Transmembrane topology of ceramide synthase in yeast.

By Natsuko Kageyama-Yahara, Howard Riezman. 2006

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In Molecular Biology

Citations in the corpus

Mammalian Ceramide Synthases (2010, background): “Within this motif, two conserved histidine residues appear to play a key role in catalysis and/or substrate binding (17), since their mutation in mammalian CerS1 (19) or in yeast Lag1 adversely affects catalytic activity (20), although no direct proof of their role in catalysis has been provided.”
Roles of bioactive sphingolipids in cancer biology and therapeutics. (2008, background): “…factor 1 (UOG1) (Lee, 1991; Venkataraman et al., 2002), demonstrated that it specifically regulates the synthesis of C18-ceramide with a high degree of fatty-acid chain length specificity (Venkataraman et al., 2002; Riebeling et al., 2003; Mizutani et al., 2005; Kageyama-Yahara and Riezman, 2006).”
CERAMIDE SYNTHASE 1 IS REGULATED BY PROTEASOMAL MEDIATED TURNOVER (2009, methodology): “This molecular genetic approach is more specific than using relatively non-specific inhibitors of ceramide synthesis such as fumonisin or myriocin which inhibit either all ceramide synthases or the upstream serine palmitoyl transferase, respectively, and the change of two amino acids is unlikely to ”
Stress-induced ER to Golgi translocation of ceramide synthase 1 is dependent on proteasomal processing (2009, unknown): “The change of two amino acids probably does not alter the folding or membrane topology of CerS1 as previously shown [25].”
Antiapoptotic roles of ceramide‐synthase‐6‐generated C16‐ceramide via selective regulation of the ATF6/ CHOP arm of ER‐stress‐response pathways (2010, methodology): “catalytic domain (35, 36), using the tetracycline (Tet)-”