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Literature summary for 2.3.1.97 extracted from

  • Perinpanayagam, M.; Beauchamp, E.; Martin, D.; Sim, J.; Yap, M.; Berthiaume, L.
    Regulation of co-and post-translational myristoylation of proteins during apoptosis: Interplay of N-myristoyltransferases and caspases (2013), FASEB J., 27, 811-821.
    View publication on PubMed
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Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol predominantly cytosolic isoform NMT2 relocalizes to membranes when cleaved by caspases Homo sapiens 5829
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membrane caspase-mediated cleavage of the predominantly membrane bound isoform NMT1 removes a polybasic domain stretch and leads to a cytosolic relocalization Homo sapiens 16020
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Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
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Source Tissue

Source Tissue Comment Organism Textmining
HeLa cell
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 Homo sapiens
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JURKAT cell
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 Homo sapiens
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General Information

General Information Comment Organism
metabolism both N-myristoyltransferases NMT1 and NMT2 are cleaved during apoptosis. The caspase-3- or -8-mediated cleavage of NMT1 at Asp72 precedes the cleavage of NMT2 by caspase-3 mainly at Asp25. The cleavage of NMTs does not significantly affect their activity in apoptotic cells until the 8 h time point. The cleavage of the predominantly membrane bound NMT1 removes a polybasic domain stretch and leads to a cytosolic relocalization, whereas predominantly cytosolic NMT2 relocalizes to membranes when cleaved after the removal of a negatively charged domain Homo sapiens