Endosome-to-TGN Trafficking: Organelle-Vesicle and Organelle-Organelle Interactions

Tu, Yingfeng; Zhao, Lin; Billadeau, Daniel D.; Jia, Da

doi:10.3389/fcell.2020.00163

Cited by 66 publications

(55 citation statements)

References 146 publications

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“…The Arp2/3 activator WASH complex is required for endosome maturation and cargo sorting 36,37 and Retromer has been shown to interact directly with the WASH complex subunit FAM21 38,39 . To investigate whether the interaction is affected in the presence of Vps35 D620N, Vps35‐GFP rescue and Vps35 D620N‐GFP rescue cells were harvested for co‐immunoprecipitation using GFPTrap agarose beads.…”

Section: Resultsmentioning

confidence: 99%

Formation of retromer transport carriers is disrupted by the Parkinson disease‐linked Vps35D620Nvariant

Cui

Yang

Flores‐Rodriguez

et al. 2021

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Retromer core complex is an endosomal scaffold that plays a critical role in orchestrating protein trafficking within the endosomal system. Here we characterized the effect of the Parkinson's disease‐linked Vps35 D620N in the endo‐lysosomal system using Vps35 D620N rescue cell models. Vps35 D620N fully rescues the lysosomal and autophagy defects caused by retromer knock‐out. Analogous to Vps35 knock out cells, the endosome‐to‐trans‐Golgi network transport of cation‐independent mannose 6‐phosphate receptor (CI‐M6PR) is impaired in Vps35 D620N rescue cells because of a reduced capacity to form endosome transport carriers. Cells expressing the Vps35 D620N variant have altered endosomal morphology, resulting in smaller, rounder structures with less tubule‐like branches. At the molecular level retromer incorporating Vps35 D620N variant has a decreased binding to retromer associated proteins wiskott–aldrich syndrome protein and SCAR homologue (WASH) and SNX3 which are known to associate with retromer to form the endosome transport carriers. Hence, the partial defects on retrograde protein trafficking carriers in the presence of Vps35 D620N represents an altered cellular state able to cause Parkinson's disease.

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Section: Resultsmentioning

confidence: 99%

Formation of retromer transport carriers is disrupted by the Parkinson disease‐linked Vps35D620Nvariant

Cui

Yang

Flores‐Rodriguez

et al. 2021

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“…WASH is required for efficient endocytic recycling of multiple cargo proteins from endosomes to TGN or to the plasma membrane, through cooperating with retromer or retriever ( Derivery et al, 2009 ; Gomez and Billadeau, 2009 ; Puthenveedu et al, 2010 ; Zech et al, 2011 ; Gomez et al, 2012 ; Piotrowski et al, 2013 ; Phillips-Krawczak et al, 2015 ). Furthermore, recent studies showed that the WASH complex subunit FAM21 directly interacted with TGN-localized TBC1D23, thus mediating vesicle capturing at the TGN during endosome-to-TGN retrieval ( Newton et al, 2010 ; Shin et al, 2017 ; Huang et al, 2019 ; Liu et al, 2020 ; Tu et al, 2020 ).…”

Section: B Cenocepacia Effector Teca and The Wash Complexmentioning

confidence: 99%

“…The choice of degradation or recycling pathways, known as endosomal sorting, not only determines the fate of cell surface proteins, but also impacts numerous signaling pathways. As a consequence, dysregulation of endosomal sorting has been implicated in a wide range of human diseases, such as cancer, neurological disorders, and diabetes ( Small and Petsko, 2015 ; McMillan et al, 2017 ; Tu et al, 2020 ).…”

Section: Introductionmentioning

confidence: 99%

Targeting Endosomal Recycling Pathways by Bacterial and Viral Pathogens

Xin

Mao

Shen

et al. 2021

Front. Cell Dev. Biol.

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Endosomes are essential cellular stations where endocytic and secretory trafficking routes converge. Proteins transiting at endosomes can be degraded via lysosome, or recycled to the plasma membrane, trans-Golgi network (TGN), or other cellular destinations. Pathways regulating endosomal recycling are tightly regulated in order to preserve organelle identity, to maintain lipid homeostasis, and to support other essential cellular functions. Recent studies have revealed that both pathogenic bacteria and viruses subvert host endosomal recycling pathways for their survival and replication. Several host factors that are frequently targeted by pathogens are being identified, including retromer, TBC1D5, SNX-BARs, and the WASH complex. In this review, we will focus on the recent advances in understanding how intracellular bacteria, human papillomavirus (HPV), and severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) hijack host endosomal recycling pathways. This exciting work not only reveals distinct mechanisms employed by pathogens to manipulate host signaling pathways, but also deepens our understanding of the molecular intricacies regulating endosomal receptor trafficking.

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“…Na + /K + -ATPases present at the Golgi are likely not the source of Na + , since their inhibition did not affect Golgi pH in cervical cancer cells ( Llopis et al, 1998 ) and reduced Golgi resting pH in cystic fibrosis control cells ( Poschet et al, 2001 ). However, luminal Na + concentration could be driven by retrograde transport from endosomes to the trans -Golgi network, which delivers extracellular Na + obtained through endocytosis ( Tu et al, 2020 ). This process is thought to contribute to the high Na + concentrations observed in lysosomes, where Na + is the predominant cation at a concentration of ∼150 mM ( Wang et al, 2012 ; Xu and Ren, 2015 ).…”

Section: Discussionmentioning

confidence: 99%

The Golgi as a “Proton Sink” in Cancer

Galenkamp

Commisso

2021

Front. Cell Dev. Biol.

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Cancer cells exhibit increased glycolytic flux and adenosine triphosphate (ATP) hydrolysis. These processes increase the acidic burden on the cells through the production of lactate and protons. Nonetheless, cancer cells can maintain an alkaline intracellular pH (pHi) relative to untransformed cells, which sets the stage for optimal functioning of glycolytic enzymes, evasion of cell death, and increased proliferation and motility. Upregulation of plasma membrane transporters allows for H+ and lactate efflux; however, recent evidence suggests that the acidification of organelles can contribute to maintenance of an alkaline cytosol in cancer cells by siphoning off protons, thereby supporting tumor growth. The Golgi is such an acidic organelle, with resting pH ranging from 6.0 to 6.7. Here, we posit that the Golgi represents a “proton sink” in cancer and delineate the proton channels involved in Golgi acidification and the ion channels that influence this process. Furthermore, we discuss ion channel regulators that can affect Golgi pH and Golgi-dependent processes that may contribute to pHi homeostasis in cancer.

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Endosome-to-TGN Trafficking: Organelle-Vesicle and Organelle-Organelle Interactions

Cited by 66 publications

References 146 publications

Formation of retromer transport carriers is disrupted by the Parkinson disease‐linked Vps35D620Nvariant

Formation of retromer transport carriers is disrupted by the Parkinson disease‐linked Vps35D620Nvariant

Targeting Endosomal Recycling Pathways by Bacterial and Viral Pathogens

The Golgi as a “Proton Sink” in Cancer

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