TY - CHAP
T1 - Animal models in the study of the unfolded protein response
AU - Bommiasamy, Hemamalini
AU - Popko, Brian
PY - 2011
Y1 - 2011
N2 - The endoplasmic reticulum, a highly dynamic and complex organelle, is the site for synthesis, folding, and modification of transmembrane and secretory proteins. Any disruptions to the endoplasmic reticulum such as an accumulation of misfolded or unfolded proteins results in activation of the unfolded protein response (UPR). The UPR is comprised of three distinct signal transduction pathways that work to restore homeostasis to the endoplasmic reticulum. This review summarizes select mouse models available to study the UPR and the information learned from the analyses of these models.
AB - The endoplasmic reticulum, a highly dynamic and complex organelle, is the site for synthesis, folding, and modification of transmembrane and secretory proteins. Any disruptions to the endoplasmic reticulum such as an accumulation of misfolded or unfolded proteins results in activation of the unfolded protein response (UPR). The UPR is comprised of three distinct signal transduction pathways that work to restore homeostasis to the endoplasmic reticulum. This review summarizes select mouse models available to study the UPR and the information learned from the analyses of these models.
UR - http://www.scopus.com/inward/record.url?scp=79951629888&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=79951629888&partnerID=8YFLogxK
U2 - 10.1016/B978-0-12-385928-0.00006-7
DO - 10.1016/B978-0-12-385928-0.00006-7
M3 - Chapter
C2 - 21329796
AN - SCOPUS:79951629888
T3 - Methods in Enzymology
SP - 91
EP - 109
BT - Methods in Enzymology
PB - Academic Press Inc
ER -