TIMM8:TIMM13 chaperones hydrophobic proteins

Stable Identifier
R-HSA-1299484
Type
Reaction [binding]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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As inferred from the yeast TIM8:TIM13 complex, the human TIMM8:TIMM13 complex chaperones hydrophobic membrane proteins in the intermembrane space until their insertion into the inner or outer membrane. In yeast experimentally verified substrates of the TIM8:TIM13 complex include TIM23 (TIMM23 in human) and TOM40 (TOMM40 in human). Many other mitochondrial proteins are anticipated to be chaperoned by the TIMM8:TIMM13 complex.
Literature References
PubMed ID Title Journal Year
15254020 The calcium-binding aspartate/glutamate carriers, citrin and aralar1, are new substrates for the DDP1/TIMM8a-TIMM13 complex

Roesch, K, Hynds, PJ, Varga, R, Tranebjaerg, L, Koehler, CM

Hum Mol Genet 2004
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
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