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Article ; Online: Breaking Bad and Breaking Good: β-Cell Autophagy Pathways in Diabetes.

Vivot, Kevin / Pasquier, Adrien / Goginashvili, Alexander / Ricci, Romeo

2019 Volume 432, Issue 5, Page(s) 1494–1513

Abstract: For many decades the lysosome has been recognized as the terminal center of cellular waste disposal. Products of lysosomal degradation are either recycled in biosynthetic pathways or are further metabolized to produce energy. As such the lysosome was ... ...

Abstract	For many decades the lysosome has been recognized as the terminal center of cellular waste disposal. Products of lysosomal degradation are either recycled in biosynthetic pathways or are further metabolized to produce energy. As such the lysosome was attributed a rather passive role in cellular metabolism merely transforming bulk material into small metabolites. More recently, however, the emerging evidence has brought the lysosome to the center of nutrient sensing as the organelle that harbors a complex signaling machinery which dynamically and actively regulates cell metabolism. The pancreatic β cell is unique in as much as nutrient sensing is directly coupled to insulin secretion. Importantly, defects in insulin secretion constitute a hallmark in the progression of patients from a state of impaired glucose tolerance to full blown type 2 diabetes (T2D). However, mechanisms linking nutrient-dependent lysosomal function to insulin secretion and more generally to β cell health have evolved only very recently. This review discusses emerging concepts in macroautophagy and macroautophagy-independent processes of cargo delivery to lysosomes as well as nutrient-dependent lysosomal signaling specifically in the context of β cell function in health and disease. Such mechanisms may provide a novel source of therapeutic targets to be exploited in the context of β cell failure in diabetes in the near future.
MeSH term(s)	Animals ; Autophagy/physiology ; Diabetes Mellitus, Type 2/metabolism ; Humans ; Hydrolases/metabolism ; Insulin/biosynthesis ; Insulin/metabolism ; Insulin-Secreting Cells/metabolism ; Lysosomes/metabolism ; Nutrients/metabolism ; Protein Transport ; Signal Transduction
Chemical Substances	Insulin ; Hydrolases (EC 3.-)
Language	English
Publishing date	2019-08-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2019.07.030
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Article: Breaking Bad and Breaking Good: β-Cell Autophagy Pathways in Diabetes

Vivot, Kevin / Pasquier, Adrien / Goginashvili, Alexander / Ricci, Romeo

Elsevier Ltd Journal of molecular biology. 2019 July 19,

2019

Abstract	For many decades the lysosome has been recognized as the terminal center of cellular waste disposal. Products of lysosomal degradation are either recycled in biosynthetic pathways or are further metabolized to produce energy. As such the lysosome was attributed a rather passive role in cellular metabolism merely transforming bulk material into small metabolites. More recently, however, the emerging evidence has brought the lysosome to the center of nutrient sensing as the organelle that harbors a complex signaling machinery which dynamically and actively regulates cell metabolism.The pancreatic β cell is unique in as much as nutrient sensing is directly coupled to insulin secretion. Importantly, defects in insulin secretion constitute a hallmark in the progression of patients from a state of impaired glucose tolerance to full blown type 2 diabetes (T2D). However, mechanisms linking nutrient-dependent lysosomal function to insulin secretion and more generally to β cell health have evolved only very recently. This review discusses emerging concepts in macroautophagy and macroautophagy-independent processes of cargo delivery to lysosomes as well as nutrient-dependent lysosomal signaling specifically in the context of β cell function in health and disease. Such mechanisms may provide a novel source of therapeutic targets to be exploited in the context of β cell failure in diabetes in the near future.
Keywords	autophagy ; biochemical pathways ; energy ; glucose tolerance ; insulin secretion ; islets of Langerhans ; lysosomes ; metabolites ; noninsulin-dependent diabetes mellitus ; patients ; therapeutics ; waste disposal
Language	English
Dates of publication	2019-0719
Publishing place	Elsevier Ltd
Document type	Article
Note	Pre-press version
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2019.07.030
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Article ; Online: Lysosomes in nutrient signalling: A focus on pancreatic β-cells.

Mészáros, Gergő / Pasquier, Adrien / Vivot, Kevin / Goginashvili, Alexander / Ricci, Romeo

Diabetes, obesity & metabolism

2018 Volume 20 Suppl 2, Page(s) 104–115

Abstract: Regulated insulin secretion from pancreatic β-cells is a major process maintaining glucose homeostasis in mammals. Enhancing insulin release in response to chronic nutrient overload and obesity-related insulin resistance (pre-diabetes) requires several ... ...

