Multiple translational isoforms give functional specificity to serum- and glucocorticoid-induced kinase 1

Serum- and glucocorticoid-induced kinase 1 is a ubiquitous kinase that regulates diverse processes such as ion transport and cell survival. We report that a single SGK1 mRNA produces isoforms with different N-termini owing to alternative translation initiation. The long isoforms, 49 and 47 kDa, are...

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Bibliographic Details
Published in:Molecular biology of the cell 2007-06, Vol.18 (6), p.2072-2080
Main Authors: Arteaga, Maria Francisca, Alvarez de la Rosa, Diego, Alvarez, Jose A, Canessa, Cecilia M
Format: Article
Language:English
Subjects:
Animals
Cell Line
Humans
Immediate-Early Proteins - chemistry
Immediate-Early Proteins - genetics
Immediate-Early Proteins - metabolism
Isoenzymes - chemistry
Isoenzymes - genetics
Isoenzymes - metabolism
Mice
Molecular Weight
Protein Biosynthesis
Protein-Serine-Threonine Kinases - chemistry
Protein-Serine-Threonine Kinases - genetics
Protein-Serine-Threonine Kinases - metabolism
RNA, Messenger - genetics
RNA, Messenger - metabolism
Substrate Specificity
Tissue Distribution
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Summary:Serum- and glucocorticoid-induced kinase 1 is a ubiquitous kinase that regulates diverse processes such as ion transport and cell survival. We report that a single SGK1 mRNA produces isoforms with different N-termini owing to alternative translation initiation. The long isoforms, 49 and 47 kDa, are the most abundant, localize to the ER membrane, exhibit rapid turnover, their expression is decreased by ER stress, activate the epithelial sodium channel (ENaC) and translocate FoxO3a transcriptional factors from the nucleus to the cytoplasm. The short isoforms, 45 and 42 kDa, localize to the cytoplasm and nucleus, exhibit long half-life and phosphorylate glycogen synthase kinase-3beta. The data indicate that activation of Sgk1 in different cellular compartments is key to providing functional specificity to Sgk1 signaling pathways. We conclude that the distinct properties and functional specialization of Sgk1 given by the N-terminus confer versatility of function while maintaining the same core kinase domain.
ISSN:1059-1524
1939-4586
DOI:10.1091/mbc.E06-10-0968