2015
DOI: 10.1073/pnas.1504615112
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Retro-translocation of mitochondrial intermembrane space proteins

Abstract: The content of mitochondrial proteome is maintained through two highly dynamic processes, the influx of newly synthesized proteins from the cytosol and the protein degradation. Mitochondrial proteins are targeted to the intermembrane space by the mitochondrial intermembrane space assembly pathway that couples their import and oxidative folding. The folding trap was proposed to be a driving mechanism for the mitochondrial accumulation of these proteins. Whether the reverse movement of unfolded proteins to the c… Show more

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Cited by 103 publications
(104 citation statements)
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“…Although the mitochondrial matrix is not accessible to the cytosolic proteasome, the outer mitochondrial membrane is. Ubiquitination of key mitochondrial outer membrane proteins can alter mitochondrial dynamics through fusion (mitofusins) and fission of mitochondria . The ubiquitination proteasome‐mediated degradation of the mitofusin proteins Mitofusin 1 and Mitofusin 2 in damaged mitochondria is necessary in order to prevent fusion with healthy mitochondria and favor fragmentation instead .…”
Section: Discussionmentioning
confidence: 99%
“…Although the mitochondrial matrix is not accessible to the cytosolic proteasome, the outer mitochondrial membrane is. Ubiquitination of key mitochondrial outer membrane proteins can alter mitochondrial dynamics through fusion (mitofusins) and fission of mitochondria . The ubiquitination proteasome‐mediated degradation of the mitofusin proteins Mitofusin 1 and Mitofusin 2 in damaged mitochondria is necessary in order to prevent fusion with healthy mitochondria and favor fragmentation instead .…”
Section: Discussionmentioning
confidence: 99%
“…Many mitochondrial precursor proteins, before they productively reach the mitochondrial compartment, are under control of the ubiquitin–proteasome system (UPS), a major protein‐degrading pathway that is involved in maintaining cellular protein homeostasis (Radke et al , ; Bragoszewski et al , ). Furthermore, IMS proteins can undergo reductive unfolding and slide back to the cytosol where they are also degraded by the UPS (Bragoszewski et al , ). However, the contribution of cytosolic protein control mechanisms to mitochondriopathies has not been investigated.…”
Section: Introductionmentioning
confidence: 99%
“…The ubiquitin-proteasome system (UPS) [9][10][11][12] is involved in the degradation of MIA substrate proteins 8,13 . Abundance of many proteins involved in the UPS did not change in mia40-4int S , including the core proteasomal subunits (Supplementary Table 3 and Extended Data Fig.…”
mentioning
confidence: 99%