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rdf:type |
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lifeskim:mentions |
umls-concept:C0031727,
umls-concept:C0033640,
umls-concept:C0086597,
umls-concept:C0205099,
umls-concept:C0288912,
umls-concept:C0521447,
umls-concept:C0524637,
umls-concept:C0525021,
umls-concept:C0599894,
umls-concept:C0851285,
umls-concept:C1514562,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
3
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pubmed:dateCreated |
2003-3-12
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pubmed:abstractText |
The transcriptionally regulated serum and glucocorticoid inducible protein kinase (Sgk) is localized to the nucleus in a serum-dependent manner, and a yeast two-hybrid genetic screen uncovered a specific interaction between Sgk and the importin-alpha nuclear import receptor. In vitro GST pull down assays demonstrated a strong and direct association of importin-alpha with endogenous Sgk and exogenously expressed HA-tagged Sgk, whereas both components coimmunoprecipitate and colocalize to the nucleus after serum stimulation. Consistent with an active mechanism of nuclear localization, the nuclear import of HA-Sgk in permeabilized cells required ATP, cytoplasm, and a functional nuclear pore complex. Ectopic addition of a 107 amino acid carboxy-terminal fragment of importin-alpha, which contains the Sgk binding region, competitively inhibited the ability of endogenous importin-alpha to import Sgk into nuclei in vitro. Mutagenesis of lysines by alanine substitution defined a KKAILKKKEEK sequence within the central domain of Sgk between amino acids 131-141 that functions as a nuclear localization signal (NLS) required for the in vitro interaction with importin-alpha and for nuclear import of full-length Sgk in cultured cells. The serum-induced nuclear import of Sgk requires the NLS-dependent recognition of Sgk by importin-alpha as well as the PI3-kinase-dependent phosphorylation of Sgk. Our results define a new role importin-alpha in the stimulus-dependent control of signal transduction by nuclear localized protein kinases.
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pubmed:grant |
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pubmed:commentsCorrections |
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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/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media, Serum-Free,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Immediate-Early Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Sorting Signals,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoplasmic and Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/alpha Karyopherins,
http://linkedlifedata.com/resource/pubmed/chemical/karyopherin alpha 2,
http://linkedlifedata.com/resource/pubmed/chemical/serum-glucocorticoid regulated...
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1059-1524
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
14
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1221-39
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pubmed:dateRevised |
2011-11-2
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pubmed:meshHeading |
pubmed-meshheading:12631736-Active Transport, Cell Nucleus,
pubmed-meshheading:12631736-Adenosine Triphosphate,
pubmed-meshheading:12631736-Animals,
pubmed-meshheading:12631736-Catalytic Domain,
pubmed-meshheading:12631736-Cell Line,
pubmed-meshheading:12631736-Culture Media, Serum-Free,
pubmed-meshheading:12631736-Enzyme Inhibitors,
pubmed-meshheading:12631736-Humans,
pubmed-meshheading:12631736-Immediate-Early Proteins,
pubmed-meshheading:12631736-Nuclear Pore,
pubmed-meshheading:12631736-Nuclear Proteins,
pubmed-meshheading:12631736-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:12631736-Protein Binding,
pubmed-meshheading:12631736-Protein Sorting Signals,
pubmed-meshheading:12631736-Protein-Serine-Threonine Kinases,
pubmed-meshheading:12631736-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:12631736-Recombinant Fusion Proteins,
pubmed-meshheading:12631736-Signal Transduction,
pubmed-meshheading:12631736-Two-Hybrid System Techniques,
pubmed-meshheading:12631736-alpha Karyopherins
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pubmed:year |
2003
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pubmed:articleTitle |
Importin-alpha mediates the regulated nuclear targeting of serum- and glucocorticoid-inducible protein kinase (Sgk) by recognition of a nuclear localization signal in the kinase central domain.
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pubmed:affiliation |
Department of Molecular and Cell Biology and The Cancer Research Laboratory, University of California at Berkeley, 94720-3200, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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