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Article ; Online: Grasping for aspartate in tumour metabolism.

Fu, Accalia / Danial, Nika N

2018 Volume 20, Issue 7, Page(s) 738–739

MeSH term(s)	Aspartic Acid ; Humans ; Neoplasms
Chemical Substances	Aspartic Acid (30KYC7MIAI)
Language	English
Publishing date	2018-06-04
Publishing country	England
Document type	Journal Article ; Comment
ZDB-ID	1474722-4
ISSN	1476-4679 ; 1465-7392
ISSN (online)	1476-4679
ISSN	1465-7392
DOI	10.1038/s41556-018-0137-9
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Zs.A 5169: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 12: Show issues

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Article ; Online: Mitochondrial pyruvate supports lymphoma proliferation by fueling a glutamate pyruvate transaminase 2-dependent glutaminolysis pathway.

Wei, Peng / Bott, Alex J / Cluntun, Ahmad A / Morgan, Jeffrey T / Cunningham, Corey N / Schell, John C / Ouyang, Yeyun / Ficarro, Scott B / Marto, Jarrod A / Danial, Nika N / DeBerardinis, Ralph J / Rutter, Jared

Science advances

2022 Volume 8, Issue 39, Page(s) eabq0117

Abstract: The fate of pyruvate is a defining feature in many cell types. One major fate is mitochondrial entry via the mitochondrial pyruvate carrier (MPC). We found that diffuse large B cell lymphomas (DLBCLs) consume mitochondrial pyruvate via glutamate-pyruvate ...

Abstract	The fate of pyruvate is a defining feature in many cell types. One major fate is mitochondrial entry via the mitochondrial pyruvate carrier (MPC). We found that diffuse large B cell lymphomas (DLBCLs) consume mitochondrial pyruvate via glutamate-pyruvate transaminase 2 to enable α-ketoglutarate production as part of glutaminolysis. This led us to discover that glutamine exceeds pyruvate as a carbon source for the tricarboxylic acid cycle in DLBCLs. As a result, MPC inhibition led to decreased glutaminolysis in DLBCLs, opposite to previous observations in other cell types. We also found that MPC inhibition or genetic depletion decreased DLBCL proliferation in an extracellular matrix (ECM)-like environment and xenografts, but not in a suspension environment. Moreover, the metabolic profile of DLBCL cells in ECM is markedly different from cells in a suspension environment. Thus, we conclude that the synergistic consumption and assimilation of glutamine and pyruvate enables DLBCL proliferation in an extracellular environment-dependent manner.
Language	English
Publishing date	2022-09-30
Publishing country	United States
Document type	Journal Article
ZDB-ID	2810933-8
ISSN	2375-2548 ; 2375-2548
ISSN (online)	2375-2548
ISSN	2375-2548
DOI	10.1126/sciadv.abq0117
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Article ; Online: MCL-1 is a master regulator of cancer dependency on fatty acid oxidation.

Prew, Michelle S / Adhikary, Utsarga / Choi, Dong Wook / Portero, Erika P / Paulo, Joao A / Gowda, Pruthvi / Budhraja, Amit / Opferman, Joseph T / Gygi, Steven P / Danial, Nika N / Walensky, Loren D

Cell reports

2022 Volume 41, Issue 1, Page(s) 111445

Abstract: MCL-1 is an anti-apoptotic BCL-2 family protein essential for survival of diverse cell types and is a major driver of cancer and chemoresistance. The mechanistic basis for the oncogenic supremacy of MCL-1 among its anti-apoptotic homologs is unclear and ... ...

Abstract	MCL-1 is an anti-apoptotic BCL-2 family protein essential for survival of diverse cell types and is a major driver of cancer and chemoresistance. The mechanistic basis for the oncogenic supremacy of MCL-1 among its anti-apoptotic homologs is unclear and implicates physiologic roles of MCL-1 beyond apoptotic suppression. Here we find that MCL-1-dependent hematologic cancer cells specifically rely on fatty acid oxidation (FAO) as a fuel source because of metabolic wiring enforced by MCL-1 itself. We demonstrate that FAO regulation by MCL-1 is independent of its anti-apoptotic activity, based on metabolomic, proteomic, and genomic profiling of MCL-1-dependent leukemia cells lacking an intact apoptotic pathway. Genetic deletion of Mcl-1 results in transcriptional downregulation of FAO pathway proteins such that glucose withdrawal triggers cell death despite apoptotic blockade. Our data reveal that MCL-1 is a master regulator of FAO, rendering MCL-1-driven cancer cells uniquely susceptible to treatment with FAO inhibitors.
MeSH term(s)	Apoptosis ; Apoptosis Regulatory Proteins/metabolism ; Cell Line, Tumor ; Fatty Acids ; Glucose ; Myeloid Cell Leukemia Sequence 1 Protein/genetics ; Myeloid Cell Leukemia Sequence 1 Protein/metabolism ; Neoplasms/genetics ; Proteomics ; Proto-Oncogene Proteins c-bcl-2/metabolism
Chemical Substances	Apoptosis Regulatory Proteins ; Fatty Acids ; Myeloid Cell Leukemia Sequence 1 Protein ; Proto-Oncogene Proteins c-bcl-2 ; Glucose (IY9XDZ35W2)
Language	English
Publishing date	2022-10-05
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2022.111445
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Article: BCL-2 family proteins: critical checkpoints of apoptotic cell death.

