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Sterol-Regulated Release of SREBP-2 from Cell Membranes Requires Two Sequential Cleavages, One Within a Transmembrane Segment

Sakai, Juro, Duncan, Elizabeth A, Rawson, Robert B, Hua, Xianxin, Brown, Michael S, Goldstein, Joseph L·1996·Cell
DOI 10.1016/s0092-8674(00)81304-5
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Abstract

Sterol regulatory element binding proteins (SREBPs) are transcription factors attached to the endoplasmic reticulum. The NH2-segment, which activates transcription, is connected to membranes by a hairpin anchor formed by two transmembrane sequences and a short lumenal loop. Using H-Ras-SREBP-2 fusion proteins, we show that the NH2-segment is released from membranes by two sequential cleavages. The first, regulated by sterols, occurs in the lumenal loop. The second, not regulated by sterols, occurs within the first transmembrane domain. The liberated NH2-segment enters the nucleus and activates genes controlling cholesterol synthesis and uptake. Certain mutant Chinese hamster ovary cells are auxotrophic for cholesterol because they fail to carry out the second cleavage; the NH2-segment remains membrane-bound and transcription is not activated.

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Metadata

Authors
Sakai, J., Duncan, E. A., Rawson, R. B., Hua, X., Brown, M. S., & Goldstein, J. L.
Venue
Cell
Publisher
Elsevier BV
Published
1996-06
Volume
85
Issue
7
Pages
1037-1046
ISSN
0092-8674
DOI
10.1016/s0092-8674(00)81304-5
Cited by
486
References
0
Language
en
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