was lost during evolution to higher plants. On the other hand, PpPHOX proteins are classified into 5 subclasses. Expression analyses based on RNAseq data together with the analysis of cis-acting regulatory elements and transcription factor binding sites in promoter regions suggest the importance of these proteins in regulating stress responses but mainly developmental processes in P. patens. The results provide valuable information and robust candidate genes for future functional analysis aiming to further explore the role of this signaling pathway mainly during growth and development of tip growing cells and during the transition from 2D to 3D growth, which could provide ancestral regulatory players undertaken during plant evolution. .

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“…The first arginine in the consensus sequence R 1 RHHCR has a substitution for glycine or serine (Supplemental Fig. 1), but in A. thaliana it maintains the ability to bind PtdIns3P, together with the SYLF domain exhibited by these proteins (Sutipatanasomboon et al 2017 (Sutipatanasomboon et al 2017).…”

Section: Evolution Of Fyve and Phox Domains In Viridiplantaementioning

confidence: 99%

Evolutionary insights into PtdIns3P signaling through FYVE and PHOX effector proteins from the moss Physcomitrella patens

Patrícia

Fortes

Suárez

et al. 2019

Preprint

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ABSTRACTPhosphatidylinositol 3-phosphate (PtdIns3P) is one of the five different phosphoinositides (PPIs) species in plant cells, which regulate several aspects of plant growth and development, as well as responses to biotic and abiotic stresses. The mechanistic insights underlying PtdIns3P mode of action, specifically through PtdIns3P-binding effectors such as FYVE and PHOX proteins have been partially explored in plants with main focus on Arabidopsis thaliana. Additionally, they have been underexplored in other plant organisms such as bryophytes, the earliest diverging group of terrestrial flora.In this study, we searched for genes coding for FYVE and PHOX domains containing sequences from different photosynthetic organisms in order to gather evolutionary insights on these PPI binding domains, followed by an in silico characterization of the FYVE and PHOX gene family in the moss Physcomitrella patens. Phylogenetic analysis showed that PpFYVE proteins can be grouped in 7 subclasses, with an additional subclass whose FYVE domain was lost during evolution to higher plants. On the other hand, PpPHOX proteins are classified into 5 subclasses. Expression analyses based on RNAseq data together with the analysis of cis-acting regulatory elements and transcription factor binding sites in promoter regions suggest the importance of these proteins in regulating stress responses but mainly developmental processes in P. patens. The results provide valuable information and robust candidate genes for future functional analysis aiming to further explore the role of this signaling pathway mainly during growth and development of tip growing cells and during the transition from 2D to 3D growth, which could provide ancestral regulatory players undertaken during plant evolution.

show abstract

Disruption of the plant-specific CFS1 gene impairs autophagosome turnover and triggers EDS1-dependent cell death

Cited by 28 publications

References 69 publications

Autophagy: An Intracellular Degradation Pathway Regulating Plant Survival and Stress Response

Autophagy: An Intracellular Degradation Pathway Regulating Plant Survival and Stress Response

Evolutionary insights into FYVE and PHOX effector proteins from the moss Physcomitrella patens

Evolutionary insights into PtdIns3P signaling through FYVE and PHOX effector proteins from the moss Physcomitrella patens

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