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Resistance to HSP90 inhibition involving loss of MCL1 addiction.

Abstract：

:Inhibition of the chaperone heat-shock protein 90 (HSP90) induces apoptosis, and it is a promising anti-cancer strategy. The mechanisms underpinning apoptosis activation following HSP90 inhibition and how they are modified during acquired drug resistance are unknown. We show for the first time that, to induce apoptosis, HSP90 inhibition requires the cooperation of multi BH3-only proteins (BID, BIK, PUMA) and the reciprocal suppression of the pro-survival BCL-2 family member MCL1, which occurs via inhibition of STAT5A. A subset of tumour cell lines exhibit dependence on MCL1 expression for survival and this dependence is also associated with tumour response to HSP90 inhibition. In the acquired resistance setting, MCL1 suppression in response to HSP90 inhibitors is maintained; however, a switch in MCL1 dependence occurs. This can be exploited by the BH3 peptidomimetic ABT737, through non-BCL-2-dependent synthetic lethality.

journal_name

Oncogene

journal_title

Oncogene

authors

Busacca S,Law EW,Powley IR,Proia DA,Sequeira M,Le Quesne J,Klabatsa A,Edwards JM,Matchett KB,Luo JL,Pringle JH,El-Tanani M,MacFarlane M,Fennell DA

doi

10.1038/onc.2015.213

subject

Has Abstract

pub_date

2016-03-24 00:00:00

pages

1483-92

issue

12

eissn

0950-9232

issn

1476-5594

pii

onc2015213

journal_volume

35

pub_type

杂志文章

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