Danial, Nika N

Clinical cancer research : an official journal of the American Association for Cancer Research

2007 Volume 13, Issue 24, Page(s) 7254–7263

Abstract: Apoptosis is a morphologically distinct form of programmed cell death essential for normal development and tissue homeostasis. Aberrant regulation of this pathway is linked to multiple human diseases, including cancer, autoimmunity, neurodegenerative ... ...

Abstract	Apoptosis is a morphologically distinct form of programmed cell death essential for normal development and tissue homeostasis. Aberrant regulation of this pathway is linked to multiple human diseases, including cancer, autoimmunity, neurodegenerative disorders, and diabetes. The BCL-2 family of proteins constitutes a critical control point in apoptosis residing immediately upstream of irreversible cellular damage, where family members control the release of apoptogenic factors from mitochondria. The cardinal member of this family, BCL-2, was originally discovered as the defining oncogene in follicular lymphomas, located at one reciprocal breakpoint of the t(14;18) (q32;q21) chromosomal translocation. Since this original discovery, remarkable efforts marshaled by many investigators around the world have advanced our knowledge of the basic biology, molecular mechanisms, and therapeutic targets in the apoptotic pathway. This review highlights findings from many laboratories that have helped uncover some of the critical control points in apoptosis. The emerging picture is that of an intricate cellular machinery orchestrated by tightly regulated molecular interactions and conformational changes within BCL-2 family proteins that ultimately govern the cellular commitment to apoptotic death.
MeSH term(s)	Animals ; Apoptosis/physiology ; Humans ; Multiprotein Complexes/physiology ; Proto-Oncogene Proteins c-bcl-2/physiology
Chemical Substances	Multiprotein Complexes ; Proto-Oncogene Proteins c-bcl-2
Language	English
Publishing date	2007-12-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1225457-5
ISSN	1557-3265 ; 1078-0432
ISSN (online)	1557-3265
ISSN	1078-0432
DOI	10.1158/1078-0432.CCR-07-1598
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Zs.A 4223: Show issues

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Article ; Online: Measurement of mitochondrial oxygen consumption rates in mouse primary neurons and astrocytes.

Ribeiro, Sofia M / Giménez-Cassina, Alfredo / Danial, Nika N

Methods in molecular biology (Clifton, N.J.)

2015 Volume 1241, Page(s) 59–69

Abstract: The introduction of microplate-based assays that measure extracellular fluxes in intact, living cells has revolutionized the field of cellular bioenergetics. Here, we describe a method for real time assessment of mitochondrial oxygen consumption rates in ...

Abstract	The introduction of microplate-based assays that measure extracellular fluxes in intact, living cells has revolutionized the field of cellular bioenergetics. Here, we describe a method for real time assessment of mitochondrial oxygen consumption rates in primary mouse cortical neurons and astrocytes. This method requires the Extracellular Flux Analyzer Instrument (XF24, Seahorse Biosciences), which uses fluorescent oxygen sensors in a microplate assay format.
MeSH term(s)	Animals ; Astrocytes/cytology ; Astrocytes/metabolism ; Cell Respiration ; Cerebral Cortex/cytology ; Extracellular Space/metabolism ; Mice ; Microtechnology/methods ; Mitochondria/metabolism ; Neurons/cytology ; Neurons/metabolism ; Oxygen Consumption
Language	English
Publishing date	2015
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-1875-1_6
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Article ; Online: Regulation of mitochondrial nutrient and energy metabolism by BCL-2 family proteins.

Giménez-Cassina, Alfredo / Danial, Nika N

Trends in endocrinology and metabolism: TEM

2015 Volume 26, Issue 4, Page(s) 165–175

Abstract: Cells have evolved a highly integrated network of mechanisms to coordinate cellular survival/death, proliferation, differentiation, and repair with metabolic states. It is therefore not surprising that proteins with canonical roles in cell death/survival ...

Abstract	Cells have evolved a highly integrated network of mechanisms to coordinate cellular survival/death, proliferation, differentiation, and repair with metabolic states. It is therefore not surprising that proteins with canonical roles in cell death/survival also modulate nutrient and energy metabolism and vice versa. The finding that many BCL-2 (B cell lymphoma 2) proteins reside at mitochondria or can translocate to this organelle has long motivated investigation into their involvement in normal mitochondrial physiology and metabolism. These endeavors have led to the discovery of homeostatic roles for BCL-2 proteins beyond apoptosis. We predominantly focus on recent findings that link select BCL-2 proteins to carbon substrate utilization at the level of mitochondrial fuel choice, electron transport, and metabolite import independent of their cell death regulatory function.
MeSH term(s)	Animals ; Diet/adverse effects ; Energy Intake ; Energy Metabolism ; Homeostasis ; Humans ; Mitochondria/enzymology ; Mitochondria/metabolism ; Models, Biological ; Oxidative Phosphorylation ; Protein Transport ; Proto-Oncogene Proteins c-bcl-2/metabolism
Chemical Substances	Proto-Oncogene Proteins c-bcl-2
Language	English
Publishing date	2015-04
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1042384-9
ISSN	1879-3061 ; 1043-2760
ISSN (online)	1879-3061
ISSN	1043-2760
DOI	10.1016/j.tem.2015.02.004
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Zs.A 2999: Show issues

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Article ; Online: Mitochondrial morphology controls fatty acid utilization by changing CPT1 sensitivity to malonyl-CoA.

The EMBO journal

2023 Volume 42, Issue 11, Page(s) e111901

Abstract: Changes in mitochondrial morphology are associated with nutrient utilization, but the precise causalities and the underlying mechanisms remain unknown. Here, using cellular models representing a wide variety of mitochondrial shapes, we show a strong ... ...

Abstract	Changes in mitochondrial morphology are associated with nutrient utilization, but the precise causalities and the underlying mechanisms remain unknown. Here, using cellular models representing a wide variety of mitochondrial shapes, we show a strong linear correlation between mitochondrial fragmentation and increased fatty acid oxidation (FAO) rates. Forced mitochondrial elongation following MFN2 over-expression or DRP1 depletion diminishes FAO, while forced fragmentation upon knockdown or knockout of MFN2 augments FAO as evident from respirometry and metabolic tracing. Remarkably, the genetic induction of fragmentation phenocopies distinct cell type-specific biological functions of enhanced FAO. These include stimulation of gluconeogenesis in hepatocytes, induction of insulin secretion in islet β-cells exposed to fatty acids, and survival of FAO-dependent lymphoma subtypes. We find that fragmentation increases long-chain but not short-chain FAO, identifying carnitine O-palmitoyltransferase 1 (CPT1) as the downstream effector of mitochondrial morphology in regulation of FAO. Mechanistically, we determined that fragmentation reduces malonyl-CoA inhibition of CPT1, while elongation increases CPT1 sensitivity to malonyl-CoA inhibition. Overall, these findings underscore a physiologic role for fragmentation as a mechanism whereby cellular fuel preference and FAO capacity are determined.
MeSH term(s)	Fatty Acids/metabolism ; Malonyl Coenzyme A/metabolism ; Malonyl Coenzyme A/pharmacology ; Carnitine O-Palmitoyltransferase/genetics ; Carnitine O-Palmitoyltransferase/metabolism ; Oxidation-Reduction ; Mitochondria/metabolism
Chemical Substances	Fatty Acids ; Malonyl Coenzyme A (524-14-1) ; Carnitine O-Palmitoyltransferase (EC 2.3.1.21)
Language	English
Publishing date	2023-03-14
Publishing country	England
Document type	Journal Article
ZDB-ID	586044-1
ISSN	1460-2075 ; 0261-4189
ISSN (online)	1460-2075
ISSN	0261-4189
DOI	10.15252/embj.2022111901
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Zs.A 1808: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 100: Show issues

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Article ; Online: BAD regulates mammary gland morphogenesis by 4E-BP1-mediated control of localized translation in mouse and human models.

Githaka, John Maringa / Tripathi, Namita / Kirschenman, Raven / Patel, Namrata / Pandya, Vrajesh / Kramer, David A / Montpetit, Rachel / Zhu, Lin Fu / Sonenberg, Nahum / Fahlman, Richard P / Danial, Nika N / Underhill, D Alan / Goping, Ing Swie

Nature communications

2021 Volume 12, Issue 1, Page(s) 2939

Abstract: Elucidation of non-canonical protein functions can identify novel tissue homeostasis pathways. Herein, we describe a role for the Bcl-2 family member BAD in postnatal mammary gland morphogenesis. In ... ...

