Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs

Robert B. Rawson, Nikolai G. Zelenski, Deepak Nijhawan, Jin Ye, Juro Sakai, Mazahir T. Hasan, T. Y. Chang, Michael S. Brown, Joseph L. Goldstein

研究成果: Article査読

389 被引用数 (Scopus)

抄録

We report the cloning of a gene, S2P, that encodes a putative metalloprotease required for intramembrane proteolysis of sterol-regulatory element-binding proteins (SREBPs) at Site-2. SREBPs are membrane-bound transcription factors that activate genes regulating cholesterol metabolism. The active NH2-terminal domains of SREBPs are released from membranes by sequential cleavage at two sites: Site-1, within the lumen of the endoplasmic reticulum ; and Site-2, within a transmembrane segment. The human S2P gene was cloned by complementation of mutant CHO cells that cannot cleave SREBPs at Site-2 and are cholesterol auxotrophs. S2P defines a new family of polytopic membrane proteins that contain an HEXXH sequence characteristic of zinc metalloproteases. Mutation of the putative zinc-binding residues abolishes S2P activity. S2P encodes an unusual metalloprotease that cleaves proteins within transmembrane segments.

本文言語English
ページ(範囲)47-57
ページ数11
ジャーナルMolecular Cell
1
1
DOI
出版ステータスPublished - 1997 12月
外部発表はい

ASJC Scopus subject areas

  • 分子生物学
  • 細胞生物学

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