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  Uth1 is a mitochondrial inner membrane protein dispensable for post-log-phase and rapamycin-induced mitophagy.

Weiter, E., Montino, M., Reinhold, R., Schlotterhose, P., Krick, R., Dudek, J., et al. (2013). Uth1 is a mitochondrial inner membrane protein dispensable for post-log-phase and rapamycin-induced mitophagy. The FEBS Journal, 280(20), 4970-4982. doi:10.1111/febs.12468.

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Weiter, E., Author
Montino, M., Author
Reinhold, R., Author
Schlotterhose, P., Author
Krick, R., Author
Dudek, J., Author
Rehling, P.1, Author           
Thumm, M., Author
Affiliations:
1Max Planck Fellow Peter Rehling, ou_1298545              

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Free keywords: Atg32; Atg33; macroautophagy; mitophagy; Saccharomycescerevisiae; Uth1; Yme1
 Abstract: Mitochondria are turned over by an autophagic process termed mitophagy. This process is considered to remove damaged, superfluous and aged organelles. However, little is known about how defective organelles are recognized, what types of damage induce turnover, and whether an identical set of factors contributes to degradation under different conditions. Here we systematically compared the mitophagy rate and requirement for mitophagy-specific proteins during post-log-phase and rapamycin-induced mitophagy. To specifically assess mitophagy of damaged mitochondria, we analyzed cells accumulating proteins prone to degradation due to lack of the mitochondrial AAA-protease Yme1. While autophagy 32 (Atg32) was required under all tested conditions, the function of Atg33 could be partially bypassed in post-log-phase and rapamycin-induced mitophagy. Unexpectedly, we found that Uth1 was dispensable for mitophagy. A re-evaluation of its mitochondrial localization revealed that Uth1 is a protein of the inner mitochondrial membrane that is targeted by a cleavable N-terminal pre-sequence. In agreement with our functional analyses, this finding excludes a role of Uth1 as a mitochondrial surface receptor.

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Language(s): eng - English
 Dates: 2013-09-022013-10
 Publication Status: Issued
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 Rev. Type: Peer
 Identifiers: DOI: 10.1111/febs.12468
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Title: The FEBS Journal
Source Genre: Journal
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Pages: - Volume / Issue: 280 (20) Sequence Number: - Start / End Page: 4970 - 4982 Identifier: -