Bif-1 regulates Atg9 trafficking by mediating the fission of Golgi membranes during autophagy

Takahashi, Yoshinori; Meyerkord, Cheryl L.; Hori, Tsukasa; Runkle, Kristin B.; Fox, Todd E.; Kester, Mark; Loughran, Thomas P.; Wang, Hong Gang

doi:10.4161/auto.7.1.14015

Cited by 152 publications

(147 citation statements)

References 45 publications

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“…It was suggested to regulate ATG9 trafficking and to mediate fission of autophagic donor membranes to trigger starvation-induced autophagy. 37,49,50 Consistent with the in vitro interaction of SH3GLB1 and TRIM63 as suggested by yeast two-hybrid and pull-down experiments, we found SH3GLB1-GFP in close proximity to the NMJ in CHRN-containing puncta. 28 Most SH3GLB1-and CHRNpositive puncta were exactly overlaying with TRIM63 (Fig.…”

Section: Discussionsupporting

confidence: 61%

Role of autophagy, SQSTM1, SH3GLB1, and TRIM63 in the turnover of nicotinic acetylcholine receptors

et al. 2013

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Section: Discussionsupporting

confidence: 61%

Role of autophagy, SQSTM1, SH3GLB1, and TRIM63 in the turnover of nicotinic acetylcholine receptors

et al. 2013

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“…Until now, no membrane-binding proteins that mediate autophagosome formation have been identified in plants. SH3P2 is structurally similar to Bif-1 ( Figure 1A), which has been proposed to function as a membrane sensor through its BAR domain (Farsad et al, 2001;Takahashi et al, 2007Takahashi et al, , 2011Takahashi et al, , 2013. SH3P2 possesses a characteristic dimerization and membranebinding ability, as evidenced by interaction studies and in vitro liposome/lipid binding assays ( Figures 9A, 9B, and 10A to 10D).…”

Section: Sh3p2 Is a Novel Membrane Binding Protein That Associates Wimentioning

confidence: 97%

“…However, SH3P1 and SH3P3, but not SH3P2, have been reported to interact with endocytic partners (Lam et al, 2001(Lam et al, , 2002, indicating that SH3P2 might function in other pathway(s). Interestingly, in mammalian cells, Bif-1, in contrast with other endophilin subfamily members, has been shown to play a role in autophagy (Takahashi et al, 2007(Takahashi et al, , 2011(Takahashi et al, , 2013.…”

Section: Green Fluorescent Protein-tagged Sh3p2 Responds To Autophagymentioning

confidence: 99%

A BAR-Domain Protein SH3P2, Which Binds to Phosphatidylinositol 3-Phosphate and ATG8, Regulates Autophagosome Formation in Arabidopsis

et al. 2013

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Autophagy is a well-defined catabolic mechanism whereby cytoplasmic materials are engulfed into a structure termed the autophagosome. In plants, little is known about the underlying mechanism of autophagosome formation. In this study, we report that SH3 DOMAIN-CONTAINING PROTEIN2 (SH3P2), a Bin-Amphiphysin-Rvs domain-containing protein, translocates to the phagophore assembly site/preautophagosome structure (PAS) upon autophagy induction and actively participates in the membrane deformation process. Using the SH3P2-green fluorescent protein fusion as a reporter, we found that the PAS develops from a cup-shaped isolation membranes or endoplasmic reticulum-derived omegasome-like structures. Using an inducible RNA interference (RNAi) approach, we show that RNAi knockdown of SH3P2 is developmentally lethal and significantly suppresses autophagosome formation. An in vitro membrane/lipid binding assay demonstrates that SH3P2 is a membrane-associated protein that binds to phosphatidylinositol 3-phosphate. SH3P2 may facilitate membrane expansion or maturation in coordination with the phosphatidylinositol 3-kinase (PI3K) complex during autophagy, as SH3P2 promotes PI3K foci formation, while PI3K inhibitor treatment inhibits SH3P2 from translocating to autophagosomes. Further interaction analysis shows that SH3P2 associates with the PI3K complex and interacts with ATG8s in Arabidopsis thaliana, whereby SH3P2 may mediate autophagy. Thus, our study has identified SH3P2 as a novel regulator of autophagy and provided a conserved model for autophagosome biogenesis in Arabidopsis.

