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Sterol regulatory element binding proteins (SREBP)-1a and SREBP-2 are linked to the MAP-kinase cascade
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ERK1/2 signaling has been previously shown to regulate SREBP2 activity in HepG2 cells via direct phosphorylation.
“ERK1/2 signaling has been previously shown to regulate SREBP2 activity in HepG2 cells via direct phosphorylation (Arito et al., 2008; Kotzka et al., 2004; Kotzka et al., 2000)”
From GPR146 Deficiency Protects against Hypercholesterolemia and Atherosclerosis (2019) · cites this paper as Kotzka et al., 2000
The Results report that MAP-kinase pathway activation increased SREBP-2 transcriptional activity in HepG2 cells, and that ERK1 or ERK2 directly phosphorylated recombinant SREBP-2 in vitro. The Abstract describes SREBP-2 as *possibly* a direct ERK1/2 substrate; it does not establish that direct phosphorylation mediates the activity change in HepG2 cells. Page numbers are not available in the supplied passages. (LLM, conf=0.88)
Experimental — accuracy not yet measuredThe MEK1/ERK cascade directly phosphorylates SREBP2 at Ser-432 and Ser-455, inhibiting its sumoylation and promoting its transcription activity.
“Previous studies in HepG2 cells showed that MEK1/ERK cascade directly phosphorylates SREBP2 at Ser-432 and Ser-455, which inhibits its sumoylation and subsequently promotes its transcription activity (Arito et al., 2008; Kotzka et al., 2004; Kotzka et al., 2000).”
From GPR146 Deficiency Protects against Hypercholesterolemia and Atherosclerosis (2019) · cites this paper as Kotzka et al., 2000
The Results report that ERK1 and ERK2 phosphorylated SREBP-2 on serine residues in vitro, and that activating the MAP-kinase cascade increased SREBP-2 transcriptional activity in HepG2 cells. The paper does not identify Ser-432 or Ser-455, test sumoylation, or establish that phosphorylation at those sites causes the increased activity. (LLM, conf=0.91)
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Metadata
- Authors
- Kotzka, J., Müller-Wieland, D., Roth, G., Kremer, L., Munck, M., Schürmann, S., Knebel, B., & Krone, W.
- Venue
- Journal of Lipid Research
- Publisher
- Elsevier BV
- Published
- 2000-01
- Volume
- 41
- Issue
- 1
- Pages
- 99-108
- ISSN
- 0022-2275
- Cited by
- 146
- References
- 3
- Language
- en
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