Abstract	Elucidation of non-canonical protein functions can identify novel tissue homeostasis pathways. Herein, we describe a role for the Bcl-2 family member BAD in postnatal mammary gland morphogenesis. In Bad
MeSH term(s)	Adaptor Proteins, Signal Transducing/metabolism ; Amino Acid Substitution ; Animals ; Cell Cycle Proteins/metabolism ; Cell Line ; Cell Movement/genetics ; Female ; Gene Knock-In Techniques ; Humans ; Mammary Glands, Animal/growth & development ; Mammary Glands, Animal/metabolism ; Mammary Glands, Human/growth & development ; Mammary Glands, Human/metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Models, Animal ; Morphogenesis ; Mutant Proteins/chemistry ; Mutant Proteins/genetics ; Mutant Proteins/metabolism ; Organoids/growth & development ; Organoids/metabolism ; Phosphorylation ; Protein Biosynthesis ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Serine/chemistry ; bcl-Associated Death Protein/deficiency ; bcl-Associated Death Protein/genetics ; bcl-Associated Death Protein/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; BAD protein, human ; Bad protein, mouse ; Cell Cycle Proteins ; EIF4EBP1 protein, human ; Eif4ebp1 protein, mouse ; Mutant Proteins ; RNA, Messenger ; bcl-Associated Death Protein ; Serine (452VLY9402)
Language	English
Publishing date	2021-05-19
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-021-23269-8
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Article ; Online: Glucose metabolism and pyruvate carboxylase enhance glutathione synthesis and restrict oxidative stress in pancreatic islets.

Fu, Accalia / van Rooyen, Lara / Evans, Lindsay / Armstrong, Nina / Avizonis, Daina / Kin, Tatsuya / Bird, Gregory H / Reddy, Anita / Chouchani, Edward T / Liesa-Roig, Marc / Walensky, Loren D / Shapiro, A M James / Danial, Nika N

Cell reports

2021 Volume 37, Issue 8, Page(s) 110037

Abstract: Glucose metabolism modulates the islet β cell responses to diabetogenic stress, including inflammation. Here, we probed the metabolic mechanisms that underlie the protective effect of glucose in inflammation by interrogating the metabolite profiles of ... ...

Abstract	Glucose metabolism modulates the islet β cell responses to diabetogenic stress, including inflammation. Here, we probed the metabolic mechanisms that underlie the protective effect of glucose in inflammation by interrogating the metabolite profiles of primary islets from human donors and identified de novo glutathione synthesis as a prominent glucose-driven pro-survival pathway. We find that pyruvate carboxylase is required for glutathione synthesis in islets and promotes their antioxidant capacity to counter inflammation and nitrosative stress. Loss- and gain-of-function studies indicate that pyruvate carboxylase is necessary and sufficient to mediate the metabolic input from glucose into glutathione synthesis and the oxidative stress response. Altered redox metabolism and cellular capacity to replenish glutathione pools are relevant in multiple pathologies beyond obesity and diabetes. Our findings reveal a direct interplay between glucose metabolism and glutathione biosynthesis via pyruvate carboxylase. This metabolic axis may also have implications in other settings where sustaining glutathione is essential.
MeSH term(s)	Adult ; Animals ; Antioxidants/physiology ; Female ; Glucose/metabolism ; Glutathione/biosynthesis ; Glutathione/metabolism ; Humans ; Insulin/metabolism ; Islets of Langerhans/metabolism ; Male ; Mice ; Mice, Inbred C57BL ; Middle Aged ; Oxidation-Reduction ; Oxidative Stress/physiology ; Primary Cell Culture ; Pyruvate Carboxylase/metabolism
Chemical Substances	Antioxidants ; Insulin ; Pyruvate Carboxylase (EC 6.4.1.1) ; Glutathione (GAN16C9B8O) ; Glucose (IY9XDZ35W2)
Language	English
Publishing date	2021-11-24
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2021.110037
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Article ; Online: BAD and K

Martínez-François, Juan Ramón / Fernández-Agüera, María Carmen / Nathwani, Nidhi / Lahmann, Carolina / Burnham, Veronica L / Danial, Nika N / Yellen, Gary

eLife

2018 Volume 7

Abstract: Brain metabolism can profoundly influence neuronal excitability. Mice with genetic deletion or alteration ... ...

Abstract	Brain metabolism can profoundly influence neuronal excitability. Mice with genetic deletion or alteration of
MeSH term(s)	Animals ; Entorhinal Cortex/physiology ; KATP Channels/metabolism ; Mice ; Mice, Knockout ; Neurons/physiology ; Seizures/physiopathology ; bcl-Associated Death Protein/genetics ; bcl-Associated Death Protein/metabolism
Chemical Substances	Bad protein, mouse ; KATP Channels ; bcl-Associated Death Protein
Language	English
Publishing date	2018-01-25
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.32721
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