Members of a mammalian SNARE complex interact in the endoplasmic reticulum in vivo and are found in COPI vesicles
| Autor: | Gabriele Fischer von Mollard, Matthias Willmann, Sophie E. Verrier, Hans-Dieter Söling, Ulrike Winter, Dirk Wenzel |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2008 |
| Předmět: |
Histology
SNARE proteins KDEL Vesicular Transport Proteins Golgi Apparatus Syntaxin 18 Live-cell FRET Golgi-to-ER transport Endoplasmic Reticulum Pathology and Forensic Medicine Mice symbols.namesake KDEL receptor Usel Chlorocebus aethiops Fluorescence Resonance Energy Transfer Animals Qc-SNARE Proteins Vero Cells Qa-SNARE Proteins Chemistry Vesicular-tubular cluster Endoplasmic reticulum USE1 Biological Transport Sec20 Cell Biology General Medicine COPI COP-Coated Vesicles Golgi apparatus COPI vesicles Rats Cell biology Proto-Oncogene Proteins c-bcl-2 symbols SNARE complex |
| Zdroj: | European Journal of Cell Biology |
| DOI: | 10.1016/j.ejcb.2008.07.003 |
| Popis: | Retrograde traffic between the Golgi apparatus and the endoplasmic reticulum (ER) is largely mediated by COPI-coated transport vesicles. In mammalian cells, retrograde traffic can pass through an intermediate compartment. Here, we report that the mammalian soluble N-ethylmaleimide-sensitive factor (NSF) attachment receptor (SNARE) proteins mSec22b, mUse1/D12, mSec20/BNIP1, and syntaxin 18 form a quaternary SNARE complex. Fluorescence resonance energy transfer (FRET) experiments prove that these interactions occur in the ER of living cells. In addition, mUse1/D12 and mSec20/BNIP1 form homo-oligomers in vivo. Furthermore, we show that rnSec22b, mUse1/D12, mSec20/BNIP1, and syntaxin 18 are recruited into COPI-coated vesicles formed in vitro. Immunogold electron microscopy confirmed that these SNARE proteins colocalize with the KDEL receptor ERD2 in COPI-coated vesicles. Moreover, both FRET and immunoprecipitation experiments reveal interactions of these SNAREs with both ERD2 and COPI subunits. We conclude that the SNAREs described here are sorted via interaction with components of the COPI-dependent budding complex into Golgi-to-ER retrograde COPI vesicles and function in retrograde transport from the Golgi to the ER Golgi intermediate compartment (ERGIC) or the ER. (C) 2008 Elsevier GmbH. All rights reserved. |
| Databáze: | OpenAIRE |
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