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  Failed mitochondrial import and impaired proteostasis trigger SUMOylation of mitochondrial proteins

Paasch, F., den Brave, F., Psakhye, I., Pfander, B., & Jentsch, S. (2018). Failed mitochondrial import and impaired proteostasis trigger SUMOylation of mitochondrial proteins. Journal of Biological Chemistry, 293(2), 599-609. doi:10.1074/jbc.M117.817833.

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J. Biol. Chem.-2018-Paasch-599-609.pdf (Publisher version), 2MB
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 Creators:
Paasch, Florian1, Author              
den Brave, Fabian1, Author              
Psakhye, Ivan1, Author              
Pfander, Boris2, Author              
Jentsch, Stefan1, Author              
Affiliations:
1Jentsch, Stefan / Molecular Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565156              
2Pfander, Boris / DNA Replication and Genome Integrity, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565165              

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Free keywords: UBIQUITIN-PROTEASOME SYSTEM; ALPHA-SYNUCLEIN AGGREGATION; SACCHAROMYCES-CEREVISIAE; HEAT-SHOCK; QUALITY-CONTROL; SUMO MODIFICATION; STRESS-RESPONSE; ALCOHOL-DEHYDROGENASE; MISFOLDED PROTEINS; PRECURSOR PROTEINBiochemistry & Molecular Biology; 70-kilodalton heat shock protein (HSP70); mitochondria; proteasome; proteostasis; small ubiquitin-like modifier (SUMO); mitochondrial proteins; protein quality control; SUMOylation;
 Abstract: Modification by the ubiquitin-like protein SUMO affects hundreds of cellular substrate proteins and regulates a wide variety of physiological processes. While the SUMO system appears to predominantly target nuclear proteins and, to a lesser extent, cytosolic proteins, hardly anything is known about the SUMOylation of proteins targeted to membrane-enclosed organelles. Here, we identify a large set of structurally and functionally unrelated mitochondrial proteins as substrates of the SUMO pathway in yeast. We show that SUMO modification of mitochondrial proteins does not rely on mitochondrial targeting and, in fact, is strongly enhanced upon import failure, consistent with the modification occurring in the cytosol. Moreover, SUMOylated forms of mitochondrial proteins particularly accumulate in HSP70- and proteasome-deficient cells, suggesting that SUMOylation participates in cellular protein quality control. We therefore propose that SUMO serves as a mark for nonfunctional mitochondrial proteins, which only sporadically arise in unstressed cells but strongly accumulate upon defective mitochondrial import and impaired proteostasis. Overall, our findings provide support for a role of SUMO in the cytosolic response to aberrant proteins.

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Language(s): eng - English
 Dates: 2017-11-282018-01
 Publication Status: Published in print
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000419915400016
DOI: 10.1074/jbc.M117.817833
 Degree: -

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Title: Journal of Biological Chemistry
  Other : J. Biol. Chem.
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 293 (2) Sequence Number: - Start / End Page: 599 - 609 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826