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Biogenesis and function of mitochondria depend on the import of about 1000 precursor proteins that are produced on cytosolic ribosomes. The translocase of the outer membrane (TOM) forms the entry gate for most proteins. After passage through the TOM channel, dedicated preprotein translocases sort the precursor proteins into the mitochondrial subcompartments. Many proteins have to be assembled into oligomeric membrane-integrated complexes in order to perform their functions. In this review, we discuss a dual role of mitochondrial preprotein translocases in protein translocation and oligomeric assembly, focusing on the biogenesis of the TOM complex and the respiratory chain. The sorting and assembly machinery (SAM) of the outer mitochondrial membrane forms a dynamic platform for coupling transport and assembly of TOM subunits. The biogenesis of the cytochrome c oxidase of the inner membrane involves a molecular circuit to adjust translation of mitochondrial-encoded core subunits to the availability of nuclear-encoded partner proteins. Thus, mitochondrial protein translocases not only import precursor proteins but can also support their assembly into functional complexes.
This article was published in the following journal.
Name: Biological chemistry
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A RHO GTP-BINDING PROTEIN involved in regulating signal transduction pathways that control assembly of focal adhesions and actin stress fibers. This enzyme was formerly listed as EC 188.8.131.52.
A rho GTP-binding protein that is prenylated (see PROTEIN PRENYLATION) at its C-terminus and cycles between the cytoplasm and plasma membrane, linking receptor signaling pathways with assembly of FOCAL ADHESIONS; STRESS FIBERS; and contractile ring formation during CYTOKINESIS. It is overexpressed in proliferating and metastatic tumor cells.
A multi-pass transmembrane protein that contains a C-terminal RING finger domain. It localizes to the PEROXISOME membrane and is essential for peroxisome biogenesis. Mutations in the PEX2 gene are associated with ZELLWEGER SYNDROME and INFANTILE REFSUM DISEASE.
The alpha subunit of mitochondrial trifunctional protein. It contains both enoyl-CoA hydratase activity (EC 184.108.40.206) and long-chain-3-hydroxyacyl-CoA dehydrogenase activity (EC 220.127.116.11). There are four of these alpha subunits in each mitochondrial trifunctional protein molecule.
A mitochondrial uncoupling protein that is expressed in many tissues and exhibits the greatest expression in SKELETAL MUSCLE. It regulates mitochondrial ATP production and the generation of REACTIVE OXYGEN SPECIES.
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