Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

This Article Full Text Full Text (PDF, 468K) PPT slides of all figures Alert me when this article is cited Citation Map Services Email this article Similar articles in this journal Similar articles in PubMed Alert me to new content in the JCB Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Cronin, S. R. Articles by Hampton, R. Y. Search for Related Content PubMed PubMed Citation Articles by Cronin, S. R. Articles by Hampton, R. Y. Pubmed/NCBI databases Gene GEO Profiles HomoloGene Protein UniGene Compound via MeSH Substance via MeSH Hazardous Substances DB CALCIUM COMPOUNDS CALCIUM, ELEMENTAL Social Bookmarking                            What's this?

© The Rockefeller University Press, 0021-9525/2002/6/1017 $5.00
The Journal of Cell Biology, Volume 157, Number 6, June 10, 2002 1017-1028

Cod1p/Spf1p is a P-type ATPase involved in ER function and Ca²⁺ homeostasis

¹ Division of Biology, University of California San Diego, La Jolla, CA 92093
² Department of Physiology, The Johns Hopkins School of Medicine, Baltimore, MD 21205

Address correspondence to Randolph Y. Hampton, Division of Biology, University of California San Diego, 9500 Gilman Dr. 0347, La Jolla, CA 92093-0347. Tel.: (858) 822-0511. Fax: (858) 534-0555. E-mail: rhampton{at}biomail.ucsd.edu

The internal environment of the ER is regulated to accommodate essential cellular processes, yet our understanding of this regulation remains incomplete. Cod1p/Spf1p belongs to the widely conserved, uncharacterized type V branch of P-type ATPases, a large family of ion pumps. Our previous work suggested Cod1p may function in the ER. Consistent with this hypothesis, we localized Cod1p to the ER membrane. The cod1 mutant disrupted cellular calcium homeostasis, causing increased transcription of calcium-regulated genes and a synergistic increase in cellular calcium when paired with disruption of the Golgi apparatus–localized Ca²⁺ pump Pmr1p. Deletion of COD1 also impaired ER function, causing constitutive activation of the unfolded protein response, hypersensitivity to the glycosylation inhibitor tunicamycin, and synthetic lethality with deletion of the unfolded protein response regulator HAC1. Expression of the Drosophila melanogaster homologue of Cod1p complemented the cod1 mutant. Finally, we demonstrated the ATPase activity of the purified protein. This study provides the first biochemical characterization of a type V P-type ATPase, implicates Cod1p in ER function and ion homeostasis, and indicates that these functions are conserved among Cod1p's metazoan homologues.

Key Words: ion transport; magnesium; protein folding; endoplasmic reticulum; Saccharomyces cerevisiae

CiteULike    Complore    Connotea    Del.icio.us    Digg    Facebook    Reddit    Technorati    Twitter    What's this?

This article has been cited by other articles:

