This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ma, S.
Right arrow Articles by Erikson, R. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ma, S.
Right arrow Articles by Erikson, R. L.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, October 2003, p. 6936-6943, Vol. 23, No. 19
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.19.6936-6943.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Role of Plk2 (Snk) in Mouse Development and Cell Proliferation

Sheng Ma,1 Jean Charron,2 and Raymond L. Erikson1*

Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138,1 Centre de Recherche en Cancérologie de l'Université Laval, L'Hôtel-Dieu de Québec, CHUQ, Québec, Canada G1R 2J62

Received 29 May 2003/ Accepted 16 June 2003

Plk2 (Snk) is a polo-like kinase expressed at G1 in cultured cells and mainly in the hippocampal neurons in the brains of adult rodents, but its function is poorly understood. We have generated mice deficient in Plk2 by gene targeting. Although Plk2 is not required for postnatal growth, Plk2-/- embryos show retarded growth and skeletal development late in gestation. The labyrinthine zone of the placenta is diminished in Plk2-/- embryos due to decreased cell proliferation. Cultured Plk2-/- embryonic fibroblasts grow more slowly than normal cells and show delayed entry into S phase. These data suggest a role for Plk2 in the cell cycle.


* Corresponding author. Mailing address: Department of Molecular and Cellular Biology, Harvard University, 16 Divinity Ave., Cambridge, MA 02138. Phone: (617) 495-5386. Fax: (617) 495-0681. E-mail: erikson{at}mcb.harvard.edu.


Molecular and Cellular Biology, October 2003, p. 6936-6943, Vol. 23, No. 19
0022-538X/03/$08.00+0     DOI: 10.1128/MCB.23.19.6936-6943.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Matsumoto, T., Wang, P.-y., Ma, W., Sung, H. J., Matoba, S., Hwang, P. M. (2009). Polo-like kinases mediate cell survival in mitochondrial dysfunction. Proc. Natl. Acad. Sci. USA 106: 14542-14546 [Abstract] [Full Text]  
  • Rudolph, D., Steegmaier, M., Hoffmann, M., Grauert, M., Baum, A., Quant, J., Haslinger, C., Garin-Chesa, P., Adolf, G. R. (2009). BI 6727, A Polo-like Kinase Inhibitor with Improved Pharmacokinetic Profile and Broad Antitumor Activity. Clin. Cancer Res. 15: 3094-3102 [Abstract] [Full Text]  
  • Inglis, K. J., Chereau, D., Brigham, E. F., Chiou, S.-S., Schobel, S., Frigon, N. L., Yu, M., Caccavello, R. J., Nelson, S., Motter, R., Wright, S., Chian, D., Santiago, P., Soriano, F., Ramos, C., Powell, K., Goldstein, J. M., Babcock, M., Yednock, T., Bard, F., Basi, G. S., Sham, H., Chilcote, T. J., McConlogue, L., Griswold-Prenner, I., Anderson, J. P. (2009). Polo-like Kinase 2 (PLK2) Phosphorylates {alpha}-Synuclein at Serine 129 in Central Nervous System. J. Biol. Chem. 284: 2598-2602 [Abstract] [Full Text]  
  • Yang, Y., Bai, J., Shen, R., Brown, S. A.N., Komissarova, E., Huang, Y., Jiang, N., Alberts, G. F., Costa, M., Lu, L., Winkles, J. A., Dai, W. (2008). Polo-like Kinase 3 Functions as a Tumor Suppressor and Is a Negative Regulator of Hypoxia-Inducible Factor-1{alpha} under Hypoxic Conditions. Cancer Res. 68: 4077-4085 [Abstract] [Full Text]  
  • Schmit, T. L, Ahmad, N. (2008). Regulation of Mitosis via Mitotic Kinases: New Opportunities for Cancer Management. aacredbook 2008: 133-150 [Abstract] [Full Text]  
  • Nishi, Y., Rogers, E., Robertson, S. M., Lin, R. (2008). Polo kinases regulate C. elegans embryonic polarity via binding to DYRK2-primed MEX-5 and MEX-6. Development 135: 687-697 [Abstract] [Full Text]  
  • Schmit, T. L., Ahmad, N. (2007). Regulation of mitosis via mitotic kinases: new opportunities for cancer management. Molecular Cancer Therapeutics 6: 1920-1931 [Abstract] [Full Text]  
  • Boylan, K. L.M., Gosse, M. A., Staggs, S. E., Janz, S., Grindle, S., Kansas, G. S., Van Ness, B. G. (2007). A Transgenic Mouse Model of Plasma Cell Malignancy Shows Phenotypic, Cytogenetic, and Gene Expression Heterogeneity Similar to Human Multiple Myeloma. Cancer Res. 67: 4069-4078 [Abstract] [Full Text]  
  • Yuan, W., Leisner, T. M., McFadden, A. W., Clark, S., Hiller, S., Maeda, N., O'Brien, D. A., Parise, L. V. (2006). CIB1 Is Essential for Mouse Spermatogenesis. Mol. Cell. Biol. 26: 8507-8514 [Abstract] [Full Text]  
  • O'Donnell, S. M., Holm, G. H., Pierce, J. M., Tian, B., Watson, M. J., Chari, R. S., Ballard, D. W., Brasier, A. R., Dermody, T. S. (2006). Identification of an NF-{kappa}B-Dependent Gene Network in Cells Infected by Mammalian Reovirus. J. Virol. 80: 1077-1086 [Abstract] [Full Text]  
  • Syed, N., Smith, P., Sullivan, A., Spender, L. C., Dyer, M., Karran, L., O'Nions, J., Allday, M., Hoffmann, I., Crawford, D., Griffin, B., Farrell, P. J., Crook, T. (2006). Transcriptional silencing of Polo-like kinase 2 (SNK/PLK2) is a frequent event in B-cell malignancies. Blood 107: 250-256 [Abstract] [Full Text]  
  • Yogosawa, S., Hatakeyama, S., Nakayama, K. I., Miyoshi, H., Kohsaka, S., Akazawa, C. (2005). Ubiquitylation and Degradation of Serum-inducible Kinase by hVPS18, a RING-H2 Type Ubiquitin Ligase. J. Biol. Chem. 280: 41619-41627 [Abstract] [Full Text]  
  • Watson, E. D., Cross, J. C. (2005). Development of Structures and Transport Functions in the Mouse Placenta. Physiology 20: 180-193 [Abstract] [Full Text]  
  • Lotz, K., Pyrowolakis, G., Jentsch, S. (2004). BRUCE, a Giant E2/E3 Ubiquitin Ligase and Inhibitor of Apoptosis Protein of the trans-Golgi Network, Is Required for Normal Placenta Development and Mouse Survival. Mol. Cell. Biol. 24: 9339-9350 [Abstract] [Full Text]  
  • Carpentier, M., Guillemette, C., Bailey, J. L., Boileau, G., Jeannotte, L., DesGroseillers, L., Charron, J. (2004). Reduced Fertility in Male Mice Deficient in the Zinc Metallopeptidase NL1. Mol. Cell. Biol. 24: 4428-4437 [Abstract] [Full Text]