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Identification of residues which regulate activity of the STE20-related kinase hMINK
- Source :
- Biochemical and Biophysical Research Communications. 300:694-698
- Publication Year :
- 2003
- Publisher :
- Elsevier BV, 2003.
-
Abstract
- Activity of the STE20-related kinase hMINK was investigated. hMINK was expressed widely, though not ubiquitously, in human tissues: highest levels being found in haematopoietic tissues but also in brain, placenta, and lung. Mutagenesis revealed that T-191. and Y-193 in the substrate recognition loop of the catalytic domain were critical for kinase activity against exogenous substrates and autophosphorylation. A mutation on T-187 showed reduced enzymatic activity against exogenous substrates but retained autophosphorylationactivity. Phosphorylation was confirmed by the use of a phospho-specific T-187 antibody. hMINK activated the JNK signal transduction pathway and optimal JNK activation occurred when the C-terminus was deleted. In addition, overexpression of the C-terminal domain devoid of kinase activity also resulted in significant activation of the JNK pathway. These data suggest that hMINK requires an activation step that dissociates the C terminal, thereby freeing the catalytic domain to interact with substrates. Models for receptor-mediated activation of hMINK are discussed. (C) 2002 Elsevier Science (USA). All rights reserved.
- Subjects :
- Potassium Channels
Saccharomyces cerevisiae Proteins
Molecular Sequence Data
Biophysics
Protein Serine-Threonine Kinases
Mitogen-activated protein kinase kinase
Biology
Kidney
Biochemistry
Cell Line
Structure-Activity Relationship
Antibody Specificity
Humans
Amino Acid Sequence
Cloning, Molecular
Phosphorylation
Kinase activity
Protein kinase A
Molecular Biology
MAP kinase kinase kinase
Kinase
Autophosphorylation
Intracellular Signaling Peptides and Proteins
JNK Mitogen-Activated Protein Kinases
Cell Biology
MAP Kinase Kinase Kinases
Protein Structure, Tertiary
Organ Specificity
Potassium Channels, Voltage-Gated
Mutagenesis, Site-Directed
Cyclin-dependent kinase 9
Mitogen-Activated Protein Kinases
Signal transduction
Subjects
Details
- ISSN :
- 0006291X
- Volume :
- 300
- Database :
- OpenAIRE
- Journal :
- Biochemical and Biophysical Research Communications
- Accession number :
- edsair.doi.dedup.....0f8e8e4465758efe5bf2e721d3f95a97