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Heat shock protein 70 binding inhibits the nuclear import of apoptosis-inducing factor.

Abstract：

:Heat shock protein 70 (HSP70) can inhibit apoptosis by neutralizing and interacting with apoptosis-inducing factor (AIF), a mitochondrial flavoprotein that translocates upon apoptosis induction to the nucleus, via the cytosol. Here, we show that only members of the HSP70 family interact with AIF. Systematic deletion mapping revealed the existence of three distinct functional regions in the AIF protein: (1) a region between amino acids 150 and 228 that binds HSP70, (2) a domain between residues 367 and 459 that includes a nuclear localization sequence (NLS) and (3) a C-terminal domain beyond residue 567 required for its chromatin-condensing activity. Deletion of the 150-268 domain completely abolished HSP70 binding and facilitated the nuclear import of AIF, resulting in a gain-of-function phenotype with enhanced AIF-mediated chromatin condensation as compared to wild-type AIF. This gain-of-function phenotype was observed in wild-type control cells (which express low but significant levels of HSP70), yet was lost when AIFDelta150-268 was introduced into HSP70 knockout cells, underscoring the functional importance of the AIF-HSP70 interaction. Altogether, our data demonstrate that AIF inhibition by HSP70 involves cytosolic retention of AIF. Moreover, it appears that endogenous HSP70 protein levels are sufficiently elevated to modulate the lethal action of AIF.

journal_name

Oncogene

journal_title

Oncogene

authors

Gurbuxani S,Schmitt E,Cande C,Parcellier A,Hammann A,Daugas E,Kouranti I,Spahr C,Pance A,Kroemer G,Garrido C

doi

10.1038/sj.onc.1206794

subject

Has Abstract

pub_date

2003-10-02 00:00:00

pages

6669-78

issue

43

eissn

0950-9232

issn

1476-5594

pii

1206794

journal_volume

22

pub_type

杂志文章

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