Yeast ubiquitin-like genes are involved in duplication of the microtubule organizing center

doi:10.1083/jcb.133.6.1331

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Yeast ubiquitin-like genes are involved in duplication of the microtubule organizing center

S Biggins, I Ivanovska and MD Rose
Princeton University, Department of Molecular Biology, New Jersey 08544- 1014, USA.

KAR1 is required for duplication of the Saccharomyces cerevisiae microtubule organizing center, the spindle pole body (SPB) (Rose, M.D., and G.R. Fink, 1987. Cell. 48:1047-1060). Suppressors of a kar1 allele defective for SPB duplication were isolated in two genes, CDC31 and DSK2 (Vallen, E.A., W.H., M. Winey, and M.D. Rose. 1994. Genetics. 137:407-422). To elucidate the role of DSK2 in SPB duplication, we cloned the gene and found it encodes a novel ubiquitin-like protein containing an NH2 terminus 36% identical to ubiquitin. The only other known yeast ubiquitin-like protein is encoded by the nucleotide excision repair gene RAD23 (Watkins, J.F.,P. Sung, L. Prakash, and S. Prakash. 1993. Mol. Cell. Bio. 13:7757-7765). Unlike ubiquitin, the NH2- terminal domain of Dsk2p is not cleaved from the protein, indicating that Dsk2p is not conjugated to other proteins. Although the DSK2-1 mutation alters a conserved residue in the Dsk2p ubiquitin-like domain, we detect no differences in Dsk2p or Cdc31p stability. Therefore, DSK2 does not act by interfering with ubiquitin-dependent protein degradation of these proteins. Although DSK2 is not essential, a strain deleted for both DSK2 and RAD23 is temperature sensitive for growth due to a block in SPB duplication. In addition, overexpression of DSK2 is toxic, and the DSK2-1 allele causes a block in SPB duplication. Therefore, DSK2 dosage is critical for SPB duplication. We determined that CDC31 gene function is downstream of DSK2 and KAR1. Dsk2p is a nuclear-enriched protein, and we propose that Dsk2p assists in Cdc31 assembly into the new SPB.
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Gabriely, G., Kama, R., Gelin-Licht, R., Gerst, J. E. (2008). Different Domains of the UBL-UBA Ubiquitin Receptor, Ddi1/Vsm1, Are Involved in Its Multiple Cellular Roles. Mol. Biol. Cell 19: 3625-3637 [Abstract] [Full Text]
Chen, L., Madura, K. (2008). Centrin/Cdc31 Is a Novel Regulator of Protein Degradation. Mol. Cell. Biol. 28: 1829-1840 [Abstract] [Full Text]
Li, X., Su, V., Kurata, W. E., Jin, C., Lau, A. F. (2008). A Novel Connexin43-interacting Protein, CIP75, Which Belongs to the UbL-UBA Protein Family, Regulates the Turnover of Connexin43. J. Biol. Chem. 283: 5748-5759 [Abstract] [Full Text]
Romero-Perez, L., Li Chen, L., Lambertson, D., Madura, K. (2007). Sts1 Can Overcome the Loss of Rad23 and Rpn10 and Represents a Novel Regulator of the Ubiquitin/Proteasome Pathway. J. Biol. Chem. 282: 35574-35582 [Abstract] [Full Text]
Ghaboosi, N., Deshaies, R. J. (2007). A Conditional Yeast E1 Mutant Blocks the Ubiquitin-Proteasome Pathway and Reveals a Role for Ubiquitin Conjugates in Targeting Rad23 to the Proteasome. Mol. Biol. Cell 18: 1953-1963 [Abstract] [Full Text]
Schmidtke, G., Kalveram, B., Weber, E., Bochtler, P., Lukasiak, S., Hipp, M. S., Groettrup, M. (2006). The UBA Domains of NUB1L Are Required for Binding but Not for Accelerated Degradation of the Ubiquitin-like Modifier FAT10. J. Biol. Chem. 281: 20045-20054 [Abstract] [Full Text]
Canaan, A., Yu, X., Booth, C. J., Lian, J., Lazar, I., Gamfi, S. L., Castille, K., Kohya, N., Nakayama, Y., Liu, Y.-C., Eynon, E., Flavell, R., Weissman, S. M. (2006). FAT10/Diubiquitin-Like Protein-Deficient Mice Exhibit Minimal Phenotypic Differences.. Mol. Cell. Biol. 26: 5180-5189 [Abstract] [Full Text]
Kim, I., Ahn, J., Liu, C., Tanabe, K., Apodaca, J., Suzuki, T., Rao, H. (2006). The Png1-Rad23 complex regulates glycoprotein turnover. JCB 172: 211-219 [Abstract] [Full Text]
