ATP-dependent zinc metalloprotease YME1L1

Definition:

ATP-dependent metalloprotease that catalyzes the degradation of folded and unfolded proteins with a suitable degron sequence in the mitochondrial intermembrane region. Plays an important role in regulating mitochondrial morphology and function by cleaving OPA1 at position S2, giving rise to a form of OPA1 that promotes maintenance of normal mitochondrial structure and mitochondrial protein metabolism. Ensures cell proliferation, maintains normal cristae morphology and complex I respiration activity, promotes antiapoptotic activity and protects mitochondria from the accumulation of oxidatively damaged membrane proteins. Required for normal, constitutive degradation of PRELID1. Catalyzes the degradation of OMA1 in response to membrane depolarization. Required to control the accumulation of nonassembled respiratory chain subunits (NDUFB6, OX4 and ND1).

References:

[1]. Hui Shi, et al. Engineered AAA+ proteases reveal principles of proteolysis at the mitochondrial inner membrane. Nat Commun. 2016 Oct 27;7:13301. [Content Brief]

[2]. Olwenn Guillery, et al. Metalloprotease-mediated OPA1 processing is modulated by the mitochondrial membrane potential. Biol Cell. 2008 May;100(5):315-25. [Content Brief]

[3]. T Kelly Rainbolt, et al. Reciprocal Degradation of YME1L and OMA1 Adapts Mitochondrial Proteolytic Activity during Stress. Cell Rep. 2016 Mar 8;14(9):2041-2049. [Content Brief]

[4]. Bianca Hartmann, et al. Homozygous YME1L1 mutation causes mitochondriopathy with optic atrophy and mitochondrial network fragmentation. Elife. 2016 Aug 6;5:e16078. [Content Brief]

[5]. Lukas Stiburek, et al. YME1L controls the accumulation of respiratory chain subunits and is required for apoptotic resistance, cristae morphogenesis, and cell proliferation. Mol Biol Cell. 2012 Mar;23(6):1010-23. [Content Brief]

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