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Literature summary for 3.4.19.6 extracted from

  • Chavez-Gutierrez, L.; Bourdais, J.; Aranda, G.; Vargas, M.A.; Matta-Camacho, E.; Ducancel, F.; Segovia, L.; Joseph-Bravo, P.; Charli, J.L.
    A truncated isoform of pyroglutamyl aminopeptidase II produced by exon extension has dominant-negative activity (2005), J. Neurochem., 92, 807-817.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
detection of a RNA species derived from an alternative processing at the exon 14Ā–intron 14 boundary. The alternatively processed RNA encodes a shorter version of PPII (PPII*), lacking part of the C-terminal domain. PPII* is expressed in COS-7 (or C6 glioma) cells but it does not exhibit any PPII activity. Co-transfection of PPII and increasing amounts of PPII* expression vectors results in a dose-dependent reduction in PPII activity and the formation of covalent PPIIĀ–PPII* heterodimers. PPII* is therefore a powerful dominant-negative isoform of PPII, and heterodimerization may be its mechanism of action. Natural expression of shortened versions of M1 aminopeptidases may constitute a new mode of regulation of their activity Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
additional information detection of a RNA species derived from an alternative processing at the exon 14Ā–intron 14 boundary. The alternatively processed RNA encodes a shorter version of PPII (PPII*), lacking part of the C-terminal domain. PPII* is expressed in COS-7 (or C6 glioma) cells but it does not exhibit any PPII activity. Co-transfection of PPII and increasing amounts of PPII* expression vectors results in a dose-dependent reduction in PPII activity and the formation of covalent PPIIĀ–PPII* heterodimers. PPII* is therefore a powerful dominant-negative isoform of PPII, and heterodimerization may be its mechanism of action. Natural expression of shortened versions of M1 aminopeptidases may constitute a new mode of regulation of their activity Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Rattus norvegicus detection of a RNA species derived from an alternative processing at the exon 14Ā–intron 14 boundary. The alternatively processed RNA encodes a shorter version of PPII (PPII*), lacking part of the C-terminal domain. PPII* is expressed in COS-7 (or C6 glioma) cells but it does not exhibit any PPII activity. Co-transfection of PPII and increasing amounts of PPII* expression vectors results in a dose-dependent reduction in PPII activity and the formation of covalent PPIIĀ–PPII* heterodimers. PPII* is therefore a powerful dominant-negative isoform of PPII, and heterodimerization may be its mechanism of action. Natural expression of shortened versions of M1 aminopeptidases may constitute a new mode of regulation of their activity ?
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Organism

Organism UniProt Comment Textmining
Rattus norvegicus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information detection of a RNA species derived from an alternative processing at the exon 14Ā–intron 14 boundary. The alternatively processed RNA encodes a shorter version of PPII (PPII*), lacking part of the C-terminal domain. PPII* is expressed in COS-7 (or C6 glioma) cells but it does not exhibit any PPII activity. Co-transfection of PPII and increasing amounts of PPII* expression vectors results in a dose-dependent reduction in PPII activity and the formation of covalent PPIIĀ–PPII* heterodimers. PPII* is therefore a powerful dominant-negative isoform of PPII, and heterodimerization may be its mechanism of action. Natural expression of shortened versions of M1 aminopeptidases may constitute a new mode of regulation of their activity Rattus norvegicus ?
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?

Synonyms

Synonyms Comment Organism
PPII
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Rattus norvegicus