Title : Yeast ceramide synthases, Lag1 and Lac1, have distinct substrate specificity.

Pub. Date : 2019 Jun 24

PMID : 31164445






3 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Lag1 and Lac1 lie in an enzymatic branch point of the sphingolipid pathway that is interconnected by the activity of the C4 hydroxylase, Sur2. Sphingolipids sphingosine N-acyltransferase LAG1 Saccharomyces cerevisiae S288C
2 By uncoupling the enzymatic branch point and using lipidomic mass spectrometry, metabolic labeling and in vitro assays we show that Lag1 preferentially synthesizes phyto-sphingolipids. phyto-sphingolipids sphingosine N-acyltransferase LAG1 Saccharomyces cerevisiae S288C
3 Using photo-bleaching experiments we show that Lag1 is uniquely required for the establishment of a lateral diffusion barrier in the nuclear envelope, which depends on phytoceramide. phytoceramide sphingosine N-acyltransferase LAG1 Saccharomyces cerevisiae S288C