COPII-dependent ER export in animal cells: adaptation and control for diverse cargo
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TLDR
The current understanding of COPII is reviewed and the current consensus on its role in packaging diverse cargo proteins is assessed, reported to be over 300 nm.Abstract:
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.read more
Citations
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Proteomic Profiling of Mammalian COPII and COPI Vesicles
Frank Adolf,Manuel Rhiel,Bernd Hessling,Qi Gao,Andrea Hellwig,Julien Béthune,Felix T. Wieland +6 more
TL;DR: The core proteomes of mammalian COPII and COPI vesicles are described and it is shown that all of the isoforms of the COPI coat produce COPI-coated vesicle with strikingly similar protein compositions.
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Membrane trafficking in health and disease.
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ER-to-Golgi Transport: A Sizeable Problem
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Tango1 coordinates the formation of endoplasmic reticulum/Golgi docking sites to mediate secretory granule formation
TL;DR: The results provide evidence that Tango1 organizes an interaction site where secretory cargo is efficiently transferred from the ER to Golgi and then to secretory vesicles, and may explain how the loss of Tango 1 can influence Golgi/ER morphology and affect the secretion of diverse proteins across many tissues.
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Multiple roles for actin in secretory and endocytic pathways
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References
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Journal ArticleDOI
COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum.
Charles Barlowe,Lelio Orci,Tom Yeung,Midori Hosobuchi,Susan Hamamoto,Nina R. Salama,M F Rexach,Mariella Ravazzola,Mylène Amherdt,Randy Schekman +9 more
TL;DR: In vitro synthesis of endoplasmic reticulum-derived transport vesicles has been reconstituted with washed membranes and three soluble proteins and it is proposed that the coat structures be called COPI and COPII.
Journal ArticleDOI
COPII-Coated Vesicle Formation Reconstituted with Purified Coat Proteins and Chemically Defined Liposomes
Ken Matsuoka,Lelio Orci,Mylène Amherdt,Sebastian Y. Bednarek,Susan Hamamoto,Randy Schekman,Thomas Yeung +6 more
TL;DR: Observations suggest that the assembly of the COPII coat on the ER occurs by a sequential binding of coat proteins to specific lipids and that this assembly promotes the budding of COPII-coated vesicles.
Journal ArticleDOI
Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles.
Elizabeth A. Miller,Traude H. Beilharz,Per Malkus,Marcus C. S. Lee,Susan Hamamoto,Lelio Orci,Randy Schekman +6 more
TL;DR: The mechanisms of cargo selection into ER-derived vesicles by the COPII subunit Sec24p are characterized and a model wherebySec24p proteins contain multiple independent cargo binding domains that allow for recognition of a diverse set of sorting signals is supported.
Journal ArticleDOI
The ER-Golgi intermediate compartment (ERGIC): in search of its identity and function
TL;DR: A stable compartment model in which ER-derived cargo is first shuttled from ER-exit sites to stationary ERGIC clusters in a COPII-dependent step and subsequently to the Golgi in a second vesicular transport step can better accommodate previous morphological and functional data on ER-to-Golgi traffic.
Journal ArticleDOI
Observing the cell in its native state: Imaging subcellular dynamics in multicellular organisms
Tsung-Li Liu,Srigokul Upadhyayula,Daniel E. Milkie,Ved P. Singh,Kai Wang,Ian A. Swinburne,Kishore R. Mosaliganti,Zach M. Collins,Tom W. Hiscock,Jamien Shea,Abraham Q. Kohrman,Taylor N Medwig,Daphné Dambournet,Ryan Forster,Brian Cunniff,Brian Cunniff,Yuan Ruan,Hanako Yashiro,Steffen Scholpp,Steffen Scholpp,Elliot M. Meyerowitz,Dirk Hockemeyer,David G. Drubin,Benjamin L. Martin,David Q. Matus,Minoru Koyama,Sean G. Megason,Tom Kirchhausen,Eric Betzig +28 more
TL;DR: AO-LLSM takes high-resolution live-cell imaging of subcellular processes from the confines of the coverslip to the more physiologically relevant 3D environment within whole transparent organisms and creates new opportunities to study the phenotypic diversity of intracellular dynamics, extracellular communication, and collective cell behavior across different cell types, organisms, and developmental stages.
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