Abstract	Regulated insulin secretion from pancreatic β-cells is a major process maintaining glucose homeostasis in mammals. Enhancing insulin release in response to chronic nutrient overload and obesity-related insulin resistance (pre-diabetes) requires several adaptive cellular mechanisms maintaining β-cell health under such stresses. Once these mechanisms are overwhelmed, β-cell failure occurs leading to full-blown Type 2 Diabetes (T2D). Nutrient-dependent macroautophagy represents one such adaptive mechanism in β-cells. While macroautophagy levels are high and protective in β-cells in pre-diabetes, they decrease at later stages contributing to β-cell failure. However, mechanisms compromising macroautophagy in β-cells remain poorly understood. In this review, we discuss how recently discovered signalling cascades that emanate from the limiting membrane of lysosomes contribute to changes in macroautophagy flux in physiology and disease. In particular, these mechanisms are put into context with β-cell function highlighting most recently described links between nutrient-dependent lysosomal signalling pathways and insulin secretion. Understanding these mechanisms in response to metabolic stress might pave the way for development of more tailored treatment strategies aimed at preserving β-cell health.
MeSH term(s)	Autophagy/physiology ; Diabetes Mellitus, Type 2/physiopathology ; Energy Metabolism/physiology ; Humans ; Insulin/metabolism ; Insulin Secretion/physiology ; Insulin-Secreting Cells/physiology ; Intracellular Membranes/enzymology ; Lysosomes/physiology ; Mechanistic Target of Rapamycin Complex 1/metabolism ; Nutrients/metabolism ; Protein Kinases/metabolism ; Signal Transduction/physiology
Chemical Substances	Insulin ; Nutrients ; Protein Kinases (EC 2.7.-) ; AMP-activated protein kinase kinase (EC 2.7.1.-) ; Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1)
Language	English
Publishing date	2018-09-19
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1454944-x
ISSN	1463-1326 ; 1462-8902
ISSN (online)	1463-1326
ISSN	1462-8902
DOI	10.1111/dom.13389
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Article ; Online: TFEB and TFE3 control glucose homeostasis by regulating insulin gene expression.

Pasquier, Adrien / Pastore, Nunzia / D'Orsi, Luca / Colonna, Rita / Esposito, Alessandra / Maffia, Veronica / De Cegli, Rossella / Mutarelli, Margherita / Ambrosio, Susanna / Tufano, Gennaro / Grimaldi, Antonio / Cesana, Marcella / Cacchiarelli, Davide / Delalleau, Nathalie / Napolitano, Gennaro / Ballabio, Andrea

The EMBO journal

2023 Volume 42, Issue 21, Page(s) e113928

Abstract: To fulfill their function, pancreatic beta cells require precise nutrient-sensing mechanisms that control insulin production. Transcription factor EB (TFEB) and its homolog TFE3 have emerged as crucial regulators of the adaptive response of cell ... ...

Abstract	To fulfill their function, pancreatic beta cells require precise nutrient-sensing mechanisms that control insulin production. Transcription factor EB (TFEB) and its homolog TFE3 have emerged as crucial regulators of the adaptive response of cell metabolism to environmental cues. Here, we show that TFEB and TFE3 regulate beta-cell function and insulin gene expression in response to variations in nutrient availability. We found that nutrient deprivation in beta cells promoted TFEB/TFE3 activation, which resulted in suppression of insulin gene expression. TFEB overexpression was sufficient to inhibit insulin transcription, whereas beta cells depleted of both TFEB and TFE3 failed to suppress insulin gene expression in response to amino acid deprivation. Interestingly, ChIP-seq analysis showed binding of TFEB to super-enhancer regions that regulate insulin transcription. Conditional, beta-cell-specific, Tfeb-overexpressing, and Tfeb/Tfe3 double-KO mice showed severe alteration of insulin transcription, secretion, and glucose tolerance, indicating that TFEB and TFE3 are important physiological mediators of pancreatic function. Our findings reveal a nutrient-controlled transcriptional mechanism that regulates insulin production, thus playing a key role in glucose homeostasis at both cellular and organismal levels.
MeSH term(s)	Animals ; Mice ; Autophagy/genetics ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors/genetics ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors/metabolism ; Gene Expression ; Glucose ; Insulin ; Lysosomes/metabolism
Chemical Substances	Basic Helix-Loop-Helix Leucine Zipper Transcription Factors ; Glucose (IY9XDZ35W2) ; Insulin ; Tcfe3 protein, mouse (136896-33-8) ; Tcfeb protein, mouse
Language	English
Publishing date	2023-09-15
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	586044-1
ISSN	1460-2075 ; 0261-4189
ISSN (online)	1460-2075
ISSN	0261-4189
DOI	10.15252/embj.2023113928
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Article ; Online: Comparison of the Oilseed rape mosaic virus and Tobacco mosaic virus movement proteins (MP) reveals common and dissimilar MP functions for tobamovirus spread.

Niehl, Annette / Pasquier, Adrien / Ferriol, Inmaculada / Mély, Yves / Heinlein, Manfred

Virology

2014 Volume 456-457, Page(s) 43–54

Abstract: Tobacco mosaic virus (TMV) is a longstanding model for studying virus movement and macromolecular transport through plasmodesmata (PD). Its movement protein (MP) interacts with cortical microtubule (MT)-associated ER sites (C-MERs) to facilitate the ... ...

