Reactome | LONP1 binds mitochondrial inner membrane proteins

LONP1 binds mitochondrial inner membrane proteins

Stable Identifier

R-HSA-9837978

Type

Reaction [binding]

Species

Homo sapiens

Compartment

mitochondrial inner membrane, mitochondrial matrix

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

LONP1 binds mitochondrial inner membrane proteins

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

LONP1 binds a substrate protein in an ATP-independent manner and then degrades the the substrate protein using an ATP-dependent mechanism in which ATP hydrolysis translocates the substrate protein to the protease active site (Ambro et al. 2014, Shin et al. 2021, Mohammed et al. 2022). The binding of proteins to LONP1 can allosterically stimulate its ATPase activity (inferred from bacterial Lon proteases in Waxman et al. 1986, Lin et al. 2016). LONP1 binds, unfolds, and degrades several mitochondrial inner membrane proteins (Ondrovicova et al. 2005, Lee et al. 2021), including the mitochondrial processing peptidase subunit PMPCA (Ondrovicova et al. 2005).

Literature References

PubMed ID	Title	Journal	Year
33637676	LONP1 and ClpP cooperatively regulate mitochondrial proteostasis for cancer cell survival Lee, YG, Kim, HW, Nam, Y, Shin, KJ, Lee, YJ, Park, DH, Rhee, HW, Seo, JK, Chae, YC	Oncogenesis	2021
15870080	Cleavage site selection within a folded substrate by the ATP-dependent lon protease Ondrovicová, G, Liu, T, Singh, K, Tian, B, Li, H, Gakh, O, Perecko, D, Janata, J, Granot, Z, Orly, J, Kutejova, E, Suzuki, CK	J Biol Chem	2005
35870450	Catalytic cycling of human mitochondrial Lon protease Mohammed, I, Schmitz, KA, Schenck, N, Balasopoulos, D, Topitsch, A, Maier, T, Abrahams, JP	Structure	2022