Vogel, Rutger O.;
Janssen, Rolf J.R.J.;
van den Brand, Mariël A.M.;
Dieteren, Cindy E.J.;
Verkaart, Sjoerd;
Koopman, Werner J.H.;
Willems, Peter H.G.M.;
Pluk, Wendy;
van den Heuvel, Lambert P.W.J.;
Smeitink, Jan A.M.;
Nijtmans, Leo G.J.
Cytosolic signaling protein Ecsit also localizes to mitochondria where it interacts with chaperone NDUFAF1 and functions in complex I assembly
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Medientyp:
E-Artikel
Titel:
Cytosolic signaling protein Ecsit also localizes to mitochondria where it interacts with chaperone NDUFAF1 and functions in complex I assembly
Beteiligte:
Vogel, Rutger O.;
Janssen, Rolf J.R.J.;
van den Brand, Mariël A.M.;
Dieteren, Cindy E.J.;
Verkaart, Sjoerd;
Koopman, Werner J.H.;
Willems, Peter H.G.M.;
Pluk, Wendy;
van den Heuvel, Lambert P.W.J.;
Smeitink, Jan A.M.;
Nijtmans, Leo G.J.
Beschreibung:
<jats:p>Ecsit is a cytosolic adaptor protein essential for inflammatory response and embryonic development via the Toll-like and BMP (bone morphogenetic protein) signal transduction pathways, respectively. Here, we demonstrate a mitochondrial function for Ecsit (an evolutionary conserved signaling intermediate in Toll pathways) in the assembly of mitochondrial complex I (NADH:ubiquinone oxidoreductase). An N-terminal targeting signal directs Ecsit to mitochondria, where it interacts with assembly chaperone NDUFAF1 in 500- to 850-kDa complexes as demonstrated by affinity purification and vice versa RNA interference (RNAi) knockdowns. In addition, Ecsit knockdown results in severely impaired complex I assembly and disturbed mitochondrial function. These findings support a function for Ecsit in the assembly or stability of mitochondrial complex I, possibly linking assembly of oxidative phosphorylation complexes to inflammatory response and embryonic development.</jats:p>