
DOI . ORG {
}
Title[redir]:
BCL-2 family: integrating stress responses at the ER to control cell demise | Cell Death & Differentiation
Description:
In the last decade, the endoplasmic reticulum (ER) has emerged as a central organelle regulating the core mitochondrial apoptosis pathway. At the ER membrane, a variety of stress signals are integrated toward determining cell fate, involving a complex cross talk between key homeostatic pathways including the unfolded protein response, autophagy, calcium signaling and mitochondrial bioenergetics. In this context, key regulators of cell death of the BCL-2 and TMBIM/BI-1 family of proteins have relevant functions as stress rheostats mediated by the formation of distinct protein complexes that regulate the switch between adaptive and proapoptotic phases under stress. Here, we overview recent advances on our molecular understanding of how the apoptotic machinery integrates stress signals toward cell fate decisions upstream of the mitochondrial gateway of death.
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Keywords {🔍}
pubmed, cell, article, bcl, google, scholar, cas, apoptosis, proteins, stress, family, death, bax, central, calcium, protein, mitochondrial, membrane, bhonly, autophagy, regulation, bak, biol, release, endoplasmic, control, reticulum, signaling, upr, response, activation, members, mitochondria, proapoptotic, tmbim, bok, mol, nature, pathway, activity, figure, antiapoptotic, chem, momp, role, ireα, hetz, permeabilization, homeostasis, sci,
Topics {✒️}
nature portfolio scientific research fa9550-16-1-0384 permissions reprints privacy policy dynamic nature naval research-global advertising c-jun n-terminal kinase nature 2016 nature 2005 nature open questions social media bax-bak1-independent lc3b lipidation ire1alpha-mediated nf-kappab activation triggering mptp-driven necrosis/apoptosis ip3-receptor-mediated ca2+ signaling author information authors genuine multi-bh-domain protein bravo-san pedro jm regulated ire1-dependent decay x-box binding protein-1 ph-sensitive calcium leak research n-terminal unstructured loop specialized cysteine–aspartic proteases nanoscale super-resolution microscopy pore-forming bacterial toxins author correspondence calcium-dependent mitochondrial enzymes higher-order homo-oligomers calcium-dependent cytosolic enzymes mouse development normal development central stress pathways bak double-deficient cells32 stress-induced cell death amphiphilic squalene-based compound personal data golgi anti-apoptotic protein hypoxia-inducible factor induction permeability transition pore mitochondrial permeability transition central organelle regulating ip3r-dependent calcium release insp3 receptor gating endoplasmic reticulum ca2+ er stress-induced apoptosis ip3-mediated calcium release data protection
Questions {❓}
- Are TMBIM proteins ion channels?
- Do BCL-2-related proteins modulate the switch between proadaptive to proapoptotic ER stress responses?
- How does ER permeabilization lead to cell death?
- What is the functional relationship between proteins of the BCL-2 and TMBIM families in the regulation of cell death?
- What is the relationship between the TMBIM and the BCL-2 protein family?
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headline:BCL-2 family: integrating stress responses at the ER to control cell demise
description:In the last decade, the endoplasmic reticulum (ER) has emerged as a central organelle regulating the core mitochondrial apoptosis pathway. At the ER membrane, a variety of stress signals are integrated toward determining cell fate, involving a complex cross talk between key homeostatic pathways including the unfolded protein response, autophagy, calcium signaling and mitochondrial bioenergetics. In this context, key regulators of cell death of the BCL-2 and TMBIM/BI-1 family of proteins have relevant functions as stress rheostats mediated by the formation of distinct protein complexes that regulate the switch between adaptive and proapoptotic phases under stress. Here, we overview recent advances on our molecular understanding of how the apoptotic machinery integrates stress signals toward cell fate decisions upstream of the mitochondrial gateway of death.
datePublished:2017-06-16T00:00:00Z
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Apoptosis
Endoplasmic reticulum
Intracellular signalling peptides and proteins
Stress signalling
Life Sciences
general
Biochemistry
Cell Biology
Stem Cells
Cell Cycle Analysis
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headline:BCL-2 family: integrating stress responses at the ER to control cell demise
description:In the last decade, the endoplasmic reticulum (ER) has emerged as a central organelle regulating the core mitochondrial apoptosis pathway. At the ER membrane, a variety of stress signals are integrated toward determining cell fate, involving a complex cross talk between key homeostatic pathways including the unfolded protein response, autophagy, calcium signaling and mitochondrial bioenergetics. In this context, key regulators of cell death of the BCL-2 and TMBIM/BI-1 family of proteins have relevant functions as stress rheostats mediated by the formation of distinct protein complexes that regulate the switch between adaptive and proapoptotic phases under stress. Here, we overview recent advances on our molecular understanding of how the apoptotic machinery integrates stress signals toward cell fate decisions upstream of the mitochondrial gateway of death.
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Endoplasmic reticulum
Intracellular signalling peptides and proteins
Stress signalling
Life Sciences
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Biochemistry
Cell Biology
Stem Cells
Cell Cycle Analysis
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