Hu, Z., Potthoff, B., Hollenberg, C. P., Ramezani-Rad, M. (2006). Mdy2, a ubiquitin-like (UBL)-domain protein, is required for efficient mating in Saccharomyces cerevisiae. J. Cell Sci. 119: 326-338 [Abstract] [Full Text]
Xie, Z., Liu, S., Zhang, Y., Wang, Z. (2004). Roles of Rad23 protein in yeast nucleotide excision repair. Nucleic Acids Res 32: 5981-5990 [Abstract] [Full Text]
Riley, B. E., Xu, Y., Zoghbi, H. Y., Orr, H. T. (2004). The Effects of the Polyglutamine Repeat Protein Ataxin-1 on the UbL-UBA Protein A1Up. J. Biol. Chem. 279: 42290-42301 [Abstract] [Full Text]
Kim, I., Mi, K., Rao, H. (2004). Multiple Interactions of Rad23 Suggest a Mechanism for Ubiquitylated Substrate Delivery Important in Proteolysis. Mol. Biol. Cell 15: 3357-3365 [Abstract] [Full Text]
N'Diaye, E.-N., Brown, E. J. (2003). The ubiquitin-related protein PLIC-1 regulates heterotrimeric G protein function through association with G{beta}{gamma}. JCB 163: 1157-1165 [Abstract] [Full Text]
Popescu, A., Miron, S., Blouquit, Y., Duchambon, P., Christova, P., Craescu, C. T. (2003). Xeroderma Pigmentosum Group C Protein Possesses a High Affinity Binding Site to Human Centrin 2 and Calmodulin. J. Biol. Chem. 278: 40252-40261 [Abstract] [Full Text]
Ng, J. M.Y., Vermeulen, W., van der Horst, G. T.J., Bergink, S., Sugasawa, K., Vrieling, H., Hoeijmakers, J. H.J. (2003). A novel regulation mechanism of DNA repair by damage-induced and RAD23-dependent stabilization of xeroderma pigmentosum group C protein. Genes Dev. 17: 1630-1645 [Abstract] [Full Text]
Paoletti, A., Bordes, N., Haddad, R., Schwartz, C. L., Chang, F., Bornens, M. (2003). Fission Yeast cdc31p Is a Component of the Half-bridge and Controls SPB Duplication. Mol. Biol. Cell 14: 2793-2808 [Abstract] [Full Text]
Raasi, S., Pickart, C. M. (2003). Rad23 Ubiquitin-associated Domains (UBA) Inhibit 26 S Proteasome-catalyzed Proteolysis by Sequestering Lysine 48-linked Polyubiquitin Chains. J. Biol. Chem. 278: 8951-8959 [Abstract] [Full Text]
McDonald, H. B., Helfant, A. H., Mahony, E. M., Khosla, S. K., Goetsch, L. (2002). Mutational Analysis Reveals a Role for the C Terminus of the Proteasome Subunit Rpt4p in Spindle Pole Body Duplication in Saccharomyces cerevisiae. Genetics 162: 705-720 [Abstract] [Full Text]
Ko, H. S., Uehara, T., Nomura, Y. (2002). Role of Ubiquilin Associated with Protein-disulfide Isomerase in the Endoplasmic Reticulum in Stress-induced Apoptotic Cell Death. J. Biol. Chem. 277: 35386-35392 [Abstract] [Full Text]
Chen, L., Madura, K. (2002). Rad23 Promotes the Targeting of Proteolytic Substrates to the Proteasome. Mol. Cell. Biol. 22: 4902-4913 [Abstract] [Full Text]
Rao, H., Sastry, A. (2002). Recognition of Specific Ubiquitin Conjugates Is Important for the Proteolytic Functions of the Ubiquitin-associated Domain Proteins Dsk2 and Rad23. J. Biol. Chem. 277: 11691-11695 [Abstract] [Full Text]
Funakoshi, M., Sasaki, T., Nishimoto, T., Kobayashi, H. (2002). Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome. Proc. Natl. Acad. Sci. USA 99: 745-750 [Abstract] [Full Text]
Elder, R. T., Song, X.-q., Chen, M., Hopkins, K. M., Lieberman, H. B., Zhao, Y. (2002). Involvement of rhp23, a Schizosaccharomyces pombe homolog of the human HHR23A and Saccharomyces cerevisiaeRAD23 nucleotide excision repair genes, in cell cycle control and protein ubiquitination. Nucleic Acids Res 30: 581-591 [Abstract] [Full Text]
Gillette, T. G., Huang, W., Russell, S. J., Reed, S. H., Johnston, S. A., Friedberg, E. C. (2001). The 19S complex of the proteasome regulates nucleotide excision repair in yeast. Genes Dev. 15: 1528-1539 [Abstract] [Full Text]
Mah, A. L., Perry, G., Smith, M. A., Monteiro, M. J. (2000). Identification of Ubiquilin, a Novel Presenilin Interactor That Increases Presenilin Protein Accumulation. JCB 151: 847-862 [Abstract] [Full Text]
