Abstract
Kinectin has been characterized as the first known receptor for the molecular motor kinesin, which is critically involved in microtubule-based vesicle transport and membrane trafficking. Here we identify kinectin as a target for caspase-mediated proteolysis during apoptosis. Treatment of cells with diverse apoptotic stimuli including TNF, anti-Fas, anticancer drugs, gamma-radiation or ceramide leads to rapid proteolytic cleavage of the 160-kDa form of kinectin to a 120-kDa fragment. Evidence is provided that kinectin cleavage is mediated by caspase 7.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Chloromethyl Ketones / pharmacology
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Antibodies / pharmacology
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Apoptosis / drug effects
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Apoptosis / radiation effects
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Caspase 7
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Caspases / drug effects
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Caspases / genetics
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Caspases / metabolism*
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Cell-Free System
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Ceramides / pharmacology
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Cisplatin / pharmacology
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Cysteine Proteinase Inhibitors / pharmacology
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Daunorubicin / pharmacology
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Etoposide / pharmacology
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HeLa Cells / drug effects
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HeLa Cells / metabolism
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HeLa Cells / radiation effects
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Humans
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Jurkat Cells / drug effects
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Jurkat Cells / metabolism
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Jurkat Cells / radiation effects
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Membrane Proteins*
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Receptors, Cell Surface / metabolism*
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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fas Receptor / immunology
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fas Receptor / metabolism
Substances
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Amino Acid Chloromethyl Ketones
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Antibodies
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Ceramides
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Cysteine Proteinase Inhibitors
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KTN1 protein, human
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Membrane Proteins
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N-acetyl-tyrosyl-valyl-alanyl-aspartyl chloromethyl ketone
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Receptors, Cell Surface
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Recombinant Proteins
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fas Receptor
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Etoposide
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CASP7 protein, human
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Caspase 7
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Caspases
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Cisplatin
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Daunorubicin