Structural highlights
Function
LAC1_YEAST Component of the ceramide synthase complex that catalyzes the transfer of the acyl chain from acyl-CoA to a sphingoid base, with high selectivity toward hexacosanoyl-CoA (C26:0-CoA) (PubMed:11694577, PubMed:15692566). N-acylates sphinganine and phytosphingosine bases to form dihydroceramides and phytoceramides, respectively (PubMed:11694577, PubMed:15692566). Redundant with LAG1. Facilitates ER-to-Golgi transport of GPI-anchored proteins.[1] [2] [3] [4]
References
- ↑ Barz WP, Walter P. Two endoplasmic reticulum (ER) membrane proteins that facilitate ER-to-Golgi transport of glycosylphosphatidylinositol-anchored proteins. Mol Biol Cell. 1999 Apr;10(4):1043-59. PMID:10198056 doi:10.1091/mbc.10.4.1043
- ↑ Guillas I, Kirchman PA, Chuard R, Pfefferli M, Jiang JC, Jazwinski SM, Conzelmann A. C26-CoA-dependent ceramide synthesis of Saccharomyces cerevisiae is operated by Lag1p and Lac1p. EMBO J. 2001 Jun 1;20(11):2655-65. PMID:11387200 doi:10.1093/emboj/20.11.2655
- ↑ Schorling S, Vallée B, Barz WP, Riezman H, Oesterhelt D. Lag1p and Lac1p are essential for the Acyl-CoA-dependent ceramide synthase reaction in Saccharomyces cerevisae. Mol Biol Cell. 2001 Nov;12(11):3417-27. PMID:11694577 doi:10.1091/mbc.12.11.3417
- ↑ Vallée B, Riezman H. Lip1p: a novel subunit of acyl-CoA ceramide synthase. EMBO J. 2005 Feb 23;24(4):730-41. PMID:15692566 doi:10.1038/sj.emboj.7600562