Davidson, J. D., Riley, B., Burright, E. N., Duvick, L. A., Zoghbi, H. Y., Orr, H. T. (2000). Identification and characterization of an ataxin-1-interacting protein: A1Up, a ubiquitin-like nuclear protein. Hum Mol Genet 9: 2305-2312 [Abstract] [Full Text]
Khalfan, W., Ivanovska, I., Rose, M. D. (2000). Functional Interaction Between the PKC1 Pathway and CDC31 Network of SPB Duplication Genes. Genetics 155: 1543-1559 [Abstract] [Full Text]
Li, W., Hesabi, B., Babbo, A., Pacione, C., Liu, J., Chen, D. J., Nickoloff, J. A., Shen, Z. (2000). Regulation of double-strand break-induced mammalian homologous recombination by UBL1, a RAD51-interacting protein. Nucleic Acids Res 28: 1145-1153 [Abstract] [Full Text]
Middendorp, S., Kuntziger, T., Abraham, Y., Holmes, S., Bordes, N., Paintrand, M., Paoletti, A., Bornens, M. (2000). A Role for Centrin 3 in Centrosome Reproduction. JCB 148: 405-416 [Abstract] [Full Text]
Wolfe, D., Reiner, T., Keeley, J. L., Pizzini, M., Keil, R. L. (1999). Ubiquitin Metabolism Affects Cellular Response to Volatile Anesthetics in Yeast. Mol. Cell. Biol. 19: 8254-8262 [Abstract] [Full Text]
Lambertson, D., Chen, L., Madura, K. (1999). Pleiotropic Defects Caused by Loss of the Proteasome-Interacting Factors Rad23 and Rpn10 of Saccharomyces cerevisiae. Genetics 153: 69-79 [Abstract] [Full Text]
Kumar, S., Talis, A. L., Howley, P. M. (1999). Identification of HHR23A as a Substrate for E6-associated Protein-mediated Ubiquitination. J. Biol. Chem. 274: 18785-18792 [Abstract] [Full Text]
Adams, I. R., Kilmartin, J. V. (1999). Localization of Core Spindle Pole Body (SPB) Components during SPB Duplication in Saccharomyces cerevisiae. JCB 145: 809-823 [Abstract] [Full Text]
Liu, Y.-C., Pan, J., Zhang, C., Fan, W., Collinge, M., Bender, J. R., Weissman, S. M. (1999). A MHC-encoded ubiquitin-like protein (FAT10) binds noncovalently to the spindle assembly checkpoint protein MAD2. Proc. Natl. Acad. Sci. USA 96: 4313-4318 [Abstract] [Full Text]
Rao-Naik, C., delaCruz, W., Laplaza, J. M., Tan, S., Callis, J., Fisher, A. J. (1998). The Rub Family of Ubiquitin-like Proteins. CRYSTAL STRUCTURE OF ARABIDOPSIS RUB1 AND EXPRESSION OF MULTIPLE RUBS IN ARABIDOPSIS. J. Biol. Chem. 273: 34976-34982 [Abstract] [Full Text]
Hinchcliffe, E. H., Cassels, G. O., Rieder, C. L., Sluder, G. (1998). The Coordination of Centrosome Reproduction with Nuclear Events of the Cell Cycle in the Sea Urchin Zygote. JCB 140: 1417-1426 [Abstract] [Full Text]
Mahajan, R., Gerace, L., Melchior, F. (1998). Molecular Characterization of the SUMO-1 Modification of RanGAP1 and Its Role in Nuclear Envelope Association. JCB 140: 259-270 [Abstract] [Full Text]
He, X, Jones, M., Winey, M, Sazer, S (1998). Mph1, a member of the Mps1-like family of dual specificity protein kinases, is required for the spindle checkpoint in S. pombe. J. Cell Sci. 111: 1635-1647 [Abstract]
Madeo, F., Schlauer, J., Zischka, H., Mecke, D., Fröhlich, K.-U. (1998). Tyrosine Phosphorylation Regulates Cell Cycle-dependent Nuclear Localization of Cdc48p. Mol. Biol. Cell 9: 131-141 [Abstract] [Full Text]
Sternsdorf, T., Jensen, K., Will, H. (1997). Evidence for Covalent Modification of the Nuclear Dot-associated Proteins PML and Sp100 by PIC1/SUMO-1. JCB 139: 1621-1634 [Abstract] [Full Text]
Zarzov, P, Boucherie, H, Mann, C (1997). A yeast heat shock transcription factor (Hsf1) mutant is defective in both Hsc82/Hsp82 synthesis and spindle pole body duplication. J. Cell Sci. 110: 1879-1891 [Abstract]
Araki, M., Masutani, C., Takemura, M., Uchida, A., Sugasawa, K., Kondoh, J., Ohkuma, Y., Hanaoka, F. (2001). Centrosome Protein Centrin 2/Caltractin 1 Is Part of the Xeroderma Pigmentosum Group C Complex That Initiates Global Genome Nucleotide Excision Repair. J. Biol. Chem. 276: 18665-18672 [Abstract] [Full Text]