Molecular cloning and characterization of a novel Ste20-related protein kinase enriched in neurons and transporting epithelia

被引:71
作者
Ushiro, H [1 ]
Tsutsumi, T [1 ]
Suzuki, K [1 ]
Kayahara, T [1 ]
Nakano, K [1 ]
机构
[1] Mie Univ, Sch Med, Dept Anat, Tsu, Mie 5148507, Japan
关键词
Ste20; family; protein kinase; transporting epithelia; choroid plexus; distal tubule of kidney; collecting duct of kidney; parietal cell; glomerulosa cell;
D O I
10.1006/abbi.1998.0736
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 1998 Academic Press.
引用
收藏
页码:233 / 240
页数:8
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