YME1L1 binds mitochondrial intermembrane space proteins

Stable Identifier
R-HSA-9839772
Type
Reaction [binding]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
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 processively unfolded and translocated in an ATP-dependent reaction to a central pore formed by the protease domains of the YME1L1 complex.
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

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

Cell Metab. 2013
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
29301859 PARL partitions the lipid transfer protein STARD7 between the cytosol and mitochondria

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

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

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

Proc Natl Acad Sci U S A 2020
Participants
Participates
Inferred From
Authored
Reviewed
Created
Cite Us!