ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs (Q24290776)

Membrane bound transcription factor peptidase, site 1

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activating transcription factor 6

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serine-type endopeptidase activity

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author name string

J Ye

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R B Rawson

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R Komuro

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X Chen

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U P Davé

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R Prywes

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M S Brown

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J L Goldstein

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 2000

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1355-64

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cites work

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7 January 2021

Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans

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7 January 2021

Transport-Dependent Proteolysis of SREBP

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7 January 2021

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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7 January 2021

Second-site cleavage in sterol regulatory element-binding protein occurs at transmembrane junction as determined by cysteine panning

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7 January 2021

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

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7 January 2021

19 Receptor-mediated endocytosis of low-density lipoprotein in cultured cells

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Somatic cell genetic and biochemical characterization of cell lines resulting from human genomic DNA transfections of Chinese hamster ovary cell mutants defective in sterol-dependent activation of sterol synthesis and LDL receptor expression

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7 January 2021

Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress

1 reference

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7 January 2021

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

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7 January 2021

A turn propensity scale for transmembrane helices

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7 January 2021

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

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7 January 2021

Regulated step in cholesterol feedback localized to budding of SCAP from ER membranes

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7 January 2021

Signal transduction from the endoplasmic reticulum to the cell nucleus

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Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs

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7 January 2021

Isolation of cholesterol-requiring mutant Chinese hamster ovary cells with defects in cleavage of sterol regulatory element-binding proteins at site 1.

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7 January 2021

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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7 January 2021

Amino acid preferences for specific locations at the ends of alpha helices

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7 January 2021

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

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7 January 2021

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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Molecular identification of the sterol-regulated luminal protease that cleaves SREBPs and controls lipid composition of animal cells

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SREBP-1, a membrane-bound transcription factor released by sterol-regulated proteolysis

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Asparagine-proline sequence within membrane-spanning segment of SREBP triggers intramembrane cleavage by site-2 protease

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Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors

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7 January 2021

Membrane topology of S2P, a protein required for intramembranous cleavage of sterol regulatory element-binding proteins

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7 January 2021

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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Loss of transcriptional repression of three sterol-regulated genes in mutant hamster cells.

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19 October 2022

https://opencitations.net/index/coci/api/v1/citations/10.1016/S0021-9258(19)84879-2

Identifiers

DOI

10.1016/S1097-2765(00)00133-7

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Consolidated OpenCitations Corpus – April 2017

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Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

11163209

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Consolidated OpenCitations Corpus – April 2017