TY - JOUR
T1 - Identification of a human cDNA encoding a novel protein structurally related to the yeast membrane-associated metalloprotease, Ste24p
AU - Kumagai, Hidetoshi
AU - Kawamura, Yuuki
AU - Yanagisawa, Katsuhiko
AU - Komano, Hiroto
N1 - Funding Information:
This study was supported by a Research Grant for Longevity Sciences from the Ministry of Health and Welfare, Japan. We acknowledge grant support for H. Kumagai from Tsukada Grant for Niigata University Medical Research, and the grant support for H. Komano from Sasagawa Foundation and Sandoz Foundation for gerontological research.
PY - 1999/2/2
Y1 - 1999/2/2
N2 - 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.
AB - 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.
KW - Mammalian Ste24 homologue
KW - Metalloprotease
KW - Proteolytic processing
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U2 - 10.1016/S0304-4165(98)00170-6
DO - 10.1016/S0304-4165(98)00170-6
M3 - Article
C2 - 10076063
AN - SCOPUS:0033034937
SN - 0304-4165
VL - 1426
SP - 468
EP - 474
JO - Biochimica et Biophysica Acta - General Subjects
JF - Biochimica et Biophysica Acta - General Subjects
IS - 3
ER -