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Journal Article

ER arrival sites for COPI vesicles localize to hotspots of membrane trafficking.

MPS-Authors
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Schröter,  S.
Research Group of Membrane Transport in Yeast, MPI for Biophysical Chemistry, Max Planck Society;

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Beckmann,  S.
Research Group of Membrane Transport in Yeast, MPI for Biophysical Chemistry, Max Planck Society;

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Schmitt,  H. D.
Research Group of Membrane Transport in Yeast, MPI for Biophysical Chemistry, Max Planck Society;

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2321030_Suppl_1.pdf
(Supplementary material), 4MB

2321030_Suppl_2.pdf
(Supplementary material), 2MB

2321030_Suppl_3.zip
(Supplementary material), 414KB

2321030_Suppl_4.zip
(Supplementary material), 205KB

2321030_Suppl_5.zip
(Supplementary material), 540KB

2321030_Suppl_6.zip
(Supplementary material), 129KB

Citation

Schröter, S., Beckmann, S., & Schmitt, H. D. (2016). ER arrival sites for COPI vesicles localize to hotspots of membrane trafficking. EMBO Journal, 35(17), 1935-1955. doi:10.15252/embj.201592873.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002B-0C0D-1
Abstract
COPI-coated vesicles mediate retrograde membrane traffic from the cis-Golgi to the endoplasmic reticulum (ER) in all eukaryotic cells. However, it is still unknown whether COPI vesicles fuse everywhere or at specific sites with the ER membrane. Taking advantage of the circumstance that the vesicles still carry their coat when they arrive at the ER, we have visualized active ER arrival sites (ERAS) by monitoring contact between COPI coat components and the ER-resident Dsl tethering complex using bimolecular fluorescence complementation (BiFC). ERAS form punctate structures near Golgi compartments, clearly distinct from ER exit sites. Furthermore, ERAS are highly polarized in an actin and myosin V-dependent manner and are localized near hotspots of plasma membrane expansion. Genetic experiments suggest that the COPI•Dsl BiFC complexes recapitulate the physiological interaction between COPI and the Dsl complex and that COPI vesicles are mistargeted in dsl1 mutants. We conclude that the Dsl complex functions in confining COPI vesicle fusion sites.