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The cAMP-dependent Protein Kinase Site (Ser312) Enhances Dorsal Nuclear Import through Facilitating Nuclear Localization Sequence/Importin Interaction (Q38334172)

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scientific article published on August 28, 1998

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English	The cAMP-dependent Protein Kinase Site (Ser312) Enhances Dorsal Nuclear Import through Facilitating Nuclear Localization Sequence/Importin Interaction	scientific article published on August 28, 1998

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scholarly article

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Europe PubMed Central

PubMed publication ID

2 September 2017

The cAMP-dependent protein kinase site (Ser312) enhances dorsal nuclear import through facilitating nuclear localization sequence/importin interaction (English)

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Europe PubMed Central

PubMed publication ID

2 September 2017

The cAMP-dependent Protein Kinase Site (Ser312) Enhances Dorsal Nuclear Import through Facilitating Nuclear Localization Sequence/Importin Interaction (English)

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10.1074/JBC.273.35.22745

https://api.crossref.org/works/10.1074/JBC.273.35.22745

6 January 2025

Drosophila proteins

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A9712906

6 January 2025

nuclear localization sequence

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6 January 2025

author name string

L. J. Briggs

1

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6 January 2025

D. Stein

2

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J. Goltz

3

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V. C. Corrigan

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A. Efthymiadis

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6 January 2025

S. Hübner

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D. A. Jans

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publication date

1 August 1998

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2 September 2017

28 August 1998

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6 January 2025

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http://www.jbc.org/article/S0021925818487832/pdf

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6 January 2025

https://api.elsevier.com/content/article/PII:S0021925818487832?httpAccept=text/xml

1 reference

10.1074/JBC.273.35.22745

https://api.crossref.org/works/10.1074/JBC.273.35.22745

6 January 2025

https://api.elsevier.com/content/article/PII:S0021925818487832?httpAccept=text/plain

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10.1074/JBC.273.35.22745

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6 January 2025

https://syndication.highwire.org/content/doi/10.1074/jbc.273.35.22745

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10.1074/JBC.273.35.22745

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Journal of Biological Chemistry

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2 September 2017

273

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2 September 2017

35

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2 September 2017

22745-22752

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2 September 2017

Proteins controlling the nuclear uptake of NF-kappa B, Rel and dorsal

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The regulation of protein transport to the nucleus by phosphorylation

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In vitro activation and nuclear translocation of NF-kappa B catalyzed by cyclic AMP-dependent protein kinase and protein kinase C.

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NF-kappa B: a pleiotropic mediator of inducible and tissue-specific gene control

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A protein kinase-A recognition sequence is structurally linked to transformation by p59v-rel and cytoplasmic retention of p68c-rel

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NF-AT-AP-1 and Rel-bZIP: hybrid vigor and binding under the influence

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The role of phosphorylation and the CDC28 protein kinase in cell cycle-regulated nuclear import of the S. cerevisiae transcription factor SWI5.

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Cyclin-dependent kinase site-regulated signal-dependent nuclear localization of the SW15 yeast transcription factor in mammalian cells

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p34cdc2-mediated phosphorylation at T124 inhibits nuclear import of SV-40 T antigen proteins

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I kappa B interacts with the nuclear localization sequences of the subunits of NF-kappa B: a mechanism for cytoplasmic retention

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Intramolecular masking of the nuclear location signal and dimerization domain in the precursor for the p50 NF-kappa B subunit

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A consensus cAMP-dependent protein kinase (PK-A) site in place of the CcN motif casein kinase II site simian virus 40 large T-antigen confers PK-A-mediated regulation of nuclear import

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Phosphorylation on protein kinase C sites inhibits nuclear import of lamin B2.

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The protein kinase CK2 site (Ser111/112) enhances recognition of the simian virus 40 large T-antigen nuclear localization sequence by importin

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Selective nuclear transport of the Drosophila morphogen dorsal can be established by a signaling pathway involving the transmembrane protein Toll and protein kinase A

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Regulation of dorsal in cultured cells by Toll and tube: tube function involves a novel mechanism

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Characterization of the Drosophila cactus locus and analysis of interactions between cactus and dorsal proteins

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Regulated nuclear import of the Drosophila rel protein dorsal: structure-function analysis

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Interactions of a Rel protein with its inhibitor.

1 reference

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Dissociation of the dorsal-cactus complex and phosphorylation of the dorsal protein correlate with the nuclear localization of dorsal

1 reference

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Dorsal, a Drosophila Rel-like protein, is phosphorylated upon activation of the transmembrane protein Toll

1 reference

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Relocalization of Drosophila dorsal protein can be induced by a rise in cytoplasmic calcium concentration and the expression of constitutively active but not wild-type Toll receptors

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A gradient of cactus protein degradation establishes dorsoventral polarity in the Drosophila embryo

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A conserved signaling pathway: the Drosophila toll-dorsal pathway

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Dorsal, an embryonic polarity gene in Drosophila, is homologous to the vertebrate proto-oncogene, c-rel

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A gradient of nuclear localization of the dorsal protein determines dorsoventral pattern in the Drosophila embryo

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A gradient of cytoplasmic Cactus degradation establishes the nuclear localization gradient of the dorsal morphogen in Drosophila

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Disulfide cross-linking in crude embryonic lysates reveals three complexes of the Drosophila morphogen dorsal and its inhibitor cactus

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Genetic investigation of cAMP-dependent protein kinase function in Drosophila development

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Kinetic characterization of the human retinoblastoma protein bipartite nuclear localization sequence (NLS) in vivo and in vitro. A comparison with the SV40 large T-antigen NLS

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Regulation of protein transport to the nucleus: central role of phosphorylation

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7

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Govind

publication date

1991

1 reference

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The rate of nuclear cytoplasmic protein transport is determined by the casein kinase II site flanking the nuclear localization sequence of the SV40 T-antigen

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Nucleoplasmin associates with and is phosphorylated by casein kinase II.

20

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10.1074/JBC.273.35.22745

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

ResearchGate publication ID

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