C26‐CoA‐dependent ceramide synthesis of Saccharomyces cerevisiae is operated by Lag1p and Lac1p
By I. Guillas, P. Kirchman, R. Chuard, M. Pfefferli, J. C. Jiang, S. Jazwinski, A. Conzelmann. 2001
287 citations recorded by the source corpus.
Subfields: Molecular Biology, Plant Science
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In Molecular Biology
- A. Futerman
- Michal Levy
- B. Ogretmen
- Yusuf A. Hannun
- C. Senkal
- J. Bielawski
- Howard Riezman
- S. Ponnusamy
Citations in the corpus
- Mammalian Ceramide Synthases (2010, background): “Interestingly, when human CerS5 was expressed in a yeast Dlag1Dlac1DLip1 mutant (71), it was able to synthesize C16-ceramides and the mutant survived in the absence of the C26-ceramides that are normally found in yeast.”
- Biologically active sphingolipids in cancer pathogenesis and treatment (2004, background): “Subsequently, several independent studies revealed that these genes are key components of (dihydro)ceramide synthase (also called dihydrosphingosine acyl transferase”
- Roles of bioactive sphingolipids in cancer biology and therapeutics. (2008, background): “Additionally, the fact that yeast aging genes, lac1 and lag1 are known to be essential components of ceramide synthase (Guillas et al., 2001) provides a genetic link between ceramide and aging.”
- Differential expression of (dihydro)ceramide synthases in mouse brain: oligodendrocyte-specific expression of CerS2/Lass2 (2008, unknown): “CerS was Wrst identiWed in yeast as a complex of three proteins, Lag1p, Lac1p and Lip1p, which all together are required for synthesis of C26-ceramide (Guillas et al. 2001; Vallee and Riezmann 2005).”
- Lag1p and Lac1p are essential for the Acyl-CoA-dependent ceramide synthase reaction in Saccharomyces cerevisae. (2001, background): “Finally, during the processing of this article another study has appeared implicating LAG1 and LAC1 in ceramide synthesis (Guillas et al., 2001).”
- Lip1p: a novel subunit of acyl‐CoA ceramide synthase (2005, background): “This activity was characterized using crude microsomal membranes (Guillas et al, 2001; Schorling et al, 2001).”
- Kinetic characterization of mammalian ceramide synthases: Determination of K m values towards sphinganine (2007, background): “Liver microsomes Tris None Tween 20 Sphingosine (coated on Celite)/ C16- and C24:1-CoAs [5] Brain microsomes Potassium phosphate Mg2+ Tween 20 Sphingosine (coated on Celite)/ C16-, C18-, and C18:1-CoAs [6] [25] Liver microsomes Potassium phosphate None None Sphingosine/C16-CoA [9] Live microsomes, H”