Involvement of the N-terminus of Bax in its intracellular localization and function

被引：58

作者：

Cartron, PF ^{[1
]}

Moreau, C ^{[1
]}

Oliver, L ^{[1
]}

Mayat, E ^{[1
]}

Meflah, K ^{[1
]}

Vallette, FM ^{[1
]}

机构：

[1] INSERM U419, IFR 26, F-44035 Nantes, France

来源：

FEBS LETTERS | 2002年 / 512卷 / 1-3期

关键词：

apoptosis; Bax; conformation; mutagenesis;

D O I：

10.1016/S0014-5793(02)02227-5

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：

We have identified, using site-directed mutagenesis, a proline located at position 13 of Baxalpha (Bax) as crucial for the maintenance of its cytosolic conformation. The substitution of this proline by a valine results in a strong binding of Bax to mitochondria and to conformational changes monitored by a decreased sensitivity of Bax to mild proteolysis and the enhancement of its oligomerization state. Deletion of the C-terminus of Bax does not modify its intracellular localization. On the other hand, the pro-apoptotic activity of Bax is enhanced by a deletion of the C-terminus in the absence of the N-terminus but is decreased in its presence. These results suggest that both extremities functionally interact to control the activity but not the subcellular localization of Bax. (C) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

引用

页码：95 / 100

页数：6

共 31 条

[1] Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells [J].