Literature DB >> 17266933

Ire1 regulated XBP1 mRNA splicing is essential for the unfolded protein response (UPR) in Drosophila melanogaster.

Nongluk Plongthongkum1, Niwed Kullawong, Sakol Panyim, Witoon Tirasophon.   

Abstract

The ability of cells to survive and recover from deteriorating effects of endoplasmic reticulum (ER) stress relies on the unfolded protein response (UPR). The signaling pathway of Ire1p mediate mRNA splicing plays diverge role in UPR response in different organisms from yeast to mammals. Here, we report that Ire1p mediated XBP1 mRNA splicing mechanism is extremely conserved and exerts a critical role for modulating Xbp1 protein synthesis in Drosophila melanogaster. This system is operative in Drosophila S2 cells as a prominent mechanism to mediate transcriptional activation of UPR responsive genes during ER stress.

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Year:  2007        PMID: 17266933     DOI: 10.1016/j.bbrc.2007.01.056

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  26 in total

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5.  A haploid genetic screen identifies the major facilitator domain containing 2A (MFSD2A) transporter as a key mediator in the response to tunicamycin.

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6.  ER stress signaling requires RHD3, a functionally conserved ER-shaping GTPase.

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8.  IRE1α nucleotide sequence cleavage specificity in the unfolded protein response.

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9.  Endoplasmic reticulum stress contributes to the cell death induced by UCH-L1 inhibitor.

Authors:  Yu-Yan Tan; Hai-Yan Zhou; Zhi-Quan Wang; Sheng-Di Chen
Journal:  Mol Cell Biochem       Date:  2008-07-12       Impact factor: 3.396

10.  BAX inhibitor-1 is a negative regulator of the ER stress sensor IRE1alpha.

Authors:  Fernanda Lisbona; Diego Rojas-Rivera; Peter Thielen; Sebastian Zamorano; Derrick Todd; Fabio Martinon; Alvaro Glavic; Christina Kress; Jonathan H Lin; Peter Walter; John C Reed; Laurie H Glimcher; Claudio Hetz
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