Precursor proteins enter TIMM23 SORT

Stable Identifier
R-HSA-1299487
Type
Reaction [binding]
Species
Homo sapiens
Compartment
mitochondrial intermembrane space, mitochondrial inner membrane
ReviewStatus
5/5
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Precursor proteins enter TIMM23 SORT
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As inferred from the yeast TIM23 complex, the human TIMM23 complex resides in the inner membrane of the mitochondrion and transfers precursor proteins to the inner membrane. The TIMM23 complex appears to adopt different configurations (and perhaps different subunit compositions) depending on whether the substrate is destined for the inner membrane or the matrix. Here we refer to the TIMM23 SORT complex as the configuration that delivers inner membrane proteins. The TIMM21 subunit is required for this activity. In yeast, the N-terminal presequences of precursors first interact with TIM50 and TIM23 (TIMM50 and TIMM23 in human, Zhang et al. 2013). The TIM17 and TIM23 subunits (TIMM17 and TIMM23 in human) form a channel and are required to initiate translocation of precursors.
In yeast experimentally verified substrates of the TIM23 SORT complex targeted to the inner membrane include CYB2, DLD (LDHD in human), ATP9 (ATP5G1 in human), COQ2, TIM54 (TIMM54 in human), COX4, COX5A, and ATP2 (ATP5B in human). Many other inner membrane proteins are believed to be substrates of the TIMM23 complex.
Literature References
PubMed ID Title Journal Year
23811401 Interaction of presequence peptides with human translocase of inner membrane of mitochondria Tim23

Zhao, Q, Zhang, Y, Deng, H, Li, SJ

Biochem. Biophys. Res. Commun. 2013
19453276 Multiple pathways for mitochondrial protein traffic

Yamano, K, Endo, T

Biol Chem 2009
18174896 Multiple pathways for sorting mitochondrial precursor proteins

Pfanner, N, Wagner, R, Sickmann, A, Bolender, N, Meisinger, C

EMBO Rep 2008
Participants
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Output
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as an event of
Inferred From
Precursor proteins enter TIM23 SORT complex (Saccharomyces cerevisiae)
Authored
May, B  (2011-05-21)
Reviewed
Endo, T  (2012-02-12)
D'Eustachio, P  (2011-11-02)
Created
May, B  (2011-05-23)
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