Journal article
Nuclear gamma-Tubulin Associates With Nucleoli and Interacts With Tumor Suppressor Protein C53
Journal of cellular physiology, v 227(1), pp 367-382
01 Jan 2012
PMID: 21465471
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
gamma-Tubulin is assumed to be a typical cytosolic protein necessary for nucleation of microtubules from microtubule organizing centers. Using immunolocalization and cell fractionation techniques in combination with siRNAi and expression of FLAG-tagged constructs, we have obtained evidence that gamma-tubulin is also present in nucleoli of mammalian interphase cells of diverse cellular origins. Immunoelectron microscopy has revealed gamma-tubulin localization outside fibrillar centers where transcription of ribosomal DNA takes place. gamma-Tubulin was associated with nucleolar remnants after nuclear envelope breakdown and could be translocated to nucleoli during mitosis. Pretreatment of cells with leptomycin B did not affect the distribution of nuclear gamma-tubulin, making it unlikely that rapid active transport via nuclear pores participates in the transport of gamma-tubulin into the nucleus. This finding was confirmed by heterokaryon assay and time-lapse imaging of photoconvertible protein Dendra2 tagged to g-tubulin. Immunoprecipitation from nuclear extracts combined with mass spectrometry revealed an association of gamma-tubulin with tumor suppressor protein C53 located at multiple subcellular compartments including nucleoli. The notion of an interaction between gamma-tubulin and C53 was corroborated by pull-down and co-immunoprecipitation experiments. Overexpression of gamma-tubulin antagonized the inhibitory effect of C53 on DNA damage G(2)/M checkpoint activation. The combined results indicate that aside from its known role in microtubule nucleation, gamma-tubulin may also have nuclear-specific function(s). J. Cell. Physiol. 227: 367-382, 2012. (C) 2011 Wiley Periodicals, Inc.
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Details
- Title
- Nuclear gamma-Tubulin Associates With Nucleoli and Interacts With Tumor Suppressor Protein C53
- Creators
- Barbora Horejsi - Cytoskeleton (United States)Stanislav Vinopal - Cytoskeleton (United States)Vladimira Sladkova - Cytoskeleton (United States)Eduarda Draberova - Cytoskeleton (United States)Vadym Sulimenko - Cytoskeleton (United States)Tetyana Sulimenko - Cytoskeleton (United States)Vera Vosecka - Cytoskeleton (United States)Anatoly Philimonenko - Czech Academy of SciencesPavel Hozak - Czech Academy of SciencesChristos D. Katsetos - St. Christopher's Hospital for ChildrenPavel Draber - Cytoskeleton (United States)
- Publication Details
- Journal of cellular physiology, v 227(1), pp 367-382
- Publisher
- Wiley
- Number of pages
- 16
- Grant note
- 203 / St Christopher's Foundation for Children (Philadelphia) Department of Cell Biology, Faculty of Science, Charles University, Prague, Czech Republic; Czech Republic Government AVOZ 50520514 / Institutional Research Support 204/09/1777; 204/09/H084; P302/10/1701 / Grant Agency of the Czech Republic LC545; 1M6837805001 / Ministry of Education, Youth and Sports of the Czech Republic; Ministry of Education, Youth & Sports - Czech Republic KAN200520701 / Grant Agency of the Czech Academy of Sciences; Grant Agency of the Czech Republic 11109 / Grant Agency of Charles University
- Resource Type
- Journal article
- Language
- English
- Web of Science ID
- WOS:000297942500039
- Scopus ID
- 2-s2.0-80054906970
- Other Identifier
- 991019353727904721
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- Collaboration types
- Domestic collaboration
- International collaboration
- Web of Science research areas
- Cell Biology
- Physiology