GORASP2/GRASP55 collaborates with the PtdIns3K UVRAG complex to facilitate autophagosome-lysosome fusion

Zhang, Xiaoyan; Wang, Leibin; Ireland, Stephen; Ahat, Erpan; Li, Jie; Bekier, Michael E.; Zhang, Zhihai; Wang, Yanzhuang

doi:10.1080/15548627.2019.1596480

Cited by 55 publications

(60 citation statements)

References 55 publications

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“…, 2016 ) and that there is a link between Golgi function and autophagy ( Zhang et al. , 2018 , 2019 ). However, this possibility was ruled out by BafA1 treatment, which inhibits lysosomal degradation but not Arl1 and Golgin-97 degradation in H 2 O 2 -treated cells.…”

Section: Discussionmentioning

confidence: 99%

Hydrogen peroxide induces Arl1 degradation and impairs Golgi-mediated trafficking

Ireland

Huang

Zhang

et al. 2020

MBoC

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Reactive oxygen species (ROS)-induced oxidative stress has been associated with diseases such as amyotrophic lateral sclerosis (ALS), stroke and cancer. While the effect of ROS on mitochondria and endoplasmic reticulum (ER) has been well documented, its consequence on the Golgi apparatus is less well understood. In this study, we characterized the Golgi structure and function in HeLa cells after exposure to hydrogen peroxide (H2O2), a reagent commonly used to introduce ROS to cells. Treatment of cells with 1 mM H2O2 for 10 min resulted in the degradation of Arl1 and dissociation of GRIP-domain containing proteins Golgin-97 and Golgin-245 from the trans-Golgi. This effect could be rescued by treatment of cells with a ROS scavenger N-acetyl cysteine (NAC) or protease inhibitors. Structurally, H2O2 treatment reduced the number of cisternal membranes per Golgi stack, suggesting a loss of trans-Golgi cisternae. Functionally, H2O2 treatment inhibited both anterograde and retrograde protein transport, consistent with the loss of membrane tethers on the trans-Golgi cisternae. This study revealed membrane tethers at the trans-Golgi as novel specific targets of ROS in cells.

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Section: Discussionmentioning

confidence: 99%

Hydrogen peroxide induces Arl1 degradation and impairs Golgi-mediated trafficking

Ireland

Huang

Zhang

et al. 2020

MBoC

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“…Enhance autophagy induction and promote autophagosome-lysosome fusion Phospholipid binding C2 domain √ √ (Liang et al, 2008;He et al, 2013;Zhang et al, 2019) WIPI2 WIPI4 Atg18 Atg21 PI3P binding protein: WIPI2 recruits ATG12∼ATG5-ATG16L1 to phagophore, retrieves of ATG9 from early autophagosome membranes; WIPI4 can bind with ATG2 in the regulation of lipid transfer 6CD loop in ß-propeller structure √ √ (Watanabe et al, 2012) Lipids and membrane-associated proteins in autophagy Ichimura et al, 2000;Nath et al, 2014) ATG5…”

Section: Vps38mentioning

confidence: 99%

“…colleagues demonstrated that cysteine-mediated oligomerization of ATG14 promotes the fusion of autophagosomes and lysosomes by tethering these two organelles and it can assist STX17 to recruit SNAP29 to autophagosomes promoting the assembly of SNARE complex (Diao et al, 2015). Besides, from the genetic analysis, the HOPS complex also plays a crucial role in the fusion between autophagosomes and lysosomes, likely through tethering of these two organelles together with SNAREs, Rabs, and other tethering related proteins such as PLEKHM1 (Pleckstrin homology domain-containing family M member 1) (McEwan et al, 2015), UVRAG (UV radiation resistance-associated protein) (Liang et al, 2008), EPG5 (Ectopic P granules protein 5 homolog) (Wang et al, 2016), BRUCE (BIR repeat-containing ubiquitin-conjugating enzyme) (Ebner et al, 2018), TECPR1 (Chen et al, 2012), GRASP55 (Golgi reassemblystacking protein 55) (Zhang et al, 2019), and etc. Together, these proteins might behave as a template for SNAREs to register and assemble on it, or to expand the fusion pore as we learned from the biochemical studies of yeast vacuole fusion (Liang et al, 2008;Jiang et al, 2014;McEwan et al, 2015;Ding et al, 2019).…”

Section: Autophagosome-lysosome Fusionmentioning

confidence: 99%

Lipids and membrane-associated proteins in autophagy

Tong

et al. 2020

Protein Cell

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Autophagy is essential for the maintenance of cellular homeostasis and its dysfunction has been linked to various diseases. Autophagy is a membrane driven process and tightly regulated by membrane-associated proteins. Here, we summarized membrane lipid composition, and membrane-associated proteins relevant to autophagy from a spatiotemporal perspective. In particular, we focused on three important membrane remodeling processes in autophagy, lipid transfer for phagophore elongation, membrane scission for phagophore closure, and autophagosome-lysosome membrane fusion. We discussed the significance of the discoveries in this field and possible avenues to follow for future studies. Finally, we summarized the membrane-associated biochemical techniques and assays used to study membrane properties, with a discussion of their applications in autophagy.

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“…Upon glucose starvation, GORASP2 is de-O-GlcNAcylated and acts as a membrane tether to facilitate autophagosome-lysosome fusion (Zhang et al, 2018). Additionally, GORASP55 interacts with BECN1 to facilitate the assembly and membrane association of the PtdIns3K UVRAG complex (Zhang et al, 2019). Furthermore, GRASP55 displays positive regulatory effects on autophagy induction and influences the lipidation of LC3b (Dupont et al, 2011).…”

Section: Gorasp2/grasp55mentioning

confidence: 99%

Golgi Apparatus: A Potential Therapeutic Target for Autophagy-Associated Neurological Diseases

Deng

Liu

et al. 2020

Front. Cell Dev. Biol.

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Autophagy has dual effects in human diseases: appropriate autophagy may protect cells from stress, while excessive autophagy may cause cell death. Additionally, close interactions exist between autophagy and the Golgi. This review outlines recent advances regarding the role of the Golgi apparatus in autophagy. The signaling processes of autophagy are dependent on the normal function of the Golgi. Specifically, (i) autophagy-related protein 9 is mainly located in the Golgi and forms new autophagosomes in response to stressors; (ii) Golgi fragmentation is induced by Golgirelated proteins and accompanied with autophagy induction; and (iii) the endoplasmic reticulum-Golgi intermediate compartment and the reticular trans-Golgi network play essential roles in autophagosome formation to provide a template for lipidation of microtubule-associated protein 1A/1B-light chain 3 and induce further ubiquitination. Golgi-related proteins regulate formation of autophagosomes, and disrupted formation of autophagy can influence Golgi function. Notably, aberrant autophagy has been demonstrated to be implicated in neurological diseases. Thus, targeted therapies aimed at protecting the Golgi or regulating Golgi proteins might prevent or ameliorate autophagy-related neurological diseases. Further studies are needed to investigate the potential application of Golgi therapy in autophagy-based neurological diseases.

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GORASP2/GRASP55 collaborates with the PtdIns3K UVRAG complex to facilitate autophagosome-lysosome fusion

Cited by 55 publications

References 55 publications

Hydrogen peroxide induces Arl1 degradation and impairs Golgi-mediated trafficking

Hydrogen peroxide induces Arl1 degradation and impairs Golgi-mediated trafficking

Lipids and membrane-associated proteins in autophagy

Golgi Apparatus: A Potential Therapeutic Target for Autophagy-Associated Neurological Diseases

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