{"id":1234,"date":"2016-02-17T09:02:55","date_gmt":"2016-02-17T09:02:55","guid":{"rendered":"http:\/\/blogs.kent.ac.uk\/biosciences\/?p=1234"},"modified":"2016-02-17T09:04:15","modified_gmt":"2016-02-17T09:04:15","slug":"research-seminar-redox-regulation-and-disulfide-formation-in-the-secretory-pathway","status":"publish","type":"post","link":"https:\/\/blogs.kent.ac.uk\/biosciences\/2016\/02\/17\/research-seminar-redox-regulation-and-disulfide-formation-in-the-secretory-pathway\/","title":{"rendered":"Research Seminar: Redox regulation and disulfide formation in the secretory pathway"},"content":{"rendered":"

Professor Neil Bulleid, Institute of Molecular, Cell & Systems Biology, University of Glasgow<\/strong><\/p>\n

Tuesday 23rd February, 1:00 p.m., Cornwallis Octagon Lecture Theatre 2 (COLT2)<\/strong><\/p>\n

 <\/p>\n

The folding and assembly of proteins within the endoplasmic reticulum (ER) is an essential process for normal healthy tissues. Breakdown in this process leads to several chronic diseases so it is critical that we have a better understanding of the molecular details of how cells fold proteins that enter the secretory pathway. Nearly a third of all proteins coded for by the human genome enter the secretory pathway and undergo disulfide formation during their folding. We know that members of the protein disulfide isomerase family catalyse disulfide formation but we know little about the function of each of the family members or how the unique redox environment of the ER is maintained. In this presentation I will review our current work to characterise the process of disulfide formation and in particular to determine how the ER ensures correct disulfide formation.<\/p>\n