• Ticconi, C. A., Lucero, R. D., Sakhonwasee, S., Adamson, A. W., Creff, A., Nussaume, L., Desnos, T., Abel, S. (2009). ER-resident proteins PDR2 and LPR1 mediate the developmental response of root meristems to phosphate availability. Proc. Natl. Acad. Sci. USA 106: 14174-14179 [Abstract] [Full Text]  
• Pu, S., Ronen, K., Vlasblom, J., Greenblatt, J., Wodak, S. J. (2008). Local coherence in genetic interaction patterns reveals prevalent functional versatility. Bioinformatics 24: 2376-2383 [Abstract] [Full Text]  
• Federovitch, C. M., Jones, Y. Z., Tong, A. H., Boone, C., Prinz, W. A., Hampton, R. Y. (2008). Genetic and Structural Analysis of Hmg2p-induced Endoplasmic Reticulum Remodeling in Saccharomyces cerevisiae. Mol. Biol. Cell 19: 4506-4520 [Abstract] [Full Text]  
• Stowell, S. R., Qian, Y., Karmakar, S., Koyama, N. S., Dias-Baruffi, M., Leffler, H., McEver, R. P., Cummings, R. D. (2008). Differential Roles of Galectin-1 and Galectin-3 in Regulating Leukocyte Viability and Cytokine Secretion. J. Immunol. 180: 3091-3102 [Abstract] [Full Text]  
• Devasahayam, G., Burke, D. J., Sturgill, T. W. (2007). Golgi Manganese Transport Is Required for Rapamycin Signaling in Saccharomyces cerevisiae. Genetics 177: 231-238 [Abstract] [Full Text]  
• Fan, W., Idnurm, A., Breger, J., Mylonakis, E., Heitman, J. (2007). Eca1, a Sarcoplasmic/Endoplasmic Reticulum Ca2+-ATPase, Is Involved in Stress Tolerance and Virulence in Cryptococcus neoformans. Infect. Immun. 75: 3394-3405 [Abstract] [Full Text]  
• Ihara-Ohori, Y., Nagano, M., Muto, S., Uchimiya, H., Kawai-Yamada, M. (2007). Cell Death Suppressor Arabidopsis Bax Inhibitor-1 Is Associated with Calmodulin Binding and Ion Homeostasis. Plant Physiol. 143: 650-660 [Abstract] [Full Text]  
• Lockshon, D., Surface, L. E., Kerr, E. O., Kaeberlein, M., Kennedy, B. K. (2007). The Sensitivity of Yeast Mutants to Oleic Acid Implicates the Peroxisome and Other Processes in Membrane Function. Genetics 175: 77-91 [Abstract] [Full Text]  
• Stowell, S. R., Karmakar, S., Stowell, C. J., Dias-Baruffi, M., McEver, R. P., Cummings, R. D. (2007). Human galectin-1, -2, and -4 induce surface exposure of phosphatidylserine in activated human neutrophils but not in activated T cells. Blood 109: 219-227 [Abstract] [Full Text]  
• Jakobsen,, M. K., Poulsen,, L. R., Schulz,, A., Fleurat-Lessard,, P., Moller,, A., Husted,, S., Schiott,, M., Amtmann,, A., Palmgren,, M. G. (2005). Pollen development and fertilization in Arabidopsis is dependent on the MALE GAMETOGENESIS IMPAIRED ANTHERS gene encoding a Type V P-type ATPase. Genes Dev. 19: 2757-2769 [Abstract] [Full Text]  
• Uccelletti, D., Farina, F., Pinton, P., Goffrini, P., Mancini, P., Talora, C., Rizzuto, R., Palleschi, C. (2005). The Golgi Ca2+-ATPase KlPmr1p Function Is Required for Oxidative Stress Response by Controlling the Expression of the Heat-Shock Element HSP60 in Kluyveromyces lactis. Mol. Biol. Cell 16: 4636-4647 [Abstract] [Full Text]  
• Ramos-Castaneda, J., Park, Y.-n., Liu, M., Hauser, K., Rudolph, H., Shull, G. E., Jonkman, M. F., Mori, K., Ikeda, S., Ogawa, H., Arvan, P. (2005). Deficiency of ATP2C1, a Golgi Ion Pump, Induces Secretory Pathway Defects in Endoplasmic Reticulum (ER)-associated Degradation and Sensitivity to ER Stress. J. Biol. Chem. 280: 9467-9473 [Abstract] [Full Text]  
• Cortes, J. C. G., Katoh-Fukui, R., Moto, K., Ribas, J. C., Ishiguro, J. (2004). Schizosaccharomyces pombe Pmr1p Is Essential for Cell Wall Integrity and Is Required for Polarized Cell Growth and Cytokinesis. Eukaryot Cell 3: 1124-1135 [Abstract] [Full Text]  
• Aiello, D. P., Fu, L., Miseta, A., Sipos, K., Bedwell, D. M. (2004). The Ca2+ Homeostasis Defects in a pgm2{Delta} Strain of Saccharomyces cerevisiae Are Caused by Excessive Vacuolar Ca2+ Uptake Mediated by the Ca2+-ATPase Pmc1p. J. Biol. Chem. 279: 38495-38502 [Abstract] [Full Text]  
• Adamikova, L., Straube, A., Schulz, I., Steinberg, G. (2004). Calcium Signaling Is Involved in Dynein-dependent Microtubule Organization. Mol. Biol. Cell 15: 1969-1980 [Abstract] [Full Text]  
• Baxter, I., Tchieu, J., Sussman, M. R., Boutry, M., Palmgren, M. G., Gribskov, M., Harper, J. F., Axelsen, K. B. (2003). Genomic Comparison of P-Type ATPase Ion Pumps in Arabidopsis and Rice. Plant Physiol. 132: 618-628 [Abstract] [Full Text]  
• Kellermayer, R., Aiello, D. P., Miseta, A., Bedwell, D. M. (2003). Extracellular Ca2+ sensing contributes to excess Ca2+ accumulation and vacuolar fragmentation in a pmr1{Delta} mutant of S. cerevisiae. J. Cell Sci. 116: 1637-1646 [Abstract] [Full Text]  
• Aiello, D. P., Fu, L., Miseta, A., Bedwell, D. M. (2002). Intracellular Glucose 1-Phosphate and Glucose 6-Phosphate Levels Modulate Ca2+ Homeostasis in Saccharomyces cerevisiae. J. Biol. Chem. 277: 45751-45758 [Abstract] [Full Text]  
• Vashist, S., Frank, C. G., Jakob, C. A., Ng, D. T.W. (2002). Two Distinctly Localized P-Type ATPases Collaborate to Maintain Organelle Homeostasis Required for Glycoprotein Processing and Quality Control. Mol. Biol. Cell 13: 3955-3966 [Abstract] [Full Text]  

Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents