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The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

Protein Sensors for Membrane Sterols

Goldstein, Joseph L., DeBose-Boyd, Russell A., Brown, Michael S.·2006·Cell
DOI 10.1016/j.cell.2005.12.022
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Crossref · 10.1016/j.cell.2005.12.022

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3 of 3 references verified0 citation errors · 0 not checkable

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  • The mature SREBP-2 transcription factor translocates to the nucleus where it binds to its target promoters.

    “The mature SREBP-2 transcription factor then translocates to the nucleus where it binds to its target promoters (Goldstein et al., 2006).”

    From Inhibition of cholesterol biosynthesis through RNF145-dependent ubiquitination of SCAP (2017) · cites this paper as Goldstein et al., 2006

    Our copy says that SREBP is processed to its nuclear form in the Golgi and that nuclear SREBP activates genes for cholesterol biosynthesis and uptake (passage 4, labeled Abstract; page unavailable). It also identifies SREBP-2 as an isoform that stimulates cholesterol synthesis (passage 1). These passages support the nuclear transcription-factor role, but do not state that mature SREBP-2 binds its target promoters. (LLM, conf=0.81)

    Experimental — accuracy not yet measured

  • SREBPs are central transcriptional regulators of lipid metabolism.

    “The sterol-regulatory element binding proteins (SREBP) are central transcriptional regulators of lipid metabolism.”

    From Haploid genetic screens identify SPRING/C12ORF49 as a determinant of SREBP signaling and cholesterol metabolism (2020) · cites this paper as [2]

  • At the transcriptional level, LDLR gene expression is controlled by a cholesterol-responsive negative feedback mechanism through SREBP-2.

    “At the transcriptional level, LDLR gene expression is controlled by a cholesterol-responsive negative feedback mechanism through sterol regulatory element-binding protein-2 (SREBP-2)6.”

    From Triciribine increases LDLR expression and LDL uptake through stabilization of LDLR mRNA (2018) · cites this paper as [6]

  • Activation of SREBP1 and SREBP2 share a common proteolytic maturation cycle.

    “The activation of SREBP1 and SREBP2 share a common proteolytic maturation cycle [9], and activation of the SREBP1 pathway necessitates SREBP2-driven cholesterol biosynthesis [54].”

    From Loss of the E3 ubiquitin ligase MARCHF6 alters hepatic lipid metabolism and drives spontaneous hepatosteatosis (2026) · cites this paper as [9]

  • SCAP and the remnant C-terminal domain of SREBP undergo retrograde transport to the ER, where remnant SREBP is degraded and SCAP can enter a new cycle of SREBP activation.

    “At the same time, SCAP and the remnant C-terminal domain of SREBP undergo retrograde transport to the ER, where remnant SREBP is degraded and SCAP can enter a new cycle of SREBP activation1,9.”

    From Hepatic SREBP signaling requires SPRING to govern systemic lipid metabolism in mice and humans (2023) · cites this paper as [1]

    The passage describing Scap/SREBP transport (indexed as Abstract; page unavailable) says the complex moves from the ER to the Golgi, where SREBP is processed. Searches for retrograde transport, the SREBP remnant, and Scap recycling found no passage saying that Scap and the remnant return to the ER or that the remnant is degraded there. (LLM, conf=0.72)

    Experimental — accuracy not yet measured

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Citations

Cites

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Research works printed but not linked: 71

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Metadata

Authors
Goldstein, J. L., DeBose-Boyd, R. A., & Brown, M. S.
Venue
Cell
Publisher
Elsevier BV
Published
2006-01
Volume
124
Issue
1
Pages
35-46
ISSN
0092-8674
DOI
10.1016/j.cell.2005.12.022
Cited by
1,517
References
3
Language
en
Licence

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