Submitted on February 4, 2008
Revised on February 27, 2008
Accepted on February 27, 2008
ISC1 (Inositol phosphosphingolipid-phospholipase C) the yeast homologue of neutral sphingomyelinases
Nabil Matmati and Yusuf A. Hannun
Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC 29425
Corresponding Author: hannun{at}musc.edu
Sphingolipid biosynthesis and breakdown in yeast share many homologies in their pathways with higher eukaryotes(1), (Fig.1). In mammals, ceramide can be generated through hydrolysis of sphingomyelin catalyzed by sphingomyelinase. To date, as many as 5 sphingomyelinases have been identified molecularly, separated in three main groups, acid, alkaline, and neutral sphingomyelinases(2). Neutral sphingomyelinase (nSMase) in mammals is represented by its homologue, inositol phosphosphingolipase C codified by ISC1 in Saccharomyces cerevisiae (Sc) and Cryptococcus neoformans (Cn) and by CSS1 (Can’t Stop Synthesizing cell wall) in Schizosaccharomyces pombe (Sp). Yeast do not have sphingomyelin but instead have inositol phosphosphingolipids, which may function as orthologues of mammalian sphingomyelin. In this review we will describe findings related to the function of ISC1, its localization, mechanisms, and its roles in cell response to different type of stresses. These studies serve as a foundation for the elucidation of the properties and functions for the extended family of nSMases.
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