Endoplasmic Reticulum Stress and STAT3 signaling
| Autor: | Tzu-Yi Chao, 趙子毅 |
|---|---|
| Rok vydání: | 2004 |
| Druh dokumentu: | 學位論文 ; thesis |
| Popis: | 92 From the perspective of protein biosynthesis, the endoplasmic reticulum (ER) can be viewed as a processing plant for folding and posttranslational modification of secreted and integral membrane proteins. Proteins are translocated into the ER in an unfolded state, it is the primary function of this organelle to modify and fold the translocated proteins to acquire their biologically active conformation. An imbalance between the load of client proteins facing the ER and the organelle’s ability to process that load is defined as ER stress. To cope with the stress, cells activate intracellular signaling pathway-the unfolded protein response (UPR), to provide adaptive responses for survival. In view of the fact that signal transducers and activators of transcription 3(STAT3) is constitutively activated in a wide variety of cancer cells and primary tumors, providing a growth advantage by inducing cell proliferation and inhibiting apoptosis, we sought to explore whether STAT3 was involved in the cellular response to ER stress. According to our data, we found that STAT3 exhibited a phenomenon under ER stress. While itsαform increases steadily, there’s a remarkable vanishment of STAT3β. Intriguingly, STAT3 translocates to the nuclear despite lacking any signs of Tyrosine 705 phosphorylation. Instead, it is phosphorylated at Serine 727. Interestingly, we found that STAT3 interacts with grp78, an ER stress-induced protein, suggesting that this interaction may lead to the translocation of STAT3.Our findings may provide a linkage for ER stress and STAT3 mediated signaling pathway, and its role under ER stress should be further studied. |
| Databáze: | Networked Digital Library of Theses & Dissertations |
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