COPI-dependent Golgi-to-ER retrograde traffic

Stable Identifier
R-HSA-6811434
Type
Pathway
Species
Homo sapiens
ReviewStatus
5/5
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Retrograde traffic from the cis-Golgi to the ERGIC or the ER is mediated in part by microtubule-directed COPI-coated vesicles (Letourneur et al, 1994; Shima et al, 1999; Spang et al, 1998; reviewed in Lord et al, 2013; Spang et al, 2013). These assemble at the cis side of the Golgi in a GBF-dependent fashion and are tethered at the ER by the ER-specific SNAREs and by the conserved NRZ multisubunit tethering complex, known as DSL in yeast (reviewed in Tagaya et al, 2014; Hong and Lev, 2014). Typical cargo of these retrograde vesicles includes 'escaped' ER chaperone proteins, which are recycled back to the ER for reuse by virtue of their interaction with the Golgi localized KDEL receptors (reviewed in Capitani and Sallese, 2009; Cancino et al, 2013).
Literature References
PubMed ID Title Journal Year
23873287 Regulation of Golgi signaling and trafficking by the KDEL receptor

Luini, A, Cancino, J, Jung, JE

Histochem. Cell Biol. 2013
10469566 Segregation of COPI-rich and anterograde-cargo-rich domains in endoplasmic-reticulum-to-Golgi transport complexes

Scales, SJ, Kreis, TE, Pepperkok, R, Shima, DT

Curr. Biol. 1999
24119662 Tethering the assembly of SNARE complexes

Hong, W, Lev, S

Trends Cell Biol. 2014
25364732 Moonlighting functions of the NRZ (mammalian Dsl1) complex

Tagaya, M, Kimura, H, Inoue, H, Arasaki, K

Front Cell Dev Biol 2014
23732476 Retrograde traffic from the Golgi to the endoplasmic reticulum

Spang, A

Cold Spring Harb Perspect Biol 2013
19854180 The KDEL receptor: new functions for an old protein

Capitani, M, Sallese, M

FEBS Lett. 2009
23378591 The highly conserved COPII coat complex sorts cargo from the endoplasmic reticulum and targets it to the golgi

Ferro-Novick, S, Miller, EA, Lord, C

Cold Spring Harb Perspect Biol 2013
9813082 Reconstitution of retrograde transport from the Golgi to the ER in vitro

Spang, A, Schekman, R

J. Cell Biol. 1998
8001155 Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum

Riezman, H, Hennecke, S, Emr, SD, Gaynor, EC, Letourneur, F, Cosson, P, Duden, R, Démollière, C

Cell 1994
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