Retrograde Transport of Golgi-localized Proteins to the ER

• DOI: 10.1083/jcb.140.1.1
• Publication Date: 2002-07-26T16:47:50Z
• Authors: Nelson B. Cole; Jan Ellenberg; Jia Song; Diane DiEuliis; Jennifer Lippinco...
• Keywords: Ectodomain; ER retention; Chaperone (clinical)

The ER is uniquely enriched in chaperones and folding enzymes that facilitate unfolding reactions ensure only correctly folded assembled proteins leave this compartment. Here we address the extent to which localize distal sites secretory pathway are able return environment during their lifetime. Retrieval of back was studied using an assay based on capacity retain misfolded proteins. lumenal domain temperature-sensitive viral glycoprotein VSVGtsO45 fused Golgi or plasma membrane targeting domains. At nonpermissive temperature, newly synthesized fusion were retained ER, indicating ectodomain sufficient for retention within ER. permissive delivered complex membrane, epitope also did not interfere with proper these molecules. Strikingly, Golgi-localized proteins, but itself, found redistribute upon a shift where they retained. This occurred over time period 15 min-2 h depending chimera, require new protein synthesis. Significantly, recycling appear be induced by misfolding chimeras complex. suggested normally cycle between while passing through at 40 degrees C become attachment thermosensitive promises useful tool studying molecular mechanisms specificity retrograde traffic