Hsp90 Inhibition Affects Cell Metabolism by Disrupting Mitochondrial Protein Insertion

URN to cite this document:: urn:nbn:de:bvb:355-epub-345281
DOI to cite this document:: 10.5283/epub.34528

Mycielska, Maria ; Wachsmuth, Christian J. ; Dettmer, Katja ; Wagner, Christine ; Oefner, Peter J. ; Geissler, Edward K. ; Lang, Sven A.

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Date of publication of this fulltext: 05 Sep 2016 13:45

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Item type:	Article
Journal or Publication Title:	HSOA Journal of Cell Biology and Cell Metabolism
Publisher:	Herald Scholarly Open Access
Volume:	1
Page Range:	002
Date:	2014
Institutions:	Medicine > Lehrstuhl für Chirurgie Medicine > Institut für Funktionelle Genomik > Lehrstuhl für Funktionelle Genomik (Prof. Oefner)
Keywords:	Cancer; Glycolysis; Mitochondrial activity; Tom40
Dewey Decimal Classification:	600 Technology > 610 Medical sciences Medicine
Status:	Published
Refereed:	Yes, this version has been refereed
Created at the University of Regensburg:	Yes
Item ID:	34528

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Abstract

Hsp90 is a molecular chaperone interacting with hundreds client proteins. Little is known, however, about Hsp90 influence on cancer cell metabolism. Here we show that the inhibition of Hsp90 affects indirectly glycolysis by disrupting mitochondrial insertion of the elements of Translocase of the Outer Membrane (TOM) complex in tumor cells. Improper insertion of Tom40 decreases the abundance of ...