Quantitative Biology Seminar
|Monday, January 14, 2019: 335 West Hall, 12:00p - 1:00p
|Presenter||Wylie Stroberg, PhD., Department of Molecular and Integrative Physiology, University of Michigan|
||Stress sensing in the endoplasmic reticulum|
||Within the endoplasmic reticulum (ER) of eukaryotic cells a complex system of chaperones and foldases work
in concert to correctly fold nascent proteins and aid their progress along the secretory pathway. Should this process
be upset, either through increased peptide translation or changes to the chemical environment within the ER, unfolded
proteins accumulate, aggregate and misfold. This state of disrupted proteostasis, known as ER stress, triggers a multifaceted
transcriptional response called the unfolded protein response (UPR) that seeks to restore proteostasis. While the UPR
has been extensively studied due to the important role it plays in protein misfolding diseases, cancer and aging, a
critical and still-poorly-understood aspect of the UPR is the mechanism through which ER stress is detected and quantified
by the cell. This talk will discuss recent theoretical work to rationalize the observed stress sensing network in the ER.
Specifically, by approaching the problem from both optimal-control and information-theoretic standpoints, we show the advantage
of measuring stress by “counting” both unfolded proteins and unutilized chaperones as opposed to either individually.
This work serves as a starting point for a more quantitative understanding of how cells regulate ER stress and the protein
|More information||Quantitative Biology Seminars|