YME1L1 binds mitochondrial inner membrane proteins

Stable Identifier
R-HSA-9839064
Type
Reaction [binding]
Species
Homo sapiens
Compartment
mitochondrial inner membrane
ReviewStatus
5/5
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YME1L1 binds mitochondrial inner membrane proteins
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YME1L1 (YME1L, i-AAA+) is a homohexameric zinc metalloprotease that is anchored in the inner membrane and protrudes into the mitochondrial intermembrane space (Coppola et al. 2000, Shah et al. 2000, Wai et al. 2016). Substrate proteins of YME1L1 initially bind conserved helices at the N-terminal end of the ATPase domain and at the C-terminal domain of the protease domain (inferred from the yeast homolog in Graef et al. 2007). The substrate protein is unfolded and translocated processively in an ATP-dependent reaction to a central pore formed by the protease domains of the YME1L1 complex.
YME1L1 binds, unfolds, and degrades specific inner membrane proteins (MacVicar et al. 2019). These include components of the mitochondrial import apparatus: TIMM17A (Rainbolt et al. 2013), TIMM22 (MacVicar et al. 2019), and improperly folded TIMM9 and TIMM10 (inferred from yeast homologs in Baker et al. 2012). Substrates of YME1L1 also include components of the respiratory chain: MT‑ND1 and MT‑CO4 (Stiburek et al. 2012, Cesnekova et al. 2018), unassembled MT‑CO2 (inferred from yeast homologs in Nakai et al. 1995), and subunits of respiratory chain complex I (Cesnekova et al. 2018) such as unassembled NDUFB6 (Stiburek et al. 2012, Cesnekova et al. 2018). YME1L1 also degrades the protease OMA1 (Rainbolt et al. 2016), a stress-activated ATP-independent protease that can act reciprocally to YME1L1, and OPA1 (Cesnekova et al. 2018), a dynamin-like protein that controls mitochondrial morphology.
Literature References
PubMed ID Title Journal Year
31695197 Lipid signalling drives proteolytic rewiring of mitochondria by YME1L

MacVicar, T, Ohba, Y, Nolte, H, Mayer, FC, Tatsuta, T, Sprenger, HG, Lindner, B, Zhao, Y, Li, J, Bruns, C, Krüger, M, Habich, M, Riemer, J, Schwarzer, R, Pasparakis, M, Henschke, S, Brüning, JC, Zamboni, N, Langer, T

Nature 2019
26923599 Reciprocal Degradation of YME1L and OMA1 Adapts Mitochondrial Proteolytic Activity during Stress

Rainbolt, TK, Lebeau, J, Puchades, C, Wiseman, RL

Cell Rep 2016
24315374 Stress-regulated translational attenuation adapts mitochondrial protein import through Tim17A degradation

Rainbolt, TK, Atanassova, N, Genereux, JC, Wiseman, RL

Cell Metab 2013
22262461 YME1L controls the accumulation of respiratory chain subunits and is required for apoptotic resistance, cristae morphogenesis, and cell proliferation

Stiburek, L, Cesnekova, J, Kostkova, O, Fornuskova, D, Vinsova, K, Wenchich, L, Houstek, J, Zeman, J

Mol Biol Cell 2012
30544562 Loss of Mitochondrial AAA Proteases AFG3L2 and YME1L Impairs Mitochondrial Structure and Respiratory Chain Biogenesis

Cesnekova, J, Rodinova, M, Hansikova, H, Zeman, J, Stiburek, L

Int J Mol Sci 2018
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Inferred From
YME1 binds COX2 (Saccharomyces cerevisiae)
Authored
May, B  (2023-06-27)
Reviewed
Aljghami, ME  (2023-11-04)
Houry, WA  (2023-11-04)
Morey, T  (2023-11-04)
Created
May, B  (2023-06-30)
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