Abstract
The endoplasmic reticulum (ER) is the entry point for most proteins residing and functioning in the eukaryotic endomembrane system. The primary mechanism by which proteins enter the ER is via the translocon complex. Dysfunction in this complex can block access into the ER, which is detrimental to cellular health. The translocon is highly conserved and has been intensely studied in Saccharomyces cerevisiae. Analysis of translocon function in protein trafficking, localization, and interactions in yeast has been facilitated by the use of epitope tags. We have found that a tag on the translocon pore subunit previously suggested not to impair translocon function subtly affects translocation of proteins into the ER in yeast cells. Intriguingly, this tag also suppresses a phenotype associated with defective protein quality control pathways, consistent with a functional link between translocation and quality control. Ongoing work includes characterizing the effects of placing different epitope tags on different translocon subunits, with the goal of identifying tags that affect translocon function the least.Support or Funding InformationThis work was supported by Ball State University ASPiRE research awards to AR and MD, a Ball State University Faculty Advance research award to ER, an Indiana Academy of Science Senior Research Grant to ER, and an NIH grant to ER (GM111713).
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