Cleavage of the nuclear matrix protein NuMA during apoptosis.
NuMA is a component of the nuclear matrix which may play a structural role in the architecture of the interphase nucleus. During apoptosis NuMA is redistributed within the nucleus and is proteolysed from a 238-kDa form to a 180- to 200-kDa form. Here we show that the cleavage site leading to the stable fragment occurs between residues 1701 and 1725. Both the changes in morphology associated with apoptosis and the cleavage of NuMA were retarded by treatment with TPCK but not by treatment by other protease inhibitors including ICE inhibitor II.
Gueth-Hallonet
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Department of Biochemistry, Max Planck Institute for Biophysical Chemistry, Goettingen, Germany.
Weber
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Osborn
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D000818:Animals; D034961:Antigens, Nuclear; D017209:Apoptosis / Q000187:drug effects; D018797:Cell Cycle Proteins; D006224:Cricetinae; D005455:Fluorescent Antibody Technique; D006367:HeLa Cells; D006801:Humans; D034521:Nuclear Matrix-Associated Proteins; D009687:Nuclear Proteins / Q000235:genetics / Q000378:metabolism*; D011480:Protease Inhibitors / Q000494:pharmacology; D011499:Protein Processing, Post-Translational; D011994:Recombinant Proteins / Q000378:metabolism; D008941:Spindle Apparatus / Q000378:metabolism*; D014162:Transfection
D034961:Antigens, Nuclear; D018797:Cell Cycle Proteins; C050045:NUMA1 protein, human; D034521:Nuclear Matrix-Associated Proteins; D009687:Nuclear Proteins; D011480:Protease Inhibitors; D011994:Recombinant Proteins