Transport-Dependent Proteolysis of SREBP (Q54231898)

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object named as

Joseph L Goldstein

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author name string

Russell A DeBose-Boyd

1

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Michael S Brown

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Wei-Ping Li

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Peter J Espenshade

The SREBP pathway: regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor

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language of work or name

English

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publication date

December 1999

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published in

Cell

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volume

99

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issue

7

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page(s)

703-712

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cites work

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Cleavage site for sterol-regulated protease localized to a leu-Ser bond in the lumenal loop of sterol regulatory element-binding protein-2.

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Sterols and isoprenoids: signaling molecules derived from the cholesterol biosynthetic pathway

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Autocatalytic processing of site-1 protease removes propeptide and permits cleavage of sterol regulatory element-binding proteins

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

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Regulated cleavage of sterol regulatory element binding proteins requires sequences on both sides of the endoplasmic reticulum membrane

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Assembly of asparagine-linked oligosaccharides

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Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence for membrane cycling from Golgi to ER

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A C-terminal signal prevents secretion of luminal ER proteins

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Effects of PS1 deficiency on membrane protein trafficking in neurons.

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Recurrent G-to-A substitution in a single codon of SREBP cleavage-activating protein causes sterol resistance in three mutant Chinese hamster ovary cell lines.

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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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Sterols regulate cycling of SREBP cleavage-activating protein (SCAP) between endoplasmic reticulum and Golgi

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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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Sterol-regulated release of SREBP-2 from cell membranes requires two sequential cleavages, one within a transmembrane segment

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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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Cleavage of sterol regulatory element-binding proteins (SREBPs) at site-1 requires interaction with SREBP cleavage-activating protein. Evidence from in vivo competition studies

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