ER exit sites in Drosophila display abundant ER-Golgi vesicles and pearled tubes but no megacarriers

Yang, Ke; Liu, Min; Feng, Zhi Jing; Rojas, Marta; Zhou, Lingjian; Ke, Hongmei; Pastor-Pareja, José Carlos

doi:10.1016/j.celrep.2021.109707

Cited by 24 publications

(46 citation statements)

References 88 publications

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“…A recent manuscript studied the Drosophila ER-Golgi interface using SIM, APEX-TEM, and FIB-SEM. [45] Apart from unidentified 50 nm diameter vesicles in the drosophila cells that were absent from the mammalian system, [31] COPI and COPII localizations and proximity were compatible with the new model advocated here.…”

Section: Rough Edges Of the Copii Hypothesissupporting

confidence: 76%

Hanging the coat on a collar: Same function but different localization and mechanism for COPII

2022

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An entirely different mechanism and localization were recently proposed for the COPII coat complex, challenging its well-accepted function to select and concentrate cargo into small COPII-coated spherical transport vesicles. Instead, the COPII complex is suggested to form a dynamic yet stationary collar that forms a boundary between the ER and the ER export membrane domain. This membrane domain, the ER exit site (ERES), is the site of COPII-mediated sorting and concentration of transport competent proteins. Subsequently, the ERES is implicated to mature and bud to form a sizeable pleiomorphic transport carrier that translocate on microtubules to fuse with the Golgi apparatus. Despite this drastic mechanistic dogma shift, most of the underlying protein-protein and protein-membrane interactions remain unchanged. Here, we attempt to provide a detailed description of the newly proposed model of how ER to Golgi transport works by describing the role of several essential proteins of the transport machinery.

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Section: Rough Edges Of the Copii Hypothesissupporting

confidence: 76%

Hanging the coat on a collar: Same function but different localization and mechanism for COPII

2022

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“…4F). These findings suggest that after residing in the tER or at ERES for approximately four minutes, the bulk of Serp-SBG translocates to an adjacent compartment, corresponding to Golgi cisternae (Yang et al, 2021), where the protein spends approximately eight minutes before exiting the Golgi apparatus (Fig. 4E).…”

Section: Resultsmentioning

confidence: 93%

“…S3A; Ivan et al, 2008) and localized adjacent to the cis -Golgi marker GRASP65-GFP (Fig. S3B; Yang et al, 2021).…”

Section: Resultsmentioning

confidence: 99%

“…The use of RUSH revealed rapid ER exit and passage of the Golgi apparatus by secretory proteins in epithelia in vivo . While mammalian cells typically contain a single pile of interconnected Golgi stacks with tubular ERES extending between ER and Golgi (Weigel et al, 2021), Drosophila cells contain several dispersed Golgi mini-stacks (Kondylis and Rabouille, 2009) adjacent to C- or ring-shaped ERES (Reynolds et al, 2019; Yang et al, 2021). Despite these differences, ER-Golgi trafficking in Drosophila tracheal cells occurred on similar time scales (2 to 3 min for Serp-SBG) as described for various GPI-linked and transmembrane RUSH cargos in mammalian cells (Weigel et al, 2021).…”

Section: Discussionmentioning

confidence: 99%

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Acute manipulation and real-time visualization of membrane trafficking and exocytosis inDrosophila

Glashauser

Camelo

Hollmann

et al. 2022

Preprint

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Intracellular trafficking of secretory proteins plays key roles in animal development and physiology, but essential tools for investigating the dynamics of trafficking have been limited to cultured cells. Here we present a system that enables acute manipulation and real-time visualization of membrane trafficking through reversible retention of proteins in the endoplasmic reticulum (ER) in living multicellular organisms. By adapting the retention using selective hooks (RUSH) approach to Drosophila, we show that trafficking of GPI-linked, secreted, and transmembrane proteins can be controlled with high temporal precision using streptavidin hooks and biotin-induced release in intact animals and cultured organs. We demonstrate the potential of this approach by analyzing the kinetics of ER exit and of apical secretion in tracheal tubes and the spatiotemporal dynamics of tricellular junction assembly in epithelia. Furthermore, hook-induced ER retention enables tissue-specific knockdown of secretory protein function. The system is compatible with available protein-traps and is widely applicable to investigate membrane trafficking in diverse cell types in vivo.

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“…It would appear that COPII proteins play a novel role focussing on cargo selection rather than vesicle formation. On the other hand, it has recently been reported that ER exit sites (ERES) display abundant COPII vesicles and pearled tubes in Drosophila , similar to the tubular ERES extensions in mammalian cells [30,32]. These novel evidence of diverse ER exit routes may underpin the existence of flexible COPII carriers in eukaryotes.…”

Section: Copii Vesicles In Er Export: Conventional Identities With Di...mentioning

confidence: 99%

COPII vesicles in plant autophagy and endomembrane trafficking

Zeng

Jiang

2022

FEBS Letters

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ER exit sites in Drosophila display abundant ER-Golgi vesicles and pearled tubes but no megacarriers

Cited by 24 publications

References 88 publications

Hanging the coat on a collar: Same function but different localization and mechanism for COPII

Hanging the coat on a collar: Same function but different localization and mechanism for COPII

Acute manipulation and real-time visualization of membrane trafficking and exocytosis inDrosophila

COPII vesicles in plant autophagy and endomembrane trafficking

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