TIMM8:TIMM13 chaperones hydrophobic proteins

Stable Identifier
Reaction [binding]
Homo sapiens
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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
19453276 Multiple pathways for mitochondrial protein traffic

Endo, T, Yamano, K

Biol Chem 2009
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
18174896 Multiple pathways for sorting mitochondrial precursor proteins

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

EMBO Rep 2008
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