Regulation of the Golgi apparatus via GOLPH3-mediated new selective autophagy

Lu, Lei; Tang, Mingzhu; Qi, Zhihao; Huang, Shifang; He, Yong-qi; Li, Dian-ke; Li, Lanfang

doi:10.1016/j.lfs.2020.117700

Cited by 22 publications

(19 citation statements)

References 22 publications

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“…2, B and D ). This shows recruitment of the fragments to autophagosomes, consistent with a recent report of sequestration of Golgi fragments into autophagosomes during starvation ( Lu et al, 2020 ). The colocalization with LC3B-positive vesicles was reduced in CALCOCO1 KO cells ( Figs.…”

Section: Resultssupporting

confidence: 91%

Regulation of Golgi turnover by CALCOCO1-mediated selective autophagy

Nthiga

Shrestha

Bruun

et al. 2021

Journal of Cell Biology

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The Golgi complex is essential for the processing, sorting, and trafficking of newly synthesized proteins and lipids. Golgi turnover is regulated to meet different cellular physiological demands. The role of autophagy in the turnover of Golgi, however, has not been clarified. Here we show that CALCOCO1 binds the Golgi-resident palmitoyltransferase ZDHHC17 to facilitate Golgi degradation by autophagy during starvation. Depletion of CALCOCO1 in cells causes expansion of the Golgi and accumulation of its structural and membrane proteins. ZDHHC17 itself is degraded by autophagy together with other Golgi membrane proteins such as TMEM165. Taken together, our data suggest a model in which CALCOCO1 mediates selective Golgiphagy to control Golgi size and morphology in eukaryotic cells via its interaction with ZDHHC17.

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Section: Resultssupporting

confidence: 91%

Regulation of Golgi turnover by CALCOCO1-mediated selective autophagy

Nthiga

Shrestha

Bruun

et al. 2021

Journal of Cell Biology

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“…The autophagic mechanism of Golgi degradation has not been thoroughly characterized, although transport from Golgi into lysosomes has been observed ( Ashok and Hegde, 2009 ; Black and Pelham, 2000 ; Briant et al, 2017 ; Chu et al, 2014 ; Gelling et al, 2012 ; Hellerschmied et al, 2019 ; Tewari et al, 2014 , 2015 ; Wolins et al, 1997 ) and Golgi components found in autophagosomes ( Lu et al, 2020 ). All of the ER-to-lysosome-associated degradation pathways that have been defined thus far require LC3 ( Chino and Mizushima, 2020 ; Fregno et al, 2018 ; Fregno and Molinari, 2019 ; Ishida et al, 2009 ; Omari et al, 2018 ), whereas autophagy of APOE in ST14A cells is not affected by knockdown of ATG7.…”

Section: Discussionmentioning

confidence: 99%

Isoform-dependent lysosomal degradation and internalization of apolipoprotein E requires autophagy proteins

Fote

Geller

Efstathiou

et al. 2022

Journal of Cell Science

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The human Apolipoprotein E4 isoform (APOE4) is the strongest genetic risk factor for late-onset Alzheimer's disease (AD), and lysosomal dysfunction has been implicated in AD pathogenesis. We found in cells stably expressing each APOE isoform that APOE4 increases lysosomal trafficking, accumulates in enlarged lysosomes and late endosomes, alters autophagic flux and the abundance of autophagy proteins and lipid droplets, and alters the proteomic contents of lysosomes following internalization. We investigated APOE-related lysosomal trafficking further in cell culture, and found that APOE from the post-golgi compartment is degraded by autophagy. We found that this autophagic process requires the lysosomal membrane protein LAMP2 in immortalized neuron-like and hepatic cells and in mouse brain tissue. Several macroautophagy-associated proteins were also required for autophagic degradation and internalization of APOE in hepatic cells. The dysregulated autophagic flux and lysosomal trafficking of APOE4 that we observed suggest a possible novel mechanism that may contribute to AD pathogenesis.

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“…More recently, Lu et al showed that GOLPH3 directly interacts with LC3 in the initiation of Golgiphagy, suggesting a role for GOLPH3 in Golgi homeostasis. However, knockdown of GOLPH3 inhibited the autophagic targeting of Golgi proteins under conditions of Golgi stress [ 88 ]; thus, the role of GOLPH3 in Golgiphagy remains to be determined. Under conditions of DNA damage, GOLPH3 is phosphorylated, causing fragmentation of the Golgi, and knockdown of GOLPH3 prevents this fragmentation under these conditions [ 89 ].…”

Section: Autophagy and The Golgi Apparatusmentioning

confidence: 99%

Maintaining Golgi Homeostasis: A Balancing Act of Two Proteolytic Pathways

Benyair

Eisenberg‐Lerner

Merbl

2022

Cells

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The Golgi apparatus is a central hub for cellular protein trafficking and signaling. Golgi structure and function is tightly coupled and undergoes dynamic changes in health and disease. A crucial requirement for maintaining Golgi homeostasis is the ability of the Golgi to target aberrant, misfolded, or otherwise unwanted proteins to degradation. Recent studies have revealed that the Golgi apparatus may degrade such proteins through autophagy, retrograde trafficking to the ER for ER-associated degradation (ERAD), and locally, through Golgi apparatus-related degradation (GARD). Here, we review recent discoveries in these mechanisms, highlighting the role of the Golgi in maintaining cellular homeostasis.

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Regulation of the Golgi apparatus via GOLPH3-mediated new selective autophagy

Cited by 22 publications

References 22 publications

Regulation of Golgi turnover by CALCOCO1-mediated selective autophagy

Regulation of Golgi turnover by CALCOCO1-mediated selective autophagy

Isoform-dependent lysosomal degradation and internalization of apolipoprotein E requires autophagy proteins

Maintaining Golgi Homeostasis: A Balancing Act of Two Proteolytic Pathways

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