ArticleThe Journal of cell biology1993
SAC1p is an integral membrane protein that influences the cellular requirement for phospholipid transfer protein function and inositol in yeast.
Article in The Journal of cell biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
74 citing papers in PubMed, 162 citations in OpenAlex.
- Intersection of Sphingolipid and Sterol Metabolism at the Level of Orm Proteins in Yeast.Cells · 2026Article
- Structure of the ceramide-bound SPOTS complex.Nature communications · 2023Article
- Review
- Regulation of phosphoinositide metabolism in Apicomplexan parasites.Frontiers in cell and developmental biology · 2023Review
- PtdIns4P restriction by hydrolase SAC1 decides specific fusion of autophagosomes with lysosomes.Autophagy · 2021Article
- Emerging Prospects for Combating Fungal Infections by Targeting Phosphatidylinositol Transfer Proteins.International journal of molecular sciences · 2021Review
- Functions and Mechanisms of SAC Phosphoinositide Phosphatases in Plants.Frontiers in plant science · 2021Review
- Lipid Exchangers: Cellular Functions and Mechanistic Links With Phosphoinositide Metabolism.Frontiers in cell and developmental biology · 2020Review
- An equal opportunity collaboration between lipid metabolism and proteins in the control of membrane trafficking in the trans-Golgi and endosomal systems.Current opinion in cell biology · 2019Review
- SAC-1 ensures epithelial endocytic recycling by restricting ARF-6 activity.The Journal of cell biology · 2018Article
- The phosphoinositide phosphatase Sac1 regulates cell shape and microtubule stability in the developingDevelopment (Cambridge, England) · 2018Article
- SAC1 degrades its lipid substrate PtdIns4eLife · 2018Article
- Identification of membrane proteome ofFuture science OA · 2017Article
- Characterization of a putative Plasmodium falciparum SAC1 phosphoinositide-phosphatase homologue potentially required for survival during the asexual erythrocytic stages.Scientific reports · 2017Article
- Mitigating Motor Neuronal Loss in C. elegans Model of ALS8.Scientific reports · 2017Article
- Phosphatidylinositol-4-phosphate-dependent membrane traffic is critical for fungal filamentous growth.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The structure of phosphoinositide phosphatases: Insights into substrate specificity and catalysis.Biochimica et biophysica acta · 2015Review
- Spatiotemporal control of phosphatidylinositol 4-phosphate by Sac2 regulates endocytic recycling.The Journal of cell biology · 2015Article
- The Sac domain-containing phosphoinositide phosphatases: structure, function, and disease.Frontiers in biology · 2013Article
- Phosphoinositides: tiny lipids with giant impact on cell regulation.Physiological reviews · 2013Review
14 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Mutations in the SAC1 gene exhibit allele-specific genetic interactions with yeast actin structural gene defects and effect a bypass of the cellular requirement for the yeast phosphatidylinositol/phosphatidylcholine transfer protein (SEC14p), a protein whose function is essential for sustained Golgi secretory function. We report that SAC1p is an integral membrane protein that localizes to the yeast Golgi complex and to the yeast ER, but does not exhibit a detectable association with the bulk of the yeast F-actin cytoskeleton. The data also indicate that the profound in vivo effects on Golgi secretory function and the organization of the actin cytoskeleton observed in sac1 mutants result from loss of SAC1p function. This cosuppression of actin and SEC14p defects is a unique feature of sac1 alleles as mutations in other SAC genes that result in a suppression of actin defects do not result in phenotypic suppression of SEC14p defects. Finally, we report that sac1 mutants also exhibit a specific inositol auxotrophy that is not exhibited by the other sac mutant strains. This sac1-associated inositol auxotrophy is not manifested by measurable defects in de novo inositol biosynthesis, nor is it the result of some obvious defect in the ability of sac1 mutants to utilize inositol for phosphatidylinositol biosynthesis. Thus, sac1 mutants represent a novel class of inositol auxotroph in that these mutants appear to require elevated levels of inositol for growth. On the basis of the collective data, we suggest that SAC1p dysfunction exerts its pleiotropic effects on yeast Golgi function, the organization of the actin cytoskeleton, and the cellular requirement for inositol, through altered metabolism of inositol glycerophospholipids.
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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.