Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz
Gewählte Publikation:
SHR Neuro Krebs Kardio Lipid Stoffw Microb
Yu, S; Satoh, A; Pypaert, M; Mullen, K; Hay, JC; Ferro-Novick, S.
mBet3p is required for homotypic COPII vesicle tethering in mammalian cells.
J Cell Biol. 2006; 174(3):359-368
Doi: 10.1083/jcb.200603044
[OPEN ACCESS]
Web of Science
PubMed
FullText
FullText_MUG
- Co-Autor*innen der Med Uni Graz
- Hay Jesse
- Altmetrics:
- Dimensions Citations:
- Plum Analytics:
- Scite (citation analytics):
- Abstract:
- TRAPPI is a large complex that mediates the tethering of COPII vesicles to the Golgi (heterotypic tethering) in the yeast Saccharomyces cerevisiae. In mammalian cells, COPII vesicles derived from the transitional endoplasmic reticulum (tER) do not tether directly to the Golgi, instead, they appear to tether to each other (homotypic tethering) to form vesicular tubular clusters (VTCs). We show that mammalian Bet3p (mBet3p), which is the most highly conserved TRAPP subunit, resides on the tER and adjacent VTCs. The inactivation of mBet3p results in the accumulation of cargo in membranes that colocalize with the COPII coat. Furthermore, using an assay that reconstitutes VTC biogenesis in vitro, we demonstrate that mBet3p is required for the tethering and fusion of COPII vesicles to each other. Consistent with the proposal that mBet3p is required for VTC biogenesis, we find that ERGIC-53 (VTC marker) and Golgi architecture are disrupted in siRNA-treated mBet3p-depleted cells. These findings imply that the TRAPPI complex is essential for VTC biogenesis.
- Find related publications in this database (using NLM MeSH Indexing)
- Animals -
- Brefeldin A - pharmacology
- COP-Coated Vesicles - metabolism
- COS Cells -
- Carrier Proteins - metabolism
- Cercopithecus aethiops -
- Endoplasmic Reticulum - ultrastructure
- Golgi Apparatus - ultrastructure
- HeLa Cells -
- Humans -
- Protein Transport - drug effects
- Vesicular Transport Proteins - metabolism