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Identification of Complexes between the COOH-terminal Domains of Sterol Regulatory Element-binding Proteins (SREBPs) and SREBP Cleavage-Activating Protein

Sakai, Juro, Nohturfft, Axel, Cheng, Dong, Ho, Y.K., Brown, Michael S., Goldstein, Joseph L.·1997·Journal of Biological Chemistry
DOI 10.1074/jbc.272.32.20213
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  • Under sufficient cellular sterols, SREBPs are retained in the ER through formation of a tripartite complex with SCAP and INSIG1/2.

    “Under conditions of sufficient cellular sterols, SREBPs are retained in the ER through formation of a tripartite complex with the sterol-sensing SREBP cleavage-activating protein (SCAP)7,8, and the ER anchor proteins insulin-induced genes 1 and 2 (INSIG1 and 2)9,10.”

    From Haploid genetic screens identify SPRING/C12ORF49 as a determinant of SREBP signaling and cholesterol metabolism (2020) · cites this paper as [8]

    The Abstract reports that sterol-replete SREBPs remain in ER membranes and that SREBPs form a complex with SCAP. The discussion of Fig. 2 says this complex persists under both sterol depletion and repletion, so the paper does not establish that forming it causes sterol-dependent retention. It does not describe INSIG1/2 as members of a tripartite complex; the citing sentence assigns INSIG1/2 separate citations. (LLM, conf=0.87)

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Research works printed but not linked: 31

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Metadata

Authors
Sakai, J., Nohturfft, A., Cheng, D., Ho, Y. K., Brown, M. S., & Goldstein, J. L.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1997-08
Volume
272
Issue
32
Pages
20213-20221
ISSN
0021-9258
DOI
10.1074/jbc.272.32.20213
Cited by
202
References
0
Language
en
Licence

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