Molecular Cloning and Characterization of a Novel Ste20-Related Protein Kinase Enriched in Neurons and Transporting Epithelia
Autor: | Hiroshi Ushiro, Kanjiro Suzuki, Tomonari Tsutsumi, Katsuma Nakano, Tetsuro Kayahara |
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Rok vydání: | 1998 |
Předmět: |
Proline
Molecular Sequence Data Biophysics Protein Serine-Threonine Kinases Biology Biochemistry Rats Sprague-Dawley medicine Animals Amino Acid Sequence Cloning Molecular Protein kinase A Molecular Biology Parietal cell Neurons Alanine chemistry.chemical_classification Base Sequence Kinase Brain Epithelial Cells Immunohistochemistry Rats Amino acid Cytosol medicine.anatomical_structure chemistry Choroid plexus Cell fractionation |
Zdroj: | Archives of Biochemistry and Biophysics. 355:233-240 |
ISSN: | 0003-9861 |
DOI: | 10.1006/abbi.1998.0736 |
Popis: | A novel cDNA encoding a protein kinase (termed PASK) was isolated from rat brain. The PASK catalytic domain was most similar to Ste20-related protein kinases, showing 45.5 and 39.2% amino acid identity with human SOK1 and yeast Sps1, respectively. The amino-terminal noncatalytic domain of 71 amino acids was rich in alanine and proline and contained several proline–alanine repeats. PASK was widely expressed in rat tissues but negligible in liver and skeletal muscle. Immunohistochemical analysis revealed that PASK was localized to a distinct set of cells including neurons, adrenal glomerulosa cells, and transporting epithelia such as epithelial cells of brain choroid plexus, distal tubule and collecting duct of kidney, duct of salivary gland, and parietal cells of stomach. Subcellular fractionation showed that PASK was present in both the cytosol and the Triton X-100-insoluble cytoskeletal fraction in brain. |
Databáze: | OpenAIRE |
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