Analysis of membrane topology of neutral sphingomyelinase 2

Motohiro Tani, Yusuf A. Hannun

Research output: Contribution to journalArticlepeer-review

43 Citations (Scopus)

Abstract

Neutral sphingomyelinase 2 (nSMase2), which has two hydrophobic segments at its NH2-terminus, plays an important role in ceramide-mediated cell regulation. Here, we investigated the membrane topology of nSMase2. When a double-tagged nSMase2 at both the NH2 and COOH termini, was overexpressed in MCF-7 cells, the signals from both tags were detected in the inner leaflet of the plasma membrane. Furthermore, insertion of a tag into the internal sequence and green fluorescent protein-fused deletion mutants revealed that the entire catalytic region of the protein was located on the cytosolic face of the membranes and each hydrophobic segment is integrated into the membranes, but unlikely to span the entire membrane. These results indicate the presence of the enzyme in the inner leaflet of plasma membrane.

Original languageEnglish
Pages (from-to)1323-1328
Number of pages6
JournalFEBS Letters
Volume581
Issue number7
DOIs
Publication statusPublished - Apr 3 2007
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint Dive into the research topics of 'Analysis of membrane topology of neutral sphingomyelinase 2'. Together they form a unique fingerprint.

Cite this