Isolation and characterization of a novel serine threonine kinase gene on chromosome 3p22-21.3

Abstract

Through large-scale DNA sequencing of a genomic region on chromosome 3p22-p21.3, we isolated a novel gene encoding a 527-amino-acid protein. Its 18 exons spanned a genomic region of about 90 kilobases, and the 4536-nucleotide cDNA contained an open reading frame of 1581 base pairs. The gene was expressed in all 16 human tissues examined by Northern blotting. The amino acid sequence of the predicted protein was 39% identical to that of human SOK1 (Ste20/oxidant stress response kinase-1), a molecule that is activated by oxidative stress. In view of its significant similarity to SOK1, we suspect that the novel gene, which we named OSR1, is a member of the SOK family of kinases in terms of function.

The regulation of salt transport and blood pressure by the WNK-SPAK/OSR1 signalling pathway

“…In addition, SPAK possesses a unique 48-amino-acid N-terminal extension that mainly comprises Ala and Pro residues (24 and 12 residues, respectively). SPAK and OSR1 were originally identified through various cloning screens, are widely expressed and arose through gene duplication during vertebrate evolution (Delpire and Gagnon, 2008;Johnston et al, 2000;Tamari et al, 1999;Ushiro et al, 1998).…”

Crystal structure of domain‐swapped STE20 OSR1 kinase domain

“…OSR1 was originally identified and named because of its sequence similarity to SOK1 (Ste20/oxidant stress responsive kinase-1). 10 OSR1 is widely expressed but highest in heart and skeletal muscle. 10 The distribution of OSR1 at the organ/tissue level largely overlaps with SPAK.…”

“…10 OSR1 is widely expressed but highest in heart and skeletal muscle. 10 The distribution of OSR1 at the organ/tissue level largely overlaps with SPAK. 4,7 OSR1 and SPAK have been suggested to be coupled to cellular events such as cell differentiation, cytoskeleton rearrangement, cell proliferation, and transformation.…”

Cloning and identification ofNS5ATP2gene and its spliced variant transactivated by hepatitis C virus non-structural protein 5A

“…Although mucins mainly affect cell adhesion and ligand binding, several membrane mucins have also been documented to trigger cell death or inhibit cell proliferation, such as CD43 (leukosialin, sialophorin), CD162 (PSGL-1), and CD164 (MGC-24v) [23] . Likewise, serine/threonine kinase, cadherin-associated protein, adenylyl cyclase-associated protein, mitogen-activated protein kinase phosphatase involving in cell cycle regulation, and cell growth may be correlated with hepatocarcinogenesis of NS5A protein [24][25][26][27][28] . Alternative pre-mRNA splicing is a fundamental mechanism for differential gene expression that has been reported to regulate the tissue distribution, the intracellular localization, and the activity of different protein kinases.…”