Golgi quality control and autophagy

Chang, Hsiu-Ju; Yang, Wan‐Fa

doi:10.1002/iub.2611

Cited by 7 publications

(3 citation statements)

References 89 publications

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“…7 ). There exists a close relationship between GA fragmentation and autophagy ( 28 ). We demonstrated that autophagy was promoted during GA fragmentation whereas it was correspondingly suppressed when GA fragmentation was inhibited by overexpression of GRASP65 ( Fig.…”

Section: Discussionmentioning

confidence: 99%

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Porcine reproductive and respiratory syndrome virus triggers Golgi apparatus fragmentation-mediated autophagy to facilitate viral self-replication

Zhao,

Qian,

Chen

et al. 2024

J Virol

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Macroautophagy/autophagy is a cellular degradation and recycling process that maintains the homeostasis of organisms. A growing number of studies have reported that autophagy participates in infection by a variety of viruses. Porcine reproductive and respiratory syndrome virus (PRRSV) causes severe financial losses to the global swine industry. Although much research has shown that PRRSV triggers autophagy for its own benefits, the exact molecular mechanisms involved in PRRSV-triggered autophagy remain to be fully elucidated. In the current study, we demonstrated that PRRSV infection significantly induced Golgi apparatus (GA) fragmentation, which promoted autophagy to facilitate viral self-replication. Mechanistically, PRRSV nonstructural protein 2 was identified to interact with and degrade the Golgi reassembly and stacking protein 65 dependent on its papain-like cysteine protease 2 activity, resulting in GA fragmentation. Upon GA fragmentation, GA-resident Ras-like protein in brain 2 was disassociated from Golgi matrix protein 130 and subsequently bound to unc-51 like autophagy activating kinase 1 (ULK1), which enhanced phosphorylation of ULK1 and promoted autophagy. Taken together, all these results expand the knowledge of PRRSV-triggered autophagy as well as PRRSV pathogenesis to support novel potential avenues for prevention and control of the virus. More importantly, these results provide the detailed mechanism of GA fragmentation-mediated autophagy, deepening the understanding of autophagic processes. IMPORTANCE Porcine reproductive and respiratory syndrome virus (PRRSV) infection results in a serious swine disease affecting pig farming worldwide. Despite that numerous studies have shown that PRRSV triggers autophagy for its self-replication, how PRRSV induces autophagy is incompletely understood. Here, we identify that PRRSV Nsp2 degrades GRASP65 to induce GA fragmentation, which dissociates RAB2 from GM130 and activates RAB2-ULK1-mediated autophagy to enhance viral replication. This work expands our understanding of PRRSV-induced autophagy and PRRSV replication, which is beneficial for anti-viral drug development.

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Section: Discussionmentioning

confidence: 99%

“…Under certain physiological and pathological circumstances, GA disorganizes into membrane fragments and small vesicles and diffuses throughout the cytoplasm, namely, GA fragmentation ( 27 ). GA fragmentation has been revealed to be involved in autophagy ( 28 ).…”

Section: Introductionmentioning

confidence: 99%

Porcine reproductive and respiratory syndrome virus triggers Golgi apparatus fragmentation-mediated autophagy to facilitate viral self-replication

Zhao,

Qian,

Chen

et al. 2024

J Virol

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“…Fragmented ER and mitochondria need to be engulfed by autophagosomes. Meanwhile, Golgi fragmentation is broadly observed in both physiological and pathological conditions, in which the Golgi ribbon structure becomes unlinked/unstacked, and is dispersed throughout the cytoplasm as tubules/vesicles (Chang and Yang, 2022 ; Wei and Seemann, 2017 ). Golgi fragmentation is induced during mitosis, under various Golgi stresses, and in pathological conditions such as apoptosis, infection, amyotrophic lateral sclerosis, Alzheimer’s disease, Parkinson’s disease, and cancer (Chang and Yang, 2022 ; Wei and Seemann, 2017 ), in addition to starvation (Lu et al, 2020 ; Nthiga et al, 2021 ; Takahashi et al, 2011 ).…”

Section: Discussionmentioning

confidence: 99%

YIPF3 and YIPF4 regulate autophagic turnover of the Golgi apparatus

Kitta,

Kaminishi,

Higashi

et al. 2024

EMBO J

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The degradation of organelles by autophagy is essential for cellular homeostasis. The Golgi apparatus has recently been demonstrated to be degraded by autophagy, but little is known about how the Golgi is recognized by the forming autophagosome. Using quantitative proteomic analysis and two novel Golgiphagy reporter systems, we found that the five-pass transmembrane Golgi-resident proteins YIPF3 and YIPF4 constitute a Golgiphagy receptor. The interaction of this complex with LC3B, GABARAP, and GABARAPL1 is dependent on a LIR motif within YIPF3 and putative phosphorylation sites immediately upstream; the stability of the complex is governed by YIPF4. Expression of a YIPF3 protein containing a mutated LIR motif caused an elongated Golgi morphology, indicating the importance of Golgi turnover via selective autophagy. The reporter assays reported here may be readily adapted to different experimental contexts to help deepen our understanding of Golgiphagy.

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