{"id":390,"date":"2013-11-05T09:08:26","date_gmt":"2013-11-05T09:08:26","guid":{"rendered":"http:\/\/blogs.kent.ac.uk\/biosciences\/?p=390"},"modified":"2013-11-05T09:08:26","modified_gmt":"2013-11-05T09:08:26","slug":"research-seminar-protein-folding-and-misfolding-in-the-secretory-pathway","status":"publish","type":"post","link":"https:\/\/blogs.kent.ac.uk\/biosciences\/2013\/11\/05\/research-seminar-protein-folding-and-misfolding-in-the-secretory-pathway\/","title":{"rendered":"Research Seminar: Protein folding and misfolding in the secretory pathway."},"content":{"rendered":"

Dr. Lisa Swanton<\/strong>
\nFaculty of Life Sciences, University of Manchester<\/strong><\/p>\n

Monday 11th November, 4.00 p.m., Jennison Lecture Theatre<\/strong><\/p>\n

Misfolded proteins represent a continuous threat to cell viability, which if allowed to accumulate, can disrupt cellular function and induce cell death. Therefore, cells possess elaborate quality control systems that survey the proteome in order to identify and eliminate non-native polypeptides. Integral membrane proteins such as ion channels and receptors present a particular challenge to these systems since they may have domains in three distinct subcellular locations; the cytosol, the extracellular surface\/organelle interior, and within the lipid bilayer. Most membrane proteins are synthesised at the endoplasmic reticulum (ER) before being trafficked along the secretory pathway to their final destination, and although much is now known about the quality control machinery that monitors folding of domains in the cysotol and within the lumen of the ER, very little is known about how membrane spanning domains are scrutinised. In this talk, I will describe our recent work aimed at defining the pathways that detect and dispose of proteins possessing non-native transmembrane domains.<\/p>\n

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