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 Hung, L.-Y.
Right arrow Articles by Tang, T. K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hung, L.-Y.
Right arrow Articles by Tang, T. K.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, October 2000, p. 7813-7825, Vol. 20, No. 20
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Protein 4.1 R-135 Interacts with a Novel Centrosomal Protein (CPAP) Which Is Associated with the gamma -Tubulin Complex

Liang-Yi Hung,1,2 Chieh-Ju C. Tang,2 and Tang K. Tang2,*

Institute of Life Science, National Defense Medical College,1 and Institute of Biomedical Sciences, Academia Sinica,2 Taipei 115, Taiwan, Republic of China

Received 12 May 2000/Returned for modification 29 June 2000/Accepted 24 July 2000

Using a yeast two-hybrid system, we isolated a novel human centrosomal protein, CPAP (centrosomal P4.1-associated protein), which specifically interacts with the head domain of the 135-kDa protein 4.1R isoform (4.1R-135). Sequence analysis revealed that the carboxyl terminus of CPAP has 31.3% amino acid identity with human Tcp-10 (a t-complex responder gene product). Interestingly, most of the sequence identity is restricted to two conserved regions. One carries a leucine zipper, which may form a series of heptad repeats involved in coiled-coil formation; the other contains unusual glycine repeats with unknown function. Immunofluorescence analysis revealed that CPAP and gamma -tubulin are localized within the centrosome throughout the cell cycle. CPAP cosediments with gamma -tubulin in sucrose gradients and coimmunoprecipitates with gamma -tubulin, indicating that CPAP is a part of the gamma -tubulin complex. Furthermore, functional analysis revealed that CPAP is localized within the center of microtubule asters and may participate in microtubule nucleation. The formation of microtubule asters was significantly inhibited by anti-CPAP antibody. Together, these observations indicate that CPAP may play an important role in cell division and centrosome function.

* Corresponding author. Mailing address: Institute of Biomedical Sciences, Academia Sinica, 128 Yen-Chiu-Yuan Rd. Sec. 2, Taipei 115, Taiwan. Phone: 886-2-26523901. Fax: 886-2-27825573. E-mail: tktang{at}ibms.sinica.edu.tw.

