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  Complementation Cloning of S2P, a Gene Encoding a Putative Metalloprotease Required for Intramembrane Cleavage of SREBPs

Rawson, R. B., Zelenski, N. G., Nijhawan, D., Ye, J., Sakai, J., Hasan, M. T., et al. (1997). Complementation Cloning of S2P, a Gene Encoding a Putative Metalloprotease Required for Intramembrane Cleavage of SREBPs. Molecular Cell, 1(1), 47-57. doi:10.1016/S1097-2765(00)80006-4.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-A557-2 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-AB76-D
Genre: Journal Article

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 Creators:
Rawson, Robert B., Author
Zelenski, Nikolai G., Author
Nijhawan, Deepak, Author
Ye, Jin, Author
Sakai, Juro, Author
Hasan, Mazahir T.1, 2, 3, Author              
Chang, Ta−Yuan, Author
Brown, Michael S., Author
Goldstein, Joseph L., Author
Affiliations:
1Mazahir Hasan Group, Max Planck Institute for Medical Research, Max Planck Society, ou_1497726              
2Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497704              
3Department of Biomedical Optics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497699              

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 Abstract: 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.

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Language(s): eng - English
 Dates: 1997-08-191997-09-172000-09-271997-12
 Publication Status: Published in print
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 664709
DOI: 10.1016/S1097-2765(00)80006-4
URI: https://www.ncbi.nlm.nih.gov/pubmed/9659902
Other: 7429
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Title: Molecular Cell
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 1 (1) Sequence Number: - Start / End Page: 47 - 57 Identifier: ISSN: 1097-2765
CoNE: https://pure.mpg.de/cone/journals/resource/954925610929