Identification of a human cDNA encoding a novel protein structurally related to the yeast membrane-associated metalloprotease, Ste24p

Hidetoshi Kumagai, Yuuki Kawamura, Katsuhiko Yanagisawa, Hiroto Komano

Research output: Contribution to journalArticle

21 Scopus citations

Abstract

Recently, a novel membrane-associated metalloprotease, designated Ste24p, has been identified in Saccharomyces cerevisiae [K. Fujimura-Kamada, F.J. Nouvet, S. Michaelis, J. Cell Biol. 27 (1997) 271-285]. We cloned a human brain cDNA encoding a protein homologous to Ste24p (designated Hs Ste24p). The predicted 475-amino acid product of its open reading frame exhibited 62% similarity to Ste24p, and contained a zinc metalloprotease motif (HEXXH) and multiple predicted membrane spans. Northern blot analysis showed that this gene was expressed in most tissues. Immunofluorescence analysis of epitope-tagged Hs Ste24p constructs suggested that it is localized in the ER and possibly also in the Golgi compartment. A search of the expression sequence tag database identified a fragment of DNA encoding a segment homologous to the segment of Hs Ste24p containing the HEXXH motif in insects and nematodes. Thus, Hs Ste24p could be a member of a new family of Ste24p-like membrane-associated metalloproteases which are widely conserved in eukaryotes. Copyright (C) 1999 Elsevier Science B.V.

Original languageEnglish (US)
Pages (from-to)468-474
Number of pages7
JournalBiochimica et Biophysica Acta - General Subjects
Volume1426
Issue number3
DOIs
Publication statusPublished - Feb 2 1999

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Keywords

  • Mammalian Ste24 homologue
  • Metalloprotease
  • Proteolytic processing

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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