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“…The discovery of a role for EndoA phosphorylation in macroautophagy at synapses and the connection to PD is also interesting in the context of the known role for Endophilin B1/Bax-interacting factor 1 (EndoB1) in macroautophagy (Takahashi et al, 2011;Wong et al, 2011). EndoB1 also contains an N-BAR domain, but the protein is not phosphorylated by LRRK2 (Arranz et al, 2015) and it is not known if EndoB1 acts at synapses.…”

mentioning

confidence: 99%

A LRRK2-Dependent EndophilinA Phosphoswitch Is Critical for Macroautophagy at Presynaptic Terminals

Soukup

Kuenen

Vanhauwaert

et al. 2016

Neuron

212

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Manuscript 2Synapses are often far from the soma and independently cope with proteopathic stress induced by intense neuronal activity. However, how presynaptic compartments turnover proteins is poorly understood. We show that the synapse-enriched protein EndophilinA, thus far studied for its role in endocytosis, induces macroautophagy at presynaptic terminals. We find that EndophilinA executes this unexpected function at least partly independent of its role in synaptic vesicle endocytosis. EndophilinA-induced macroautophagy is activated when the kinase LRRK2 phosphorylates the EndophilinA-BAR domain and is blocked in animals where EndophilinA cannot be phosphorylated. EndophilinA INTRODUCTIONNeurons can be metabolically very active, firing at rates of more than 100 Hz.Synaptic proteins and organelles are used and re-used multiple times and accumulate damage as a result of this stress. Furthermore, synapses are often located far away from the cell body and must therefore in part operate independently. This raises the question how synapses maintain protein quality. Given that neurodegeneration is thought to start with subtle synaptic defects before evolving into blunt neuronal death (Burke and O'Malley, 2013;, the mechanisms of synaptic protein homeostasis are likely relevant for the understanding of neurodegenerative disease.Macroautophagy is well-placed to mediate protein turnover, but how the needs of synapses are served by this process has not been well-studied. Cellular signals like stress and amino acid deprivation induce macroautophagy, where cytoplasm is engulfed by double membrane structures before fusion with degradative lysosomes (Mizushima et al., 2011).Autophagosomes have been visualized using fluorescent markers in yeast, Drosophila and mammalian cells and are often observed as Atg8/LC3 positive puncta (Kabeya et al., 2000;Scott et al., 2004). At the stage of initiation, Atg9-positive vesicles fuse into elongated preautophagosomal structures with growing edges (He et al., 2006). These edges are highly curved and harbor lipid packing defects. These edges serve as protein docking sites, attracting specific autophagic factors such as Atg3, Atg14/Barkor and Atg1 that insert into such zones, recognizing specific lipids (phosphatidylinositol-3-phosphate (PI(3)P)) and lipid packing defects (Fan et al., 2011;Nath et al., 2014;Ragusa et al., 2012). The recruitment of these factors then promotes the further steps of autophagosome formation; in particular the E2-like protein Atg3 itself recruits the autophagic marker LC3/Atg8 (Nath et al., 2014). However, how these highly curved edges are formed and maintained is very poorly understood.While autophagy has been mostly analyzed in the soma of cultured cells and yeast, autophagic markers have also been observed away from the soma at neuronal synapses 4 (Hernandez et al., 2012;Maday and Holzbaur, 2014;Williamson et al., 2010) and these markers were shown to be transported along axons (Maday and Holzbaur, 2014). However, how autophagosomes are formed at synapses an...

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Bif-1 regulates Atg9 trafficking by mediating the fission of Golgi membranes during autophagy

Cited by 152 publications

References 45 publications

Role of autophagy, SQSTM1, SH3GLB1, and TRIM63 in the turnover of nicotinic acetylcholine receptors

Role of autophagy, SQSTM1, SH3GLB1, and TRIM63 in the turnover of nicotinic acetylcholine receptors

A BAR-Domain Protein SH3P2, Which Binds to Phosphatidylinositol 3-Phosphate and ATG8, Regulates Autophagosome Formation in Arabidopsis

A LRRK2-Dependent EndophilinA Phosphoswitch Is Critical for Macroautophagy at Presynaptic Terminals

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