Abstract
The mixed lineage kinase (MLK) family is a recently described protein kinase family. The MLKs contain a kinase domain followed by a dual leucine zipper-like motif. We previously reported the molecular cloning of LZK (leucine zipper-bearing kinase), a novel MLK, and that LZK activated the c-Jun NH2 terminal kinase (JNK)/stress-activated protein kinase (SAPK) pathway through MKK7 in cells. Here, we reveal that LZK forms dimers/oligomers through its dual leucine zipper-like motif, and that this is necessary for activation of the JNK/SAPK pathway. We also identify the C-terminal functional region of LZK, which is indispensable for the activation of SEK1, but not that of MKK7.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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COS Cells
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Dimerization
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Enzyme Activation
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Gene Deletion
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Humans
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JNK Mitogen-Activated Protein Kinases
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Leucine Zippers*
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MAP Kinase Kinase 4*
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MAP Kinase Kinase 7
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MAP Kinase Kinase Kinases / chemistry*
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MAP Kinase Kinase Kinases / genetics
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MAP Kinase Kinase Kinases / metabolism*
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Mitogen-Activated Protein Kinase Kinases / genetics
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Mitogen-Activated Protein Kinase Kinases / metabolism
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Mitogen-Activated Protein Kinases / genetics
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Mitogen-Activated Protein Kinases / metabolism
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Precipitin Tests
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Protein Binding
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Protein Structure, Tertiary
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Recombinant Fusion Proteins / metabolism
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Signal Transduction
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Transfection
Substances
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Recombinant Fusion Proteins
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JNK Mitogen-Activated Protein Kinases
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Mitogen-Activated Protein Kinases
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MAP Kinase Kinase Kinases
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MAP3K13 protein, human
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MAP Kinase Kinase 4
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MAP Kinase Kinase 7
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MAP2K4 protein, human
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MAP2K7 protein, human
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Mitogen-Activated Protein Kinase Kinases