Previous Article | Next Article ![]()
Molecular and Cellular Biology, May 2008, p. 3336-3343, Vol. 28, No. 10
0270-7306/08/$08.00+0 doi:10.1128/MCB.00567-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.
,
Department of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, Illinois 60637
Received 30 March 2007/ Returned for modification 19 June 2007/ Accepted 27 February 2008
In the budding yeast Saccharomyces cerevisiae, mutations in the essential gene CDC1 cause defects in Golgi inheritance and actin polarization. However, the biochemical function of Cdc1p is unknown. Previous work showed that cdc1 mutants accumulate intracellular Ca2+ and display enhanced sensitivity to the extracellular Mn2+ concentration, suggesting that Cdc1p might regulate divalent cation homeostasis. By contrast, our data indicate that Cdc1p is a Mn2+-dependent protein that can affect Ca2+ levels. We identified a cdc1 allele that activates Ca2+ signaling but does not show enhanced sensitivity to the Mn2+ concentration. Furthermore, our studies show that Cdc1p is an endoplasmic reticulum-localized transmembrane protein with a putative phosphoesterase domain facing the lumen. cdc1 mutant cells accumulate an unidentified phospholipid, suggesting that Cdc1p may be a lipid phosphatase. Previous work showed that deletion of the plasma membrane Ca2+ channel Cch1p partially suppressed the cdc1 growth phenotype, and we find that deletion of Cch1p also suppresses the Golgi inheritance and actin polarization phenotypes. The combined data fit a model in which the cdc1 mutant phenotypes result from accumulation of a phosphorylated lipid that activates Ca2+ signaling.
Published ahead of print on 10 March 2008.
Supplemental material for this article may be found at http://mcb.asm.org/.
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»