title: Identification of 14-3-3γ as a Mieap-interacting protein and its role in mitochondrial quality control.
abstract: Mieap, a p53-inducible protein, controls mitochondrial integrity by inducing the accumulation of lysosomal proteins within mitochondria. This phenomenon is designated MALM, for Mieap-induced accumulation of lysosome-like organelles within mitochondria. To identify this novel Mieap-interacting protein(s), we performed a two-dimensional image-converted analysis of liquid chromatography and mass spectrometry (2DICAL) on the proteins immunoprecipitated by an anti-Mieap antibody. We indentified 14-3-3γ as one of the proteins that was included in the Mieap-binding protein complex when MALM was induced. The interaction between Mieap and 14-3-3γ was confirmed on the exogenous and endogenous proteins. Interestingly, 14-3-3γ was localized within mitochondria when MALM occurred. A 14-3-3γ deficiency did not affect the accumulation of Mieap and lysosomal proteins within mitochondria, but dramatically inhibited the elimination of oxidized mitochondrial proteins. These results suggest that 14-3-3γ plays a critical role in eliminating oxidized mitochondrial proteins during the MALM process by interacting with Mieap within mitochondria.
authors.forename: Takafumi
authors.initials: T
authors.lastname: Miyamoto
authors.forename: Noriaki
authors.initials: N
authors.lastname: Kitamura
authors.forename: Masaya
authors.initials: M
authors.lastname: Ono
authors.forename: Yasuyuki
authors.initials: Y
authors.lastname: Nakamura
authors.forename: Masaki
authors.initials: M
authors.lastname: Yoshida
authors.forename: Hiroki
authors.initials: H
authors.lastname: Kamino
authors.forename: Ryuya
authors.initials: R
authors.lastname: Murai
authors.forename: Tesshi
authors.initials: T
authors.lastname: Yamada
authors.forename: Hirofumi
authors.initials: H
authors.lastname: Arakawa