Detail IRE1 Signaling Affects Cell Fate During the Unfolded Protein Response   Oleh:  Lin, Jonathan H. ; Han, Li ; Yasumura, Douglas ; Cohen, Hannah ; Chao, Zhang ; Panning, Barbara ; Shokat, Kevan M. ; LaVail, Matthew M. ; Walter, Peter Jenis: Article from Bulletin/Magazine Dalam koleksi: SCIENCE (keterangan: ada di Proquest) vol. 318 no. 5852 (Nov. 2007), page 944. Ketersediaan Perpustakaan FK Nomor Panggil: S01.K.2007.09 Non-tandon: 1 (dapat dipinjam: 0) Tandon: tidak ada     Lihat Detail Induk Isi artikel Endoplasmic reticulum (ER) stress activates a set of signaling pathways, collectively termed the unfolded protein response (UPR). The three UPR branches (IRE1, PERK, and ATF6) promote cell survival by reducing misfolded protein levels. UPR signaling also promotes apoptotic cell death if ER stress is not alleviated. How the UPR integrates its cytoprotective and proapoptotic outputs to select between life or death cell fates is unknown. We found that IRE1 and ATF6 activities were attenuated by persistent ER stress in human cells. By contrast, PERK signaling, including translational inhibition and proapoptotic transcription regulator Chop induction, was maintained. When IRE1 activity was sustained artificially, cell survival was enhanced, suggesting a causal link between the duration of UPR branch signaling and life or death cell fate after ER stress. Key findings from our studies in cell culture were recapitulated in photoreceptors expressing mutant rhodopsin in animal models of retinitis pigmentosa. Opini Anda Klik untuk menuliskan opini Anda tentang koleksi ini! Kembali

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