Emr. 1997. COPI-independent anterograde transport: cargo-selective ER to Golgi protein transport in yeast COPI mutants. J. Cell Biol. 136:789-802.Gaynor, E. C. and S. D. Emr 1997 COPI-independent anterograde transport: Cargo-selective ER to Golgi transport in yeast COPI mutants . J. ...
We next investigated the association of WFS1 with the COPII complex, the coatomer of vesicles involved in ER-to-Golgi anterograde trafficking25. COPII interacts with the cargo receptors via its SEC24 subunits, which recognize the specific cytosolic ER export signals within the protein sequence of t...
Anterograde and retrograde transport is mediated by distinct sets of cytosolic coat proteins, the COPII and COPI coats, respectively, which act on the membrane to capture cargo proteins into nascent vesicles. We review the mechanisms that govern coat recruitment to the membrane, cargo capture into ...
Overexpression and depletion studies indicate that WHAMM is important for maintaining Golgi structure and facilitating anterograde membrane transport. The ability of WHAMM to interact with microtubules plays a role in membrane tubulation, while its capacity to induce actin assembly promotes tubule ...
of anterograde carriers from stationary ERGIC-53-positive membranes, however, suggest a stable compartment model in which ER-derived cargo is first shuttled from ER-exit sites to stationary ERGIC clusters in a COPII-dependent step and subsequently to the Golgi in a second vesicular transport step....
Sec23a has crucial roles in coat protein complex II (COPII) vesicle formation and anterograde transport from the ER to the Golgi. During chondrocyte differentiation, mild ER stress occurs and activates BBF2H7. The phenotypes of Oasis–/– and Bbf2h7–/– mice indicate the possibility that a ...
Facing ERES, we find a pre-cis-Golgi region, equivalent to the vertebrate ER-Golgi intermediate compartment (ERGIC), involved in both anterograde and retrograde transport. This pre-cis-Golgi is continuous with the rest of the Golgi, not a separate compartment or collection of large carriers, ...
Introduction Endoplasmic reticulum export sites (ERES) are specific domains on the ER surface where cargo proteins, both soluble and membrane-bound, exit the ER in transit to the cis-side of the Golgi apparatus for processing and secretion. In mammalian
The endoplasmic reticulum (ER) is the starting site of the journey of newly synthesized proteinsto the apoplast, plasma membrane and to the vacuolar compartments. Transport between these membranecompartments of the secretory pathway in eukaryotic cells i
et al. Post-Golgi anterograde transport requires GARP-dependent endosome-to-TGN retrograde transport. Mol. Biol. Cell 26, 3071–3084 (2015). Article PubMed PubMed Central CAS Google Scholar Haeussler, M. et al. Evaluation of off-target and on-target scoring algorithms and integration into ...