Du, J., Hannon, G. J. (2002) The centrosomal kinase Aurora-A/STK15 interacts with a putative tumor suppressor NM23-H1. Nucleic Acids Research, 30 (24). pp. 5465-5475. ISSN 03051048 (ISSN)
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Abstract
Alterations in the activity of the centrosomal kinase, Aurora-A/STK15, have been implicated in centrosome amplification, genome instability and cellular transformation. How STK15 participates in all of these processes remains largely mysterious. The activity of STK15 is regulated by phosphorylation and ubiquitin-mediated degradation, and physically interacts with protein phosphatase 1 (PP1) and CDC20. However, the precise roles of these modifications and interactions have yet to be fully appreciated. Here we show that STK15 associates with a putative tumor and metastasis suppressor, NM23-H1. STK15 and NM23 were initially found to interact in yeast in a two-hybrid assay. Association of these proteins in human cells was confirmed by co-immunoprecipitation from cell lysates and biochemical fractionation indicating that STK15 and NM23-H1 are present in a stable, physical complex. Notably, SKT15 and NM23 both localize to centrosomes throughout the cell cycle irrespective of the integrity of the microtubule network in normal human fibroblasts.
| Item Type: | Paper |
|---|---|
| Uncontrolled Keywords: | cell cycle protein cell cycle protein 20 phosphoprotein phosphatase 1 phosphotransferase tumor suppressor protein ubiquitin unclassified drug bioassay cell cycle cell fractionation cell lysate cell transformation centrosome complex formation controlled study enzyme activity enzyme degradation enzyme localization enzyme phosphorylation enzyme regulation enzyme stability fibroblast gene amplification genetic stability human human cell immunoprecipitation metastasis microtubule nonhuman priority journal protein protein interaction review Saccharomyces cerevisiae two hybrid system Cell Line Hela Cells Humans Immunoblotting Microscopy, Fluorescence Monomeric GTP-Binding Proteins Nucleoside-Diphosphate Kinase Plasmids Precipitin Tests Protein-Serine-Threonine Kinases Transcription Factors Two-Hybrid System Techniques Saccharomyces |
| Subjects: | diseases & disorders > cancer bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > kinase bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > suppressor |
| CSHL Authors: | |
| Communities: | CSHL labs > Hannon lab |
| Depositing User: | Matt Covey |
| Date: | 2002 |
| Date Deposited: | 09 Jan 2013 16:56 |
| Last Modified: | 09 Jan 2013 16:56 |
| PMCID: | PMC140054 |
| Related URLs: | |
| URI: | https://repository.cshl.edu/id/eprint/26469 |
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