pubmed-article:12631736 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12631736 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
pubmed-article:12631736 | lifeskim:mentions | umls-concept:C0521447 | lld:lifeskim |
pubmed-article:12631736 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
pubmed-article:12631736 | lifeskim:mentions | umls-concept:C0033640 | lld:lifeskim |
pubmed-article:12631736 | lifeskim:mentions | umls-concept:C0288912 | lld:lifeskim |
pubmed-article:12631736 | lifeskim:mentions | umls-concept:C0525021 | lld:lifeskim |
pubmed-article:12631736 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:12631736 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:12631736 | lifeskim:mentions | umls-concept:C0599894 | lld:lifeskim |
pubmed-article:12631736 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:12631736 | lifeskim:mentions | umls-concept:C0086597 | lld:lifeskim |
pubmed-article:12631736 | lifeskim:mentions | umls-concept:C0205099 | lld:lifeskim |
pubmed-article:12631736 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:12631736 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:12631736 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:12631736 | pubmed:dateCreated | 2003-3-12 | lld:pubmed |
pubmed-article:12631736 | 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. | lld:pubmed |
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