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Literature summary for 3.4.21.105 extracted from

  • Sik, A.; Passer, B.J.; Koonin, E.V.; Pellegrini, L.
    Self-regulated cleavage of the mitochondrial intramembrane-cleaving protease PARL yields Pbeta, a nuclear-targeted peptide (2004), J. Biol. Chem., 279, 15323-15329.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
HEK 293 cells transfected with a FLAG-tagged PARL construct Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens regulated intramembrane proteolysis in which the putative signaling moiety is part of the intramembrane-cleaving protease itself. Cytosolic N-terminal domain of PARL is cleaved at positions 52–53 (alpha-site) and 77–78 (beta-site). Whereas alpha-cleavage is constitutive and removes the mitochondrial targeting sequence, beta-cleavage appears to be developmentally controlled and dependent on PARL intramembrane-cleaving protease activity supplied in trans. The beta-cleavage of PARL liberates Pbeta, a nuclear targeted peptide whose sequence is conserved only in mammals. Thus, in addition to its evolutionarily conserved function in regulating mitochondrial dynamics, PARL might mediate a mammalian-specific, developmentally regulated mitochondria-to-nuclei signaling through regulated proteolysis of its N-terminus and release of the Pbeta peptide ?
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Organism

Organism UniProt Comment Textmining
Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information regulated intramembrane proteolysis in which the putative signaling moiety is part of the intramembrane-cleaving protease itself. Cytosolic N-terminal domain of PARL is cleaved at positions 52–53 (alpha-site) and 77–78 (beta-site). Whereas alpha-cleavage is constitutive and removes the mitochondrial targeting sequence, beta-cleavage appears to be developmentally controlled and dependent on PARL intramembrane-cleaving protease activity supplied in trans. The beta-cleavage of PARL liberates Pbeta, a nuclear targeted peptide whose sequence is conserved only in mammals. Thus, in addition to its evolutionarily conserved function in regulating mitochondrial dynamics, PARL might mediate a mammalian-specific, developmentally regulated mitochondria-to-nuclei signaling through regulated proteolysis of its N-terminus and release of the Pbeta peptide Homo sapiens ?
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?

Synonyms

Synonyms Comment Organism
PARL
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Homo sapiens
presenilins-associated rhomboid-like protein
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Homo sapiens