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rdf:type |
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lifeskim:mentions |
umls-concept:C0017262,
umls-concept:C0017471,
umls-concept:C0024554,
umls-concept:C0086206,
umls-concept:C0185117,
umls-concept:C0205314,
umls-concept:C0679622,
umls-concept:C0760772,
umls-concept:C1157562,
umls-concept:C1414270,
umls-concept:C1424862,
umls-concept:C1521840,
umls-concept:C2911684
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pubmed:issue |
1-4
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pubmed:dateCreated |
2007-6-27
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pubmed:abstractText |
PASKIN links energy flux and protein synthesis in yeast, regulates glycogen synthesis in mammals, and has been implicated in glucose-stimulated insulin production in pancreatic beta-cells. Using newly generated monoclonal antibodies, PASKIN was localized in the nuclei of human testis germ cells and in the midpiece of human sperm tails. A speckle-like nuclear pattern was observed for endogenous PASKIN in HeLa cells in addition to its cytoplasmic localization. By yeast two-hybrid screening, we identified the multifunctional eukaryotic translation elongation factor eEF1A1 as a novel interaction partner of PASKIN. This interaction was mapped to the PAS A and kinase domains of PASKIN and to the C-terminus of eEF1A1 using mammalian two-hybrid and GST pull-down assays. Kinase assays, mass spectrometry and site-directed mutagenesis revealed PASKIN auto-phosphorylation as well as eEF1A1 target phosphorylation mainly but not exclusively at Thr432. Wild-type but not kinase-inactive PASKIN increased the in vitro translation of a reporter cRNA. Whereas eEF1A1 did not localize to the nucleus, it co-localizes with PASKIN to the cytoplasm of HeLa cells. The two proteins also showed a remarkably similar localization in the midpiece of the sperm tail. These data suggest regulation of eEF1A1 by PASKIN-dependent phosphorylation in somatic as well as in sperm cells.
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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 |
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pubmed:status |
MEDLINE
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pubmed:issn |
1015-8987
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pubmed:author |
pubmed-author:BarthSandraS,
pubmed-author:BorterEmanuelaE,
pubmed-author:CamenischGieriG,
pubmed-author:EckhardtKatrinK,
pubmed-author:HunzikerPeterP,
pubmed-author:KatschinskiDörthe MDM,
pubmed-author:PaaschUweU,
pubmed-author:ReissmannJanaJ,
pubmed-author:SchlafliPhilippP,
pubmed-author:SpielmannPatrickP,
pubmed-author:StengelPetraP,
pubmed-author:StiehlDaniel PDP,
pubmed-author:TrogerJulianeJ,
pubmed-author:WagnerKlaus FKF,
pubmed-author:WengerRoland HRH
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pubmed:issnType |
Print
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pubmed:volume |
20
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
227-40
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:17595531-Antibodies, Monoclonal,
pubmed-meshheading:17595531-Base Sequence,
pubmed-meshheading:17595531-Cell Nucleus,
pubmed-meshheading:17595531-Cell-Free System,
pubmed-meshheading:17595531-Cytoplasm,
pubmed-meshheading:17595531-DNA Primers,
pubmed-meshheading:17595531-Gene Expression,
pubmed-meshheading:17595531-HeLa Cells,
pubmed-meshheading:17595531-Humans,
pubmed-meshheading:17595531-Male,
pubmed-meshheading:17595531-Peptide Elongation Factor 1,
pubmed-meshheading:17595531-Phosphorylation,
pubmed-meshheading:17595531-Protein Biosynthesis,
pubmed-meshheading:17595531-Protein Interaction Mapping,
pubmed-meshheading:17595531-Protein Structure, Tertiary,
pubmed-meshheading:17595531-Protein-Serine-Threonine Kinases,
pubmed-meshheading:17595531-Recombinant Proteins,
pubmed-meshheading:17595531-Sperm Tail,
pubmed-meshheading:17595531-Spermatozoa,
pubmed-meshheading:17595531-Transfection,
pubmed-meshheading:17595531-Two-Hybrid System Techniques
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pubmed:year |
2007
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pubmed:articleTitle |
Male germ cell expression of the PAS domain kinase PASKIN and its novel target eukaryotic translation elongation factor eEF1A1.
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pubmed:affiliation |
Institute of Physiology and Zürich Center for Integrative Human Physiology, University of Zürich, Zürich, Switzerland.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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