Accelerated degradation of HMG CoA reductase mediated by binding of insig-1 to its sterol-sensing domain (Q28204022)

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Tong Yang

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Michael S Brown

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Russell A DeBose-Boyd

Heart attacks: gone with the century?

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language of work or name

English

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publication date

January 2003

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published in

Molecular Cell

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volume

11

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issue

1

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page(s)

25-33

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cites work

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Nucleotide sequence of 3-hydroxy-3-methyl-glutaryl coenzyme A reductase, a glycoprotein of endoplasmic reticulum

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Regulation of HMG-CoA reductase degradation requires the P-type ATPase Cod1p/Spf1p

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Transport-Dependent Proteolysis of SREBP

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Regulation of synthesis and degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase by low density lipoprotein and 25-hydroxycholesterol in UT-1 cells

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A highly conserved signal controls degradation of 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase in eukaryotes

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Membrane-bound domain of HMG CoA reductase is required for sterol-enhanced degradation of the enzyme

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Regulation of the mevalonate pathway

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Mutant mammalian cells as tools to delineate the sterol regulatory element-binding protein pathway for feedback regulation of lipid synthesis

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Genetic analysis of hydroxymethylglutaryl-coenzyme A reductase regulated degradation

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ER-associated degradation in protein quality control and cellular regulation

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Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein

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Sterol resistance in CHO cells traced to point mutation in SREBP cleavage-activating protein

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The hypocholesterolemic agent LY295427 up-regulates INSIG-1, identifying the INSIG-1 protein as a mediator of cholesterol homeostasis through SREBP

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Cellular cholesterol efflux mediated by cyclodextrins

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Feedback regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in livers of mice treated with mevinolin, a competitive inhibitor of the reductase

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Degradation of 3-hydroxy-3-methylglutaryl-CoA reductase in endoplasmic reticulum membranes is accelerated as a result of increased susceptibility to proteolysis.

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Sterols regulate processing of carbohydrate chains of wild-type SREBP cleavage-activating protein (SCAP), but not sterol-resistant mutants Y298C or D443N.

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The ubiquitin-proteasome pathway mediates the regulated degradation of mammalian 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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Failure to cleave sterol regulatory element-binding proteins (SREBPs) causes cholesterol auxotrophy in Chinese hamster ovary cells with genetic absence of SREBP cleavage-activating protein.

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Identification of complexes between the COOH-terminal domains of sterol regulatory element-binding proteins (SREBPs) and SREBP cleavage-activating protein

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Insig-2, a second endoplasmic reticulum protein that binds SCAP and blocks export of sterol regulatory element-binding proteins

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Crucial step in cholesterol homeostasis: sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER

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Transport-dependent proteolysis of SREBP: relocation of site-1 protease from Golgi to ER obviates the need for SREBP transport to Golgi

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/S1097-2765(02)00822-5

Identifiers

DOI

10.1016/S1097-2765(02)00822-5

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Consolidated OpenCitations Corpus – April 2017

3763155

3763155

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference