Maturation-driven transport and AP-1–dependent recycling of a secretory cargo in the Golgi

Casler, Jason C.; Papanikou, Effrosyni; Barrero, Juan J.; Glick, Benjamin S.

doi:10.1083/jcb.201807195

Cited by 68 publications

(101 citation statements)

References 106 publications

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“…We used a pixel size of 60-70 nm, a frame size of 256 × 128 or 256 × 256 pixels, and a Z-step interval of 0.30 µm. For 4D imaging, Z-stacks were collected at intervals of 2 s. Three-color imaging using the JF 646 HaloTag dye (Grimm et al, 2015) was performed as previously described (Casler et al, 2019). The image stacks were deconvolved using Huygens Professional software and further processed using ImageJ (National Institutes of Health; Schneider et al, 2012).…”

Section: Construction Of a Strain Expressing Tagged Sec63mentioning

confidence: 99%

ER arrival sites associate with ER exit sites to create bidirectional transport portals

Chowdhury

Bhattacharjee

Casler

et al. 2020

Journal of Cell Biology

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COPI vesicles mediate Golgi-to-ER recycling, but COPI vesicle arrival sites at the ER have been poorly defined. We explored this issue using the yeast Pichia pastoris. ER arrival sites (ERAS) can be visualized by labeling COPI vesicle tethers such as Tip20. Our results place ERAS at the periphery of COPII-labeled ER export sites (ERES). The dynamics of ERES and ERAS are indistinguishable, indicating that these structures are tightly coupled. Displacement or degradation of Tip20 does not alter ERES organization, whereas displacement or degradation of either COPII or COPI components disrupts ERAS organization. We infer that Golgi compartments form at ERES and then produce COPI vesicles to generate ERAS. As a result, ERES and ERAS are functionally linked to create bidirectional transport portals at the ER–Golgi interface. COPI vesicles likely become tethered while they bud, thereby promoting efficient retrograde transport. In mammalian cells, the Tip20 homologue RINT1 associates with ERES, indicating possible conservation of the link between ERES and ERAS.

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Section: Construction Of a Strain Expressing Tagged Sec63mentioning

confidence: 99%

ER arrival sites associate with ER exit sites to create bidirectional transport portals

Chowdhury

Bhattacharjee

Casler

et al. 2020

Journal of Cell Biology

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“…To counter these problems, we used an alternative system that allowed synchronized release of bound fluorescent cargo from the ER (Casler, Papanikou et al 2019). In this system, the cargo, a modified DsRed-Express2, forms homo-aggregates in the ER lumen when expressed.…”

Section: Do Secreted Proteins Traffic Through Dispersed Golgi Membranmentioning

confidence: 99%

“…Other cDNAs generously provided include: St3-eGFP from Dr. Sakari Kellokumpu, (University of Oulu, Oulu, Finland), GalNAc T2-mCherry from Dr. Dibbyendu Bhattacharya (Tata Memorial Center, Mumbai, India), GalT-3xGFP and mCherry-Sec23 from Dr. Jennifer Lippincott-Schwartz (HHMI, Janelia Research Campus), GM130 GFP from Dr. Christine Suetterlin (University of California, Irvine, CA), pDsRed-ER (Takara Bio, CA), RUSH-GPI-mApple, Rush-GPI-Halo, and Ensconsin-mCherry (Addgene, MA). For imaging ER bulk flow trafficking to Golgi, a bicistronic plasmid encoding a modified DsRed-Express2 cargo (Casler, Papanikou et al 2019) and ManII-GFP was generated in the laboratory of Benjamin Glick (University of Chicago, Chicago, IL). The M. musculus ManIIA1gene was obtained from BioBasic (Toronto, Canada), PCR amplified and inserted into the DsRed-Express2 plasmid using in-fusion cloning (Takara Bio, CA).…”

Section: Antibodies Cdna Constructs and Reagentsmentioning

confidence: 99%

Nicotine exposure and neuronal activity regulate Golgi membrane dispersal and distribution

Govind

Jeyifous

Russell

et al. 2020

Preprint

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How nicotine exposure produces long-lasting changes that remodel neural circuits with addiction is unknown. Here, we report that long-term nicotine exposure alters the trafficking of a4b2-type nicotinic acetylcholine receptors (a4b2Rs) by dispersing and redistributing the Golgi apparatus. In cultured neurons, dispersed Golgi membranes were distributed throughout somata, dendrites and axons. Small, mobile vesicles in dendrites and axons lacked standard Golgi markers and were identified by other Golgi enzymes that modify glycans. Nicotine exposure increased levels of dispersed Golgi membranes, which required a4b2R expression. Similar nicotine-induced changes occurred in vivo at dopaminergic neurons at mouse nucleus accumbens terminals, consistent with these events contributing to nicotine's addictive effects. Characterization in vitro demonstrated that dispersal was reversible, that dispersed Golgi membranes were functional, and that membranes were heterogenous in size, with smaller vesicles emerging from larger "ministacks", similar to Golgi dispersal induced by nocadazole. Protocols that increased cultured neuronal synaptic excitability also increased Golgi dispersal, without the requirement of a4b2R expression. Our findings reveal novel activity-and nicotine-dependent changes in neuronal intracellular morphology. These changes regulate levels and location of dispersed Golgi membranes at dendrites and axons, which function in local trafficking at subdomains.

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“…The recycling of glyco-enzymes requires specific adaptors that gate their entry into COPI coated retrograde transport vesicles. Among the adaptors so far identified the COPI  and  subunits and the Golgi phosphoprotein 3 (GOLPH3) are the best characterized (Casler et al, 2019;Liu et al, 2018;Schmitz et al, 2008;Tu et al, 2008). The role of GOLPH3 in enzyme recycling was first demonstrated in yeast by Banfield and Burd (Schmitz et al, 2008;Tu et al, 2008) and later shown to be conserved in metazoa including mammals (Ali et al, 2012;Chang et al, 2013;Eckert et al, 2014;Isaji et al, 2014;Pereira et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

“…This results in the incorporation of the Vps74p clients into COPI recycling vesicles and hence in their retrograde transport within the secretory pathway. Thus, changing the levels of Vps74p alters the distribution of the Vps74p clients across the transport stations (Casler et al, 2019;Liu et al, 2018;Schmitz et al, 2008;Tu et al, 2008;Wood et al, 2009). Importantly, the human GOLPH3 gene is amplified in solid tumors where it stimulates mitogenic signaling and cell proliferation, acting as an oncogene (Scott et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

The Glyco-enzyme adaptor GOLPH3 Links Intra-Golgi Transport Dynamics to Glycosylation Patterns and Cell Proliferation

Rizzo

Russo

Kurokawa

et al. 2019

Preprint

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Glycans are ubiquitous sugar polymers with major biological functions that are assembled by glyco-enzymes onto cargo molecules during their transport through the Golgi complex. How the Golgi determines glycan assembly is poorly understood. By relying on the Golgi cisternal maturation model and using the glyco-enzyme adaptor and oncoprotein GOLPH3 as a molecular tool, we define the first example of how the Golgi controls glycosylation and associated cell functions. GOLPH3, acting as a component of the cisternal maturation mechanism, selectively binds and recycles a subset of glyco-enzymes of the glycosphingolipid synthetic pathway, hinders their escape to the lysosomes and hence increases their levels through a novel lysosomal degradation-regulated mechanism. This enhances the production of specific growth-inducing glycosphingolipids and reprograms the glycosphingolipid pathway to potentiate mitogenic signaling and cell proliferation. These findings unravel unforeseen organizing principles of Golgi-dependent glycosylation and delineate a paradigm for glycan assembly by the Golgi transport mechanisms. Moreover, they indicate a new role of cisternal maturation as a regulator of glycosylation, and outline a novel mechanism of action for GOLPH3-induced proliferation.

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Maturation-driven transport and AP-1–dependent recycling of a secretory cargo in the Golgi

Abstract: The Golgi cisternal maturation model predicts that secretory cargo proteins should be continuously present within the cisternae while resident Golgi proteins come and go. Casler et al. verify this prediction by tracking the passage of a fluorescent secretory cargo through the yeast Golgi.

Cited by 68 publications

References 106 publications

ER arrival sites associate with ER exit sites to create bidirectional transport portals

ER arrival sites associate with ER exit sites to create bidirectional transport portals

Nicotine exposure and neuronal activity regulate Golgi membrane dispersal and distribution

The Glyco-enzyme adaptor GOLPH3 Links Intra-Golgi Transport Dynamics to Glycosylation Patterns and Cell Proliferation

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