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Papers In Press, published online ahead of print March 3, 2006
Institute for Microbiology, University of Cologne, Koeln 50935
Corresponding Author: M.Kroenke{at}uni-koeln.de
Two genes encoding neutral sphingomyelinases-1, and -2 (sphingomyelin phosphodiesterase-2 and -3, SMPD2 and-31) have been recently identified that hydrolyze sphingomyelin to phosphorylcholine and ceramide. Databank searches using a peptide sequence derived from a previously purified bovine neutral sphingomyelinase (nSMase) allowed us to identify a cDNA encoding a novel human sphingomyelinase, nSMase3, that shows only little homology to nSMase1 and -2. nSMase3 was biochemically characterized by overexpression in a yeast strain, JK9-3dDIsc1p, lacking endogenous SMase activity. Like nSMase2, nSMase3 is Mg2+ dependent, shows optimal activity at pH7, which is enhanced in the presence of phosphatidylserine and inhibited by scyphostatin. NSMase3 is ubiquitously expressed as a 4.6kb mRNA species. nSMase3 lacks an N-terminal signal peptide yet contains a 23 aminoacid transmembrane domain close to the C- terminus, which is indicative for the family of C-tail-anchored integral membrane proteins. Cellular localization studies with HA-tagged nSMase3 demonstrated colocalization with markers of the endoplasmic reticulum (ER) as well as with Golgi markers. TNF stimulates rapid activation of nSMase3 in MCF7 cells with peak activity at 1.5 min, which was impaired by expression of dominant-negative FAN.
J. Biol. Chem, 10.1074/jbc.M511306200
Submitted on October 18, 2005
Revised on March 1, 2006
Accepted on March 3, 2006
Novel TNF-responsive mammalian neutral sphingomyelinase-3 is a C-tail-anchored protein
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