YTA12/YMR089C Literature Guide Help

Other names published for YTA12: RCA1, m-AAA protease subunit YTA12, YMR089C

YTA12 - Substrates/Ligands/Cofactors (10)

ReferenceOther Genes Addressed
Claypool SM, et al.  (2011) Barth syndrome mutations that cause tafazzin complex lability. J Cell Biol 192(3):447-62
Lee S, et al.  (2011) Electron Cryomicroscopy Structure of a Membrane-anchored Mitochondrial AAA Protease. J Biol Chem 286(6):4404-11
Di Bella D, et al.  (2010) Mutations in the mitochondrial protease gene AFG3L2 cause dominant hereditary ataxia SCA28. Nat Genet 42(4):313-21
Augustin S, et al.  (2009) An intersubunit signaling network coordinates ATP hydrolysis by m-AAA proteases. Mol Cell 35(5):574-85
Suppanz IE, et al.  (2009) The m-AAA protease processes cytochrome c peroxidase preferentially at the inner boundary membrane of mitochondria. Mol Biol Cell 20(2):572-80
Tatsuta T, et al.  (2007) m-AAA protease-driven membrane dislocation allows intramembrane cleavage by rhomboid in mitochondria. EMBO J 26(2):325-35
Ishihara N, et al.  (2006) Regulation of mitochondrial morphology through proteolytic cleavage of OPA1. EMBO J 25(13):2966-77
Korbel D, et al.  (2004) Membrane protein turnover by the m-AAA protease in mitochondria depends on the transmembrane domains of its subunits. EMBO Rep 5(7):698-703
Esser K, et al.  (2002) A novel two-step mechanism for removal of a mitochondrial signal sequence involves the mAAA complex and the putative rhomboid protease Pcp1. J Mol Biol 323(5):835-43
Leonhard K, et al.  (2000) Membrane protein degradation by AAA proteases in mitochondria: extraction of substrates from either membrane surface. Mol Cell 5(4):629-38