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Cheon, Seon Ah,Bal, Jyotiranjan,Song, Yunkyoung,Hwang, Hai‐,min,Kim, Ah Ruem,Kang, Woo Kyu,Kang, Hyun Ah,Hannibal‐,Bach, Hans K.,Knudsen, Jens,Ejsing, Christer S.,Kim, Jeong‐,Yoon Blackwell Publishing Ltd 2012 Molecular microbiology Vol.83 No.4
<P><B>Summary</B></P><P>Lag1p and Lac1p catalyse ceramide synthesis in <I>Saccharomyces cerevisiae.</I> This study shows that Lag1 family proteins are generally required for polarized growth in hemiascomycetous yeast. However, in contrast to <I>S. cerevisiae</I> where these proteins are functionally redundant, <I>C. albicans</I> Lag1p (CaLag1p) and Lac1p (CaLac1p) are functionally distinct. Lack of CaLag1p, but not CaLac1p, caused severe defects in the growth and hyphal morphogenesis of <I>C. albicans</I>. Deletion of <I>CaLAG1</I> decreased expression of the hypha‐specific <I>HWP1</I> and <I>ECE1</I> genes. Moreover, overexpression of <I>CaLAG1</I> induced pseudohyphal growth in this organism under non‐hypha‐inducing conditions, suggesting that CaLag1p is necessary for relaying signals to induce hypha‐specific gene expression. Analysis of ceramide and sphingolipid composition revealed that CaLag1p predominantly synthesizes ceramides with C24:0/C26:0 fatty acid moieties, which are involved in generating inositol‐containing sphingolipids, whereas CaLac1p produces ceramides with C18:0 fatty acid moieties, which are precursors for glucosylsphingolipids. Thus, our study demonstrates that CaLag1p and CaLac1p have distinct substrate specificities and physiological roles in <I>C. albicans</I>.</P>