The unfolded protein response and cell fate control
Author
Abstract
The secretory capacity of a cell is constantly challenged by physiological demands and pathological perturbations. To adjust and match the protein-folding capacity of the endoplasmic reticulum (ER) to changing secretory needs, cells employ a dynamic intracellular signaling pathway known as the unfolded protein response (UPR). Homeostatic activation of the UPR enforces adaptive programs that modulate and augment key aspects of the entire secretory pathway, whereas maladaptive UPR outputs trigger apoptosis. Here, we discuss recent advances into how the UPR integrates information about the intensity and duration of ER stress stimuli in order to control cell fate. These findings are timely and significant because they inform an evolving mechanistic understanding of a wide variety of human diseases, including diabetes mellitus, neuro-degeneration, and cancer, thus opening up the potential for new therapeuticmodalities to treat these diverse diseases.
Patrocinador
FONDECYT
1140549
FONDAP program
15150012
Millennium Institute
P09-015-F
European Commission RD MSCA-RISE
734749
Michael J. Fox Foundation for Parkinson's Research - Target Validation grant
9277
FONDEF
ID16I10223
D11E1007
U.S. Office of Naval Research-Global (ONR-G)
N62909-16-1-2003
U.S. Air Force Office of Scientific Research
FA9550-16-1-0384
ALSRP Therapeutic Idea Award
AL150111
Muscular Dystrophy Association
382453
CONICYT-Brazil
441921/2016-7
NIH
RO1DK080955
RO1 DK100623
Burroughs Wellcome Fund
Juvenile Diabetes Research Foundation (JDRF)
2-SRA-2016-234-S-N
Breakthrough Therapeutics Initiative from Leona M. and Harry B. Helmsley Charitable Trust
Indexation
Artículo de publicación ISI
Quote Item
Molecular Cell Volumen: 69 Número: 2 Páginas: 169-181
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