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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2009-2-2
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pubmed:abstractText |
SGK1 (serum- and glucocorticoid-induced kinase 1) is a member of the AGC branch of the protein kinase family. Among well described functions of SGK1 is the regulation of epithelial transport through phosphorylation of the ubiquitin protein ligase Nedd4-2 (neuronal precursor cell expressed developmentally down-regulated 4-2). The activation of SGK1 has been widely accepted to be dependent on the phosphorylation of Thr256 in the activation loop and Ser422 in the hydrophobic motif near the C terminus. Here, we report the identification of two additional phosphorylation sites, Ser397 and Ser401. Both are required for maximum SGK1 activity induced by extracellular agents or by coexpression with other protein kinases, with the largest loss of activity from mutation of Ser397. Coexpression with active Akt1 increased the phosphorylation of Ser397 and thereby SGK1 kinase activity. SGK1 activation was further augmented by coexpression with the protein kinase WNK1 (with no lysine kinase 1). These findings reveal further complexity underlying the regulation of SGK1 activity.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-10191262,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-10574945,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-10675318,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-10828064,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-11376011,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-11500365,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-11914378,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-12080070,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-12218062,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-12417564,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-12488318,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-12495431,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-14611643,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-14707132,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-14729942,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-15262962,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-15568999,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-16006511,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-16081417,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-16301204,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-16619268,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-16817852,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-16895519,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-17015487,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-1737788,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-17446865,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-17965184,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-18570873,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-7545671,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-8455596,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-9271440,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19068477-9690513
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/AKT1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Endosomal Sorting Complexes...,
http://linkedlifedata.com/resource/pubmed/chemical/Immediate-Early Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Nedd4 ubiquitin protein ligases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-akt,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/WNK1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/serum-glucocorticoid regulated...
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
284
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3453-60
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:19068477-Amino Acid Motifs,
pubmed-meshheading:19068477-Endosomal Sorting Complexes Required for Transport,
pubmed-meshheading:19068477-Enzyme Activation,
pubmed-meshheading:19068477-HeLa Cells,
pubmed-meshheading:19068477-Humans,
pubmed-meshheading:19068477-Immediate-Early Proteins,
pubmed-meshheading:19068477-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:19068477-Mutation,
pubmed-meshheading:19068477-Phosphorylation,
pubmed-meshheading:19068477-Protein Transport,
pubmed-meshheading:19068477-Protein-Serine-Threonine Kinases,
pubmed-meshheading:19068477-Proto-Oncogene Proteins c-akt,
pubmed-meshheading:19068477-Ubiquitin-Protein Ligases
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pubmed:year |
2009
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pubmed:articleTitle |
Regulation of a third conserved phosphorylation site in SGK1.
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pubmed:affiliation |
Department of Pharmacology and Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas 75390-9041, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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