DOI: 10.1128/MCB.22.19.6809-6819.2002
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PubMed
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History
- Received May 16, 2002
- Returned for modification June 25, 2002
- Accepted July 2, 2002
- Published online October 1, 2002.
Copyright & Usage
Copyright © 2002 American Society for Microbiology
Author Information
- Marta Prymakowska-Bosak1,
- Robert Hock2,
- Frédéric Catez1,
- Jae-Hwan Lim1,
- Yehudit Birger1,
- Hitoshi Shirakawa3,
- Kyung Lee1 and
- Michael Bustin1*
- 1Laboratory of Metabolism, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892
- 2Department of Cell and Developmental Biology, University of Wuerzburg, Wuerzburg, Germany
- 3Laboratory of Nutrition, Tohoku University, Sendai, Japan
- ↵* Corresponding author. Mailing address: Bldg. 37, Room 2D-21, NCI, NIH, Bethesda, MD 20892. Phone: (301) 496-5234. Fax: (301) 496-8419. E-mail: bustin{at}helix.nih.gov .
Article usage
- Top
- Article
- ABSTRACT
- MATERIALS AND METHODS
- In vitro phosphorylation of the recombinant HMGN1 proteins.
- Nuclear import assay.
- Microinjection of proteins into cells.
- Transfection into HmgN1−/− fibroblasts and HeLa cells.
- FRAP.
- GST pull down assay.
- Immunoprecipitation of HMGN1-14.3.3 complexes from HMGN1-FLAG-expressing HeLa cells.
- Confocal microscopy.
- RESULTS
- Nuclear import of HMGN is abolished by phosphorylation but not by negative charges.
- Phosphorylated HMGN1 binds to 14.3.3ζ protein.
- DISCUSSION
- Interaction of HMGN1 with 14.3.3 proteins.
- Regulating the nuclear entry of HMGN.
- Functional consequences of HMGN mitotic phosphorylation.
- ACKNOWLEDGMENTS
- FOOTNOTES
- REFERENCES
- Figures & Data
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