A novel protein, RTN-XS, interacts with both Bcl-XL and Bcl-2 on endoplasmic reticulum and reduces their anti-apoptotic activity.

Abstract:

:Bcl-2 and Bcl-XL serve as critical inhibitors of apoptosis triggered by a broad range of stimuli, mainly acting on the mitochondria. We identified two members of the reticulon (RTN) family as Bcl-XL binding proteins, i.e., NSP-C (RTN1-C) and a new family member, RTN-XS, both of which did not belong to the Bcl-2 family and were predominantly localized on the endoplasmic reticulum (ER). RTN-XS interacted with both Bcl-XL and Bcl-2, increased the localization of Bcl-XL and Bcl-2 on the ER, and reduced the anti-apoptotic activity of Bcl-XL and Bcl-2. On the other hand, NSP-C interacted only with Bcl-XL, affected the localization of Bcl-XL, and reduced Bcl-XL activity, but had no effect on Bcl-2. These results suggest that RTN family proteins can modulate the anti-apoptotic activity of Bcl-XL and Bcl-2 by binding with them and can change their localization to the ER.

journal_name

Oncogene

journal_title

Oncogene

authors

Tagami S,Eguchi Y,Kinoshita M,Takeda M,Tsujimoto Y

doi

10.1038/sj.onc.1203948

subject

Has Abstract

pub_date

2000-11-23 00:00:00

pages

5736-46

issue

50

eissn

0950-9232

issn

1476-5594

journal_volume

19

pub_type

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