Sidedness of ceramide-phosphoethanolamine synthesis on rat liver plasma membrane

Sphingomyelin synthase SMS2 displays dual activity as ceramide phosphoethanolamine synthase

“…In vitro enzyme assays previously demonstrated the presence of CPE synthase activities in microsomes and the PM from rat liver and brain (6)(7)(8)(9). While SMSr qualifi es for the microsomal CPE synthase activity ( 14 ), our present fi ndings indicate that SMS2 most likely accounts for the PM-localized CPE synthase activity.…”

“…The identity of the PM-associated CPE synthase activity ( 6,8,9 ), however, remains to be established. Because this second CPE synthase shares the same subcellular location as SMS2 and because the enzymatic reactions leading to SM and CPE formation are very similar, we now systematically revisit the substrate specifi cities of all three SMS family members.…”

Sphingomyelin synthase SMS2 displays dual activity as ceramide phosphoethanolamine synthase

“…In vitro enzyme assays previously demonstrated the presence of CPE synthase activities in microsomes and the PM from rat liver and brain (6)(7)(8)(9). While SMSr qualifi es for the microsomal CPE synthase activity ( 14 ), our present fi ndings indicate that SMS2 most likely accounts for the PM-localized CPE synthase activity.…”

“…The identity of the PM-associated CPE synthase activity ( 6,8,9 ), however, remains to be established. Because this second CPE synthase shares the same subcellular location as SMS2 and because the enzymatic reactions leading to SM and CPE formation are very similar, we now systematically revisit the substrate specifi cities of all three SMS family members.…”

Ceramide Phosphoethanolamine Biosynthesis in Drosophila Is Mediated by a Unique Ethanolamine Phosphotransferase in the Golgi Lumen

“…We previously demonstrated that SMS2 is a bifunctional enzyme that produces both SM and CPE (17). Thus, SMS2 likely accounts for the plasma membrane-resident CPE synthase activity reported previously (14,16). The function of SMSr had so far been unknown, but we recently identified it to be a monofunctional CPE synthase that resides in the ER (17,18).…”

Sphingomyelin synthase SMS2 displays dual activity as ceramide phosphoethanolamine synthase

“…In vitro enzyme assays previously demonstrated the presence of CPE synthase activities in microsomes and the PM from rat liver and brain (6)(7)(8)(9). While SMSr qualifi es for the microsomal CPE synthase activity ( 14 ), our present fi ndings indicate that SMS2 most likely accounts for the PM-localized CPE synthase activity.…”

“…The identity of the PM-associated CPE synthase activity ( 6,8,9 ), however, remains to be established. Because this second CPE synthase shares the same subcellular location as SMS2 and because the enzymatic reactions leading to SM and CPE formation are very similar, we now systematically revisit the substrate specifi cities of all three SMS family members.…”

Ceramide Phosphoethanolamine Biosynthesis in Drosophila Is Mediated by a Unique Ethanolamine Phosphotransferase in the Golgi Lumen

“…We previously demonstrated that SMS2 is a bifunctional enzyme that produces both SM and CPE (17). Thus, SMS2 likely accounts for the plasma membrane-resident CPE synthase activity reported previously (14,16). The function of SMSr had so far been unknown, but we recently identified it to be a monofunctional CPE synthase that resides in the ER (17,18).…”

Sphingomyelin synthase SMS2 displays dual activity as ceramide phosphoethanolamine synthase

“…In vitro enzyme assays previously demonstrated the presence of CPE synthase activities in microsomes and the PM from rat liver and brain (6)(7)(8)(9). While SMSr qualifi es for the microsomal CPE synthase activity ( 14 ), our present fi ndings indicate that SMS2 most likely accounts for the PM-localized CPE synthase activity.…”

“…The identity of the PM-associated CPE synthase activity ( 6,8,9 ), however, remains to be established. Because this second CPE synthase shares the same subcellular location as SMS2 and because the enzymatic reactions leading to SM and CPE formation are very similar, we now systematically revisit the substrate specifi cities of all three SMS family members.…”

Ceramide Phosphoethanolamine Biosynthesis in Drosophila Is Mediated by a Unique Ethanolamine Phosphotransferase in the Golgi Lumen

“…We previously demonstrated that SMS2 is a bifunctional enzyme that produces both SM and CPE (17). Thus, SMS2 likely accounts for the plasma membrane-resident CPE synthase activity reported previously (14,16). The function of SMSr had so far been unknown, but we recently identified it to be a monofunctional CPE synthase that resides in the ER (17,18).…”