Feyza Engin

Biomolecular Chemistry Department

Endoplasmic reticulum stress, organelle dysfunction, unfolded protein response, beta cell function and diabetes

fengin@wisc.edu

6260 Biochemistry Building
420 Henry Mall
Madison, WI 53706

Headshot

lab website:

https://bmolchem.wisc.edu/staff/engin-feyza/

focus groups:

Cellular & Molecular Metabolism; Transcriptional Mechanisms; Developmental Biology and Regenerative Medicine

research description:

Type 1 diabetes (T1D) results from the destruction of the insulin-secreting b-cells. Endoplasmic reticulum (ER) stress, caused by protein misfolding, chronic inflammation and environmental factors, is emerging as a novel concept for diabetes pathogenesis. To cope with ER stress, the Unfolded Protein Response (UPR), a signaling cascade mediated by ER membrane-localized sensors ATF6, IRE1 and PERK, is triggered to re-establish cellular homeostasis. ER stress and aberrant UPR have been shown to play a role in the pathogenesis of inflammatory and including type 2 diabetes and atherosclerosis. However, the role of ER stress and the UPR in pathophysiology of T1D remains incompletely defined. Our lab is interested in understanding the role of organelle dysfunction and cellular stress responses in pancreatic beta cell pathophysiology and diabetes. We have developed unique tissue specific transgenic mouse models to identify the previously unknown functions of endoplasmic reticulum stress and unfolded protein response in type 1 diabetes Our ultimate goal is by using these unique tools and cutting edge methods to prevent and ultimately cure metabolic and autoimmune disorders.

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