The calcium‐binding protein ALG‐2 promotes endoplasmic reticulum exit site localization and polymerization of Trk‐fused gene (TFG) protein

Kanadome, Takashi; Shibata, Hideki; Kuwata, Keiko; Takahara, Taishi; Maki, Masatoshi

doi:10.1111/febs.13949

Cited by 29 publications

(23 citation statements)

References 49 publications

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“…Strikingly, in the absence of COPII carrier formation, TFG fails to accumulate near ER subdomains, suggesting that the presence of COPII‐coated transport carriers is a prerequisite for concentrated assembly of TFG in cells . Beyond binding to Sec23 and tethering COPII carriers, TFG has also been shown to interact with ALG‐2 in a calcium‐dependent manner . in vitro studies suggest that this association may enhance co‐assembly of TFG octamers into larger complexes.…”

Section: Regulation Of Copii Coat Disassembly At the Er/ergic Interfacementioning

confidence: 99%

“…in vitro studies suggest that this association may enhance co‐assembly of TFG octamers into larger complexes. However, depletion of ALG‐2 has minimal impact on the levels of TFG at the ER/ERGIC interface . Further work is necessary to define the mechanistic basis for TFG assembly in the early secretory pathway and how this process is regulated.…”

Section: Regulation Of Copii Coat Disassembly At the Er/ergic Interfacementioning

confidence: 99%

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COPII‐mediated trafficking at the ER/ERGIC interface

Peotter

Kasberg

Pustova

et al. 2019

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Coat proteins play multiple roles in the life cycle of a membrane-bound transport intermediate, functioning in lipid bilayer remodeling, cargo selection and targeting to an acceptor compartment. The Coat Protein complex II (COPII) coat is known to act in each of these capacities, but recent work highlights the necessity for numerous accessory factors at all stages of transport carrier existence. Here, we review recent findings that highlight the roles of COPII and its regulators in the biogenesis of tubular COPII-coated carriers in mammalian cells that enable cargo transport between the endoplasmic reticulum and ER-Golgi intermediate compartments, the first step in a series of trafficking events that ultimately allows for the distribution of biosynthetic secretory cargoes throughout the entire endomembrane system. K E Y W O R D S COPII coat, early secretory pathway, endoplasmic reticulum, ER exit site, posttranslational modification, Sec16A, Tango1/cTAGE5, TFG

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Section: Regulation Of Copii Coat Disassembly At the Er/ergic Interfacementioning

confidence: 99%

Section: Regulation Of Copii Coat Disassembly At the Er/ergic Interfacementioning

confidence: 99%

COPII‐mediated trafficking at the ER/ERGIC interface

Peotter

Kasberg

Pustova

et al. 2019

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109

110

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“…PEF1 was also shown to modulate COPII kinetics in yeast (Yoshibori et al 2012). Intriguingly, ALG-2 is required for the localization and assembly of TFG [(Kanadome et al 2017), Fig. 3A].…”

Section: Flexibility Of the Copii Coat: The Case For Large Copii-depementioning

confidence: 99%

COPII-dependent ER export in animal cells: adaptation and control for diverse cargo

McCaughey

Stephens

2018

Histochem Cell Biol

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The export of newly synthesized proteins from the endoplasmic reticulum is fundamental to the ongoing maintenance of cell and tissue structure and function. After co-translational translocation into the ER, proteins destined for downstream intracellular compartments or secretion from the cell are sorted and packaged into transport vesicles by the COPII coat protein complex. The fundamental discovery and characterization of the pathway has now been augmented by a greater understanding of the role of COPII in diverse aspects of cell function. We now have a deep understanding of how COPII contributes to the trafficking of diverse cargoes including extracellular matrix molecules, developmental signalling proteins, and key metabolic factors such as lipoproteins. Structural and functional studies have shown that the COPII coat is both highly flexible and subject to multiple modes of regulation. This has led to new discoveries defining roles of COPII in development, autophagy, and tissue organization. Many of these newly emerging features of the canonical COPII pathway are placed in a context of procollagen secretion because of the fundamental interest in how a coat complex that typically generates 80-nm transport vesicles can package a cargo reported to be over 300 nm. Here we review the current understanding of COPII and assess the current consensus on its role in packaging diverse cargo proteins.

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“…For instance, ALG-2 binds to both ALIX and TSG101, an ESCRT-I protein (22,23), or binds to both Sec31A and annexin A11 to regulate ER-to-Golgi transport (16). ALG-2 also binds to Trk-fused gene (TFG) molecules to promote TFG polymerization by its adaptor function (24).…”

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confidence: 99%

The calcium-binding protein ALG-2 regulates protein secretion and trafficking via interactions with MISSL and MAP1B proteins

Takahara¹,

Inoue²,

Arai³

et al. 2017

Journal of Biological Chemistry

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Mobilization of intracellular calcium is essential for a wide range of cellular processes, including signal transduction, apoptosis, and vesicular trafficking. Several lines of evidence have suggested that apoptosis-linked gene 2 (ALG-2, also known as ), a calcium-binding protein, acts as a calcium sensor linking calcium levels with efficient vesicular trafficking, especially at the endoplasmic reticulum (ER)-to-Golgi transport step. However, how ALG-2 regulates these processes remains largely unclear. Here, we report thatAPK1-nteracting and pindle-tabilizing (MISS)-ike (MISSL), a previously uncharacterized protein, interacts with ALG-2 in a calcium-dependent manner. Live-cell imaging revealed that upon a rise in intracellular calcium levels, GFP-tagged MISSL (GFP-MISSL) dynamically relocalizes in a punctate pattern and colocalizes with ALG-2. MISSL knockdown caused disorganization of the components of the ER exit site, the ER-Golgi intermediate compartment, and Golgi. Importantly, knockdown of either MISSL or ALG-2 attenuated the secretion of cretedlkaline hosphatase (SEAP), a model secreted cargo protein, with similar reductions in secretion by single- and double-protein knockdowns, suggesting that MISSL and ALG-2 act in the same pathway to regulate the secretion process. Furthermore, ALG-2 or MISSL knockdown delayed ER-to-Golgi transport of procollagen type I. We also found that ALG-2 and MISSL interact with microtubule-associated protein 1B (MAP1B) and that MAP1B knockdown reverts the reduced secretion of SEAP caused by MISSL or ALG-2 depletion. These results suggest that a change in the intracellular calcium level plays a role in regulation of the secretory pathway via interaction of ALG-2 with MISSL and MAP1B.

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The calcium‐binding protein ALG‐2 promotes endoplasmic reticulum exit site localization and polymerization of Trk‐fused gene (TFG) protein

Cited by 29 publications

References 49 publications

COPII‐mediated trafficking at the ER/ERGIC interface

COPII‐mediated trafficking at the ER/ERGIC interface

COPII-dependent ER export in animal cells: adaptation and control for diverse cargo

The calcium-binding protein ALG-2 regulates protein secretion and trafficking via interactions with MISSL and MAP1B proteins

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