Abstract
The GTPase Rab1 regulates endoplasmic reticulum-Golgi and early Golgi traffic. The guanine nucleotide exchange factor (GEF) or factors that activate Rab1 at these stages of the secretory pathway are currently unknown. Trs130p is a subunit of the yeast TRAPPII (transport protein particle II) complex, a multisubunit tethering complex that is a GEF for the Rab1 homologue Ypt1p. Here, we show that mammalian Trs130 (mTrs130) is a component of an analogous TRAPP complex in mammalian cells, and we describe for the first time the role that this complex plays in membrane traffic. mTRAPPII is enriched on COPI (Coat Protein I)-coated vesicles and buds, but not Golgi cisternae, and it specifically activates Rab1. In addition, we find that mTRAPPII binds to γ1COP, a COPI coat adaptor subunit. The depletion of mTrs130 by short hairpin RNA leads to an increase of vesicles in the vicinity of the Golgi and the accumulation of cargo in an early Golgi compartment. We propose that mTRAPPII is a Rab1 GEF that tethers COPI-coated vesicles to early Golgi membranes.
| Original language | English |
|---|---|
| Pages (from-to) | 4205-4215 |
| Number of pages | 11 |
| Journal | Molecular Biology of the Cell |
| Volume | 20 |
| Issue number | 19 |
| DOIs | |
| Publication status | Published - Oct 1 2009 |
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ASJC Scopus subject areas
- Molecular Biology
- Cell Biology
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mTrs130 is a component of a mammalian TRAPPII complex, a Rab1 GEF that binds to COPI-coated vesicles. / Yamasaki, Akinori; Menon, Shekar; Yu, Sidney; Barrowman, Jemima; Meerloo, Timo; Oorschot, Viola; Klumperman, Judith; Satoh, Ayano; Ferro-Novick, Susan.
In: Molecular Biology of the Cell, Vol. 20, No. 19, 01.10.2009, p. 4205-4215.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - mTrs130 is a component of a mammalian TRAPPII complex, a Rab1 GEF that binds to COPI-coated vesicles
AU - Yamasaki, Akinori
AU - Menon, Shekar
AU - Yu, Sidney
AU - Barrowman, Jemima
AU - Meerloo, Timo
AU - Oorschot, Viola
AU - Klumperman, Judith
AU - Satoh, Ayano
AU - Ferro-Novick, Susan
PY - 2009/10/1
Y1 - 2009/10/1
N2 - The GTPase Rab1 regulates endoplasmic reticulum-Golgi and early Golgi traffic. The guanine nucleotide exchange factor (GEF) or factors that activate Rab1 at these stages of the secretory pathway are currently unknown. Trs130p is a subunit of the yeast TRAPPII (transport protein particle II) complex, a multisubunit tethering complex that is a GEF for the Rab1 homologue Ypt1p. Here, we show that mammalian Trs130 (mTrs130) is a component of an analogous TRAPP complex in mammalian cells, and we describe for the first time the role that this complex plays in membrane traffic. mTRAPPII is enriched on COPI (Coat Protein I)-coated vesicles and buds, but not Golgi cisternae, and it specifically activates Rab1. In addition, we find that mTRAPPII binds to γ1COP, a COPI coat adaptor subunit. The depletion of mTrs130 by short hairpin RNA leads to an increase of vesicles in the vicinity of the Golgi and the accumulation of cargo in an early Golgi compartment. We propose that mTRAPPII is a Rab1 GEF that tethers COPI-coated vesicles to early Golgi membranes.
AB - The GTPase Rab1 regulates endoplasmic reticulum-Golgi and early Golgi traffic. The guanine nucleotide exchange factor (GEF) or factors that activate Rab1 at these stages of the secretory pathway are currently unknown. Trs130p is a subunit of the yeast TRAPPII (transport protein particle II) complex, a multisubunit tethering complex that is a GEF for the Rab1 homologue Ypt1p. Here, we show that mammalian Trs130 (mTrs130) is a component of an analogous TRAPP complex in mammalian cells, and we describe for the first time the role that this complex plays in membrane traffic. mTRAPPII is enriched on COPI (Coat Protein I)-coated vesicles and buds, but not Golgi cisternae, and it specifically activates Rab1. In addition, we find that mTRAPPII binds to γ1COP, a COPI coat adaptor subunit. The depletion of mTrs130 by short hairpin RNA leads to an increase of vesicles in the vicinity of the Golgi and the accumulation of cargo in an early Golgi compartment. We propose that mTRAPPII is a Rab1 GEF that tethers COPI-coated vesicles to early Golgi membranes.
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UR - http://www.scopus.com/inward/citedby.url?scp=70350115572&partnerID=8YFLogxK
U2 - 10.1091/mbc.E09-05-0387
DO - 10.1091/mbc.E09-05-0387
M3 - Article
C2 - 19656848
AN - SCOPUS:70350115572
VL - 20
SP - 4205
EP - 4215
JO - Molecular Biology of the Cell
JF - Molecular Biology of the Cell
SN - 1059-1524
IS - 19
ER -