2017
DOI: 10.1038/s41598-017-08577-8
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Disruption of the plant-specific CFS1 gene impairs autophagosome turnover and triggers EDS1-dependent cell death

Abstract: Cell death, autophagy and endosomal sorting contribute to many physiological, developmental and immunological processes in plants. They are mechanistically interconnected and interdependent, but the molecular basis of their mutual regulation has only begun to emerge in plants. Here, we describe the identification and molecular characterization of CELL DEATH RELATED ENDOSOMAL FYVE/SYLF PROTEIN 1 (CFS1). The CFS1 protein interacts with the ENDOSOMAL SORTING COMPLEX REQUIRED FOR TRANSPORT I (ESCRT-I) component EL… Show more

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Cited by 28 publications
(31 citation statements)
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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%
“…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%
“…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%
“…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%