Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans (Q28145545)

Presenilins: molecular switches between proteolysis and signal transduction

Europe PubMed Central

title

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

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4

J L Goldstein

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author name string

M S Brown

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1

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J Ye

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2

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R B Rawson

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3

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language of work or name

English

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publication date

18 February 2000

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published in

Cell

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volume

100

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issue

4

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page(s)

391-8

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cites work

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Presenilins, processing of beta-amyloid precursor protein, and notch signaling.

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Intracellular signaling from the endoplasmic reticulum to the nucleus

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A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response

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Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase

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Transport-Dependent Proteolysis of SREBP

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Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein

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A presenilin-1-dependent gamma-secretase-like protease mediates release of Notch intracellular domain

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

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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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Protein folding in the cell

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

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Hairpin orientation of sterol regulatory element-binding protein-2 in cell membranes as determined by protease protection

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Modeling studies of the change in conformation required for cleavage of limited proteolytic sites

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Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex

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Presenilin-1 mutations downregulate the signalling pathway of the unfolded-protein response

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A simple method for displaying the hydropathic character of a protein

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Facilitation of lin-12-mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene

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A novel clan of zinc metallopeptidases with possible intramembrane cleavage properties

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Structural basis of the action of thermolysin and related zinc peptidases

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A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus

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A role for presenilin-1 in nuclear accumulation of Ire1 fragments and induction of the mammalian unfolded protein response

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Cell surface presenilin-1 participates in the gamma-secretase-like proteolysis of Notch

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A family of membrane-embedded metalloproteases involved in regulated proteolysis of membrane-associated transcription factors

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

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A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells

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

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Cloning of mammalian Ire1 reveals diversity in the ER stress responses

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Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity

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Neurogenic phenotypes and altered Notch processing in Drosophila Presenilin mutants.

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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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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/S0092-8674(00)80675-3

Identifiers

DOI

10.1016/S0092-8674(00)80675-3

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

10693756

1 reference

Consolidated OpenCitations Corpus – April 2017