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

MPG-Autoren
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Hasan,  Mazahir T.
Mazahir Hasan Group, Max Planck Institute for Medical Research, Max Planck Society;
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;
Department of Biomedical Optics, Max Planck Institute for Medical Research, Max Planck Society;

Externe Ressourcen

http://www.sciencedirect.com/science/article/pii/S1097276500800064/pdfft?md5=1613c68d515c9bd78474034f3a3ac95f&pid=1-s2.0-S1097276500800064-main.pdf
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https://doi.org/10.1016/S1097-2765(00)80006-4
(beliebiger Volltext)

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Zitation

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.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0019-A557-2
Zusammenfassung
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.