ArticleMolecular and cellular biology2008
Cdc1p is an endoplasmic reticulum-localized putative lipid phosphatase that affects Golgi inheritance and actin polarization by activating Ca2+ signaling.
Article in Molecular and cellular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 22 citations in OpenAlex.
- Potential Physiological Relevance of ERAD to the Biosynthesis of GPI-Anchored Proteins in Yeast.International journal of molecular sciences · 2021Review
- Cdc1p is a Golgi-localized glycosylphosphatidylinositol-anchored protein remodelase.Molecular biology of the cell · 2020Article
- The natural anticancer agent cantharidin alters GPI-anchored protein sorting by targeting Cdc1-mediated remodeling in endoplasmic reticulum.The Journal of biological chemistry · 2019Article
- Cdc1 removes the ethanolamine phosphate of the first mannose of GPI anchors and thereby facilitates the integration of GPI proteins into the yeast cell wall.Molecular biology of the cell · 2014Article
- The yeast p5 type ATPase, spf1, regulates manganese transport into the endoplasmic reticulum.PloS one · 2013Article
- Impaired manganese metabolism causes mitotic misregulation.The Journal of biological chemistry · 2012Article
- The yeast Golgi apparatus: insights and mysteries.FEBS letters · 2009Review
- Requirement of the spindle pole body for targeting and/or tethering proteins to the inner nuclear membrane.Nucleus (Austin, Tex.)Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
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 Ca(2+) and display enhanced sensitivity to the extracellular Mn(2+) concentration, suggesting that Cdc1p might regulate divalent cation homeostasis. By contrast, our data indicate that Cdc1p is a Mn(2+)-dependent protein that can affect Ca(2+) levels. We identified a cdc1 allele that activates Ca(2+) signaling but does not show enhanced sensitivity to the Mn(2+) 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 Ca(2+) 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 Ca(2+) signaling.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.