Search results for PMPCA

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Species

Types

Compartments

Reaction types

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Protein (1 results from a total of 1)

PMPCA

Identifier: R-HSA-1299450
Species: Homo sapiens
Compartment: mitochondrial matrix
Primary external reference: UniProt: PMPCA: Q10713

Reaction (4 results from a total of 4)

PMPCA:PMPCB cleaves the transit peptide of proSMDT1 (proEMRE)

Identifier: R-HSA-8949649
Species: Homo sapiens
Compartment: mitochondrial inner membrane
The mitochondrial endopeptidase PMPCA:PMPCB cleaves the transit peptide of proSMDT1 (proEMRE) yielding SMDT1 (Konig et al. 2016). Mature SMDT1 is assembled into the MCU complex where it serves to bridge the MCU pore and the MCU regulators MICU1 and MICU2 (or MICU3 in neurons).

YME1L1 proteolyzes unassembled proSMDT1

Identifier: R-HSA-8949668
Species: Homo sapiens
Compartment: mitochondrial inner membrane
ProSMDT1 (proEMRE) that is not bound by C2orf47:AFG3L2 and processed by PMPCA,B is proteolyzed by YME1L1 (Konig et al. 2016) in a large complex containing STOML2 (SLP2) and PARL (Wai et al. 2016). Thus YME1L1 appears to prevent accumulation of proSMDT1.

LONP1 degrades mitochondrial inner membrane proteins

Identifier: R-HSA-9838004
Species: Homo sapiens
Compartment: mitochondrial inner membrane
After binding a substrate protein, LONP1 degrades the substrate protein using an ATP-dependent mechanism in which ATP hydrolysis causes translocation of the substrate protein to the protease site (Ambro et al. 2014, Mohammed et al. 2022). LONP1 predominantly cleaves peptide bonds adjacent to hydrophobic amino acid residues (He et al. 2018). LONP1 binds 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).

LONP1 binds mitochondrial inner membrane proteins

Identifier: R-HSA-9837978
Species: Homo sapiens
Compartment: mitochondrial inner membrane, mitochondrial matrix
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).
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