期刊
ONCOGENE
卷 19, 期 50, 页码 5736-5746出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/sj.onc.1203948
关键词
RTN-x(S); Bcl-x(L); Bcl-2; endoplasmic reticulum; apoptosis
Bcl-2 and Bcl-x(L) 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-x(L) binding proteins, i.e,, NSP-C (RTNt-C) and a new family member, RTN-x(S), both of which did not belong to the Bcl-2 family and were predominantly localized on the endoplasmic reticulum (ER). RTN-x(S) interacted with both Bcl-x(L) 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-x(L), affected the localization of Bcl-x(L), 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-x(L) and Bcl-2 by binding with them and can change their localization to the ER.
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