BCL-2 modulates the unfolded protein response by enhancing splicing of X-box binding protein-1

被引：19

作者：

Chonghaile, Triona Ni ^{[1
,2
]}

Gupta, Sanjeev ^{[1
,3
]}

John, Mohan ^{[1
,2
]}

Szegezdi, Eva ^{[1
,2
]}

Logue, Susan E. ^{[1
,2
]}

Samali, Afshin ^{[1
,2
]}

机构：

[1] Natl Univ Ireland, Apoptosis Res Ctr, Galway, Ireland

[2] Natl Univ Ireland, Sch Nat Sci, Galway, Ireland

[3] Natl Univ Ireland, Sch Med, Galway, Ireland

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2015年 / 466卷 / 01期

关键词：

BCL-2; XBP-1; Unfolded protein response; ER stress; Apoptosis; ENDOPLASMIC-RETICULUM STRESS; SENSOR IRE1-ALPHA; INDUCED APOPTOSIS; PROAPOPTOTIC BAX; CA2+; INHIBITOR-1; CELLS; BI-1;

D O I：

10.1016/j.bbrc.2015.08.100

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Accumulation of unfolded proteins within the endoplasmic reticulum (ER) triggers a highly conserved stress response mechanism termed the unfolded protein response (UPR). The UPR is a complex series of signaling pathways controlled by ER localized transmembrane receptors, PERK, ATF6 and IRE1 alpha. Following activation IRE1 alpha splices XBP-1 mRNA facilitating the formation of a potent transcription factor, spliced XBP-1. The BCL-2 family members, BAX and BAK, in addition to the mitochondrion also localize to the ER and have been demonstrated to directly interact with IRE1 alpha promoting its activity. In this study we show that in addition to BAX and BAK, the anti-apoptotic BCL-2 protein can regulate IRE1 alpha activity. Enhanced splicing of XBP-1 was observed in BCL-2 overexpressing cells implicating BCL-2 in the complex regulation of IRE1 alpha activity. (C) 2015 Elsevier Inc. All rights reserved.

引用

页码：40 / 45

页数：6

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