YME1L1 degrades mitochondrial intermembrane space proteins

Stable Identifier
R-HSA-9839751
Type
Reaction [uncertain]
Species
Homo sapiens
Compartment
mitochondrial inner membrane
ReviewStatus
5/5
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YME1L1 degrades mitochondrial intermembrane space proteins
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YME1L1 (YME1L, i-AAA) is a hexameric 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). Each monomer of YME1L1 contains a membrane-proximal ATPase, protein unfolding domain and a membrane-distal protease domain (inferred from the yeast homolog in Puchades et al. 2017). The substrate protein enters a central channel formed by the ATPase domains, where it is unfolded and translocated into the pore formed by the protease domains (inferred from the yeast homolog in Puchades et al. 2017). Within the protease pore, it is hydrolyzed by zinc cofactors bound to the protease domains (inferred from the yeast homolog in Puchades et al. 2017).
YME1L1 binds, unfolds, and degrades specific intermembrane space proteins, including STARD7 (Saita et al. 2018, MacVicar et al. 2019), TRIAP1 (MacVicar et al. 2019), PRELID1 (Potting et al. 2013, MacVicar et al. 2019), and CHCHD2 (also called MNRR) (Aras et al. 2020).
Literature References
PubMed ID Title Journal Year
23931759 TRIAP1/PRELI complexes prevent apoptosis by mediating intramitochondrial transport of phosphatidic acid

Tatsuta, T, König, T, Aaltonen, MJ, Langer, T, Wai, T, Potting, C, Haag, M

Cell Metab. 2013
31695197 Lipid signalling drives proteolytic rewiring of mitochondria by YME1L

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

Nature 2019
29301859 PARL partitions the lipid transfer protein STARD7 between the cytosol and mitochondria

Tatsuta, T, Lampe, PA, Ohba, Y, König, T, Saita, S, Langer, T

EMBO J 2018
33257573 Mitochondrial Nuclear Retrograde Regulator 1 (MNRR1) rescues the cellular phenotype of MELAS by inducing homeostatic mechanisms

Zhang, K, Gladyck, S, Somayajulu-Nitu, M, Grossman, LI, Wallace, DC, Aras, S, Purandare, N

Proc Natl Acad Sci U S A 2020
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Catalyst Activity

ATP-dependent peptidase activity of YME1L1:substrate protein (mitochondrial intermembrane space) [mitochondrial inner membrane]

Physical Entity
YME1L1:substrate protein (mitochondrial intermembrane space) [mitochondrial inner membrane] (Homo sapiens)
Activity
ATP-dependent peptidase activity (GO:0004176)
Inferred From
YME1 degrades TIM10 (Saccharomyces cerevisiae)
Authored
May, B  (2023-07-09)
Reviewed
Houry, WA  (2023-11-04)
Morey, T  (2023-11-04)
Aljghami, ME  (2023-11-04)
Created
May, B  (2023-07-10)
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