Proteomic Profiling of Mammalian COPII and COPI Vesicles

Adolf, Frank; Rhiel, Manuel; Heßling, Bernd; Gao, Qi; Hellwig, Andrea; Béthune, Julien; Wieland, Felix

doi:10.1016/j.celrep.2018.12.041

Cited by 86 publications

(122 citation statements)

References 76 publications

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“…In mammals and Arabidopsis, it has been proposed that different isoforms may be part of alternative coatomer complexes with different localization and perhaps different functions (Wegmann et al, 2004;Donohoe et al, 2007;Moelleken et al, 2007;Popoff et al, 2011;Gao et al, 2014). However, it has been recently reported that all of the isoforms of the mammalian COPI coat produce COPI-coated vesicles with strikingly similar protein compositions (Adolf et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

Loss of Arabidopsis β-COP Function Affects Golgi Structure, Plant Growth and Tolerance to Salt Stress

et al. 2020

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The early secretory pathway involves bidirectional transport between the endoplasmic reticulum (ER) and the Golgi apparatus and is mediated by coat protein complex I (COPI)-coated and coat protein complex II (COPII)-coated vesicles. COPII vesicles are involved in ER to Golgi transport meanwhile COPI vesicles mediate intra-Golgi transport and retrograde transport from the Golgi apparatus to the ER. The key component of COPI vesicles is the coatomer complex, that is composed of seven subunits (α/β/β'/γ/δ/ε/ζ). In Arabidopsis two genes coding for the β-COP subunit have been identified, which are the result of recent tandem duplication. Here we have used a lossof-function approach to study the function of β-COP. The results we have obtained suggest that β-COP is required for plant growth and salt tolerance. In addition, β-COP function seems to be required for maintaining the structure of the Golgi apparatus.

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Section: Introductionmentioning

confidence: 99%

Loss of Arabidopsis β-COP Function Affects Golgi Structure, Plant Growth and Tolerance to Salt Stress

et al. 2020

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“…In these examples, the outcome of the mutations or treatment is a virtually complete block of ER/Golgi trafficking. This is however not expected in the absence of g1-COP, especially with the concomitant overexpression of g2-COP, as g1-COP-depleted cells are viable and g2-COPcontaining coatomer is as efficient in forming COPI vesicles as g1-COPcontaining coatomer in vitro 5,41 . One possibility is that g1-COP acts as a specific cargo receptor for proteins that are important for neuronal polarization.…”

Section: Discussionmentioning

confidence: 96%

“…This suggests that g-COP paralogs help maintaining protein concentration gradients across the Golgi stack, with g1-COP being more active at the ER/cis-Golgi interface. Proteomic analysis of COPI vesicles generated from various cell lines revealed that they mainly contain membrane trafficking regulating proteins, such as SNAREs (SNAP [soluble NSF attachment protein] receptor), and glycosylation enzymes 5 . The absence of one g-COP paralog may then affect the distribution or trafficking kinetics of such proteins across the Golgi, which might explain the phenotype of Copg1 KO cells.…”

Section: Discussionmentioning

confidence: 99%

“…In mammals, two coatomer subunits come as two paralogs: g1-COP and g2-COP that share 80% protein sequence identity and that are encoded by the Copg1 and Copg2 genes 3 , and z1-COP and z2-COP encoded by the Copz1 and Copz2 genes 4 . In the COPII system, paralogs of the SEC24 subunit expand the cargo repertoire of COPII vesicles by providing distinct binding sites for specific sorting motifs 5,6,7,8,9 . By contrast, proteomics profiling of paralog-specific COPI vesicles generated in vitro from HeLa cells revealed no major difference in their cargo content 5 and to date no specialized function has been ascribed to the paralogous COP subunits, which until now have thus been considered as functionally redundant.…”

Section: Introductionmentioning

confidence: 99%

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A paralog-specific role of the COPI pathway in the neuronal differentiation of murine pluripotent cells

Goyal

Zhao

Bozhinova

et al. 2020

Preprint

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Coat protein complex I (COPI)-coated vesicles mediate membrane trafficking between Golgi cisternae as well as retrieval of proteins from the Golgi to the endoplasmic reticulum. There are several flavors of the COPI coat defined by paralogous subunits of the protein complex coatomer. However, whether paralogous COPI proteins have specific functions is currently unknown. Here we show that the paralogous coatomer subunits g1-COP and g2-COP are differentially expressed during the neuronal differentiation of mouse pluripotent cells. Moreover, through a combination of genome editing experiments, we demonstrate that whereas g-COP paralogs are largely functionally redundant, g1-COP specifically promotes neurite outgrowth. Our work stresses a role of the COPI pathway in neuronal polarization and provides evidence for distinct functions for coatomer paralogous subunits in this process.

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“…There has been recent interest in quantifying the ab-solute numbers of proteins associated with intracellular vesicles. Proteomic estimates of protein composition have been obtained for COPII and COPI vesicles (Adolf et al, 2019), AP-1/clathrin-coated vesicles (Hirst et al, 2015) and for synaptic vesicles (Takamori et al, 2006;Wilhelm et al, 2014). In the latter two cases these data were used to build 3D models of an average vesicle which contains cargo.…”

Section: Introductionmentioning

confidence: 99%

Calculating the maximum capacity of intracellular transport vesicles

Em¹,

Royle²

2019

Preprint

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In eukaryotic cells, vesicles transport protein cargo to various destinations in the cell. As part of an effort to count the number of cargo molecules in vesicles in cells, we asked a simple question: what is the maximum number of cargo molecules that can be packed into a vesicle? The answer to this question lies in the Tammes Problem, which seeks to determine the packing of circles on a spherical surface. The solution to this problem depends on the sizes of the vesicle and the cargo. We present here the computational results that determine the maximum theoretical capacity of a range of biologically relevant cargo in a variety of meaningful vesicle sizes. Our results could be generalized in order to describe an equation that allows the calculation of the approximate maximum capacity of any vesicle, whatever the size; provided that the size and geometry of the cargo is known. vesicle transport | spherical packing | Tammes Problem | cargo proteins | clathrin-coated vesicleCorrespondence: E.Martins-Ratamero.1@warwick.ac.uk s.j.royle@warwick.ac.uk

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Proteomic Profiling of Mammalian COPII and COPI Vesicles

Cited by 86 publications

References 76 publications

Loss of Arabidopsis β-COP Function Affects Golgi Structure, Plant Growth and Tolerance to Salt Stress

Loss of Arabidopsis β-COP Function Affects Golgi Structure, Plant Growth and Tolerance to Salt Stress

A paralog-specific role of the COPI pathway in the neuronal differentiation of murine pluripotent cells

Calculating the maximum capacity of intracellular transport vesicles

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