Molecular and Cellular Biology, October 2000, p. 7813-7825, Vol. 20, No. 20
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Blau-Wasser, R., Euteneuer, U., Xiong, H., Gassen, B., Schleicher, M., Noegel, A. A. (2009). CP250, a Novel Acidic Coiled Coil Protein of the Dictyostelium centrosome, Affects Growth, Chemotaxis, and the Nuclear Envelope. Mol. Biol. Cell 20: 4348-4361 [Abstract] [Full Text]  
  • Blachon, S., Cai, X., Roberts, K. A., Yang, K., Polyanovsky, A., Church, A., Avidor-Reiss, T. (2009). A Proximal Centriole-Like Structure Is Present in Drosophila Spermatids and Can Serve as a Model to Study Centriole Duplication. Genetics 182: 133-144 [Abstract] [Full Text]  
  • Nicholas, A K, Swanson, E A, Cox, J J, Karbani, G, Malik, S, Springell, K, Hampshire, D, Ahmed, M, Bond, J, Di Benedetto, D, Fichera, M, Romano, C, Dobyns, W B, Woods, C G (2009). The molecular landscape of ASPM mutations in primary microcephaly. J. Med. Genet. 46: 249-253 [Abstract] [Full Text]  
  • Cormier, A., Clement, M.-J., Knossow, M., Lachkar, S., Savarin, P., Toma, F., Sobel, A., Gigant, B., Curmi, P. A. (2009). The PN2-3 Domain of Centrosomal P4.1-associated Protein Implements a Novel Mechanism for Tubulin Sequestration. J. Biol. Chem. 284: 6909-6917 [Abstract] [Full Text]  
  • Krauss, S. W., Spence, J. R., Bahmanyar, S., Barth, A. I. M., Go, M. M., Czerwinski, D., Meyer, A. J. (2008). Downregulation of Protein 4.1R, a Mature Centriole Protein, Disrupts Centrosomes, Alters Cell Cycle Progression, and Perturbs Mitotic Spindles and Anaphase. Mol. Cell. Biol. 28: 2283-2294 [Abstract] [Full Text]  
  • Delgehyr, N., Sillibourne, J., Bornens, M. (2005). Microtubule nucleation and anchoring at the centrosome are independent processes linked by ninein function. J. Cell Sci. 118: 1565-1575 [Abstract] [Full Text]  
  • Koyanagi, M., Hijikata, M., Watashi, K., Masui, O., Shimotohno, K. (2005). Centrosomal P4.1-associated Protein Is a New Member of Transcriptional Coactivators for Nuclear Factor-{kappa}B. J. Biol. Chem. 280: 12430-12437 [Abstract] [Full Text]  
  • Perez-Ferreiro, C. M., Vernos, I., Correas, I. (2004). Protein 4.1R regulates interphase microtubule organization at the centrosome. J. Cell Sci. 117: 6197-6206 [Abstract] [Full Text]  
  • Krauss, S. W., Lee, G., Chasis, J. A., Mohandas, N., Heald, R. (2004). Two Protein 4.1 Domains Essential for Mitotic Spindle and Aster Microtubule Dynamics and Organization in Vitro. J. Biol. Chem. 279: 27591-27598 [Abstract] [Full Text]  
  • Hung, L.-Y., Chen, H.-L., Chang, C.-W., Li, B.-R., Tang, T. K. (2004). Identification of a Novel Microtubule-destabilizing Motif in CPAP That Binds to Tubulin Heterodimers and Inhibits Microtubule Assembly. Mol. Biol. Cell 15: 2697-2706 [Abstract] [Full Text]  
  • Parra, M. K., Gee, S. L., Koury, M. J., Mohandas, N., Conboy, J. G. (2003). Alternative 5' exons and differential splicing regulate expression of protein 4.1R isoforms with distinct N-termini. Blood 101: 4164-4171 [Abstract] [Full Text]  
  • Luque, C. M., Perez-Ferreiro, C. M., Perez-Gonzalez, A., Englmeier, L., Koffa, M. D., Correas, I. (2003). An Alternative Domain Containing a Leucine-rich Sequence Regulates Nuclear Cytoplasmic Localization of Protein 4.1R. J. Biol. Chem. 278: 2686-2691 [Abstract] [Full Text]  
  • Sun, C.-X., Robb, V. A., Gutmann, D. H. (2002). Protein 4.1 tumor suppressors: getting a FERM grip on growth regulation. J. Cell Sci. 115: 3991-4000 [Abstract] [Full Text]  
  • Delhommeau, F., Vasseur-Godbillon, C., Leclerc, P., Schischmanoff, P.-O., Croisille, L., Rince, P., Moriniere, M., Benz, E. J. Jr, Tchernia, G., Tamagnini, G., Ribeiro, L., Delaunay, J., Baklouti, F. (2002). A splicing alteration of 4.1R pre-mRNA generates 2 protein isoforms with distinct assembly to spindle poles in mitotic cells. Blood 100: 2629-2636 [Abstract] [Full Text]  
  • Peng, B., Sutherland, K. D., Sum, E. Y. M., Olayioye, M., Wittlin, S., Tang, T. K., Lindeman, G. J., Visvader, J. E. (2002). CPAP Is a Novel Stat5-Interacting Cofactor that Augments Stat5-Mediated Transcriptional Activity. Mol. Endocrinol. 16: 2019-2033 [Abstract] [Full Text]  
  • Tang, C.-J. C., Chuang, C.-K., Hu, H.-M., Tang, T. K. (2001). The Zinc Finger Domain of Tzfp Binds to the tbs Motif Located at the Upstream Flanking Region of the Aie1 (aurora-C) Kinase Gene. J. Biol. Chem. 276: 19631-19639 [Abstract] [Full Text]  
  • Perez-Ferreiro, C. M., Luque, C. M., Correas, I. (2001). 4.1R Proteins Associate with Interphase Microtubules in Human T Cells. A 4.1R CONSTITUTIVE REGION IS INVOLVED IN TUBULIN BINDING. J. Biol. Chem. 276: 44785-44791 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»