Abstract	Tobacco mosaic virus (TMV) is a longstanding model for studying virus movement and macromolecular transport through plasmodesmata (PD). Its movement protein (MP) interacts with cortical microtubule (MT)-associated ER sites (C-MERs) to facilitate the formation and transport of ER-associated viral replication complexes (VRCs) along the ER-actin network towards PD. To investigate whether this movement mechanism might be conserved between tobamoviruses, we compared the functions of Oilseed rape mosaic virus (ORMV) MP with those of MP(TMV). We show that MP(ORMV) supports TMV movement more efficiently than MP(TMV). Moreover, MP(ORMV) localizes to C-MERs like MP(TMV) but accumulates to lower levels and does not localize to larger inclusions/VRCs or along MTs, patterns regularly seen for MP(TMV). Our findings extend the role of C-MERs in viral cell-to-cell transport to a virus commonly used for functional genomics in Arabidopsis. Moreover, accumulation of tobamoviral MP in inclusions or along MTs is not required for virus movement.
MeSH term(s)	Arabidopsis/virology ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum/virology ; Inclusion Bodies, Viral ; Microtubules/metabolism ; Plant Viral Movement Proteins/genetics ; Plant Viral Movement Proteins/metabolism ; Tobamovirus/genetics ; Tobamovirus/physiology
Chemical Substances	Plant Viral Movement Proteins
Language	English
Publishing date	2014-05
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	200425-2
ISSN	1096-0341 ; 0042-6822
ISSN (online)	1096-0341
ISSN	0042-6822
DOI	10.1016/j.virol.2014.03.007
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Article ; Online: Analysis of Tomato spotted wilt virus NSs protein indicates the importance of the N-terminal domain for avirulence and RNA silencing suppression.

de Ronde, Dryas / Pasquier, Adrien / Ying, Su / Butterbach, Patrick / Lohuis, Dick / Kormelink, Richard

Molecular plant pathology

2013 Volume 15, Issue 2, Page(s) 185–195

Abstract: Recently, Tomato spotted wilt virus (TSWV) nonstructural protein NSs has been identified unambiguously as an avirulence (Avr) determinant for Tomato spotted wilt (Tsw)-based resistance. The observation that NSs from two natural resistance-breaking ... ...

Abstract	Recently, Tomato spotted wilt virus (TSWV) nonstructural protein NSs has been identified unambiguously as an avirulence (Avr) determinant for Tomato spotted wilt (Tsw)-based resistance. The observation that NSs from two natural resistance-breaking isolates had lost RNA silencing suppressor (RSS) activity and Avr suggested a link between the two functions. To test this, a large set of NSs mutants was generated by alanine substitutions in NSs from resistance-inducing wild-type strains (NSs(RI) ), amino acid reversions in NSs from resistance-breaking strains (NSs(RB)), domain deletions and swapping. Testing these mutants for their ability to suppress green fluorescent protein (GFP) silencing and to trigger a Tsw-mediated hypersensitive response (HR) revealed that the two functions can be separated. Changes in the N-terminal domain were found to be detrimental for both activities and indicated the importance of this domain, additionally supported by domain swapping between NSs(RI) and NSs(RB). Swapping domains between the closely related Tospovirus Groundnut ringspot virus (GRSV) NSs and TSWV NSs(RI) showed that Avr functionality could not simply be transferred between species. Although deletion of the C-terminal domain rendered NSs completely dysfunctional, only a few single-amino-acid mutations in the C-terminus affected both functions. Mutation of a GW/WG motif (position 17/18) rendered NSs completely dysfunctional for RSS and Avr activity, and indicated a putative interaction between NSs and Argonaute 1 (AGO1), and its importance in TSWV virulence and viral counter defence against RNA interference.
MeSH term(s)	Amino Acid Sequence ; Gene Silencing ; Green Fluorescent Proteins/chemistry ; Molecular Sequence Data ; RNA, Viral/genetics ; Sequence Homology, Amino Acid ; Tospovirus/genetics ; Tospovirus/metabolism ; Tospovirus/pathogenicity ; Viral Nonstructural Proteins/chemistry ; Viral Nonstructural Proteins/metabolism ; Virulence
Chemical Substances	RNA, Viral ; Viral Nonstructural Proteins ; Green Fluorescent Proteins (147336-22-9)
Language	English
Publishing date	2013-12-05
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2020755-4
ISSN	1364-3703 ; 1464-6722
ISSN (online)	1364-3703
ISSN	1464-6722
DOI	10.1111/mpp.12082
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Article ; Online: Lysosomal degradation of newly formed insulin granules contributes to β cell failure in diabetes.

Nature communications

2019 Volume 10, Issue 1, Page(s) 3312

Abstract: Compromised function of insulin-secreting pancreatic β cells is central to the development and progression of Type 2 Diabetes (T2D). However, the mechanisms underlying β cell failure remain incompletely understood. Here, we report that metabolic stress ... ...

Abstract	Compromised function of insulin-secreting pancreatic β cells is central to the development and progression of Type 2 Diabetes (T2D). However, the mechanisms underlying β cell failure remain incompletely understood. Here, we report that metabolic stress markedly enhances macroautophagy-independent lysosomal degradation of nascent insulin granules. In different model systems of diabetes including of human origin, stress-induced nascent granule degradation (SINGD) contributes to loss of insulin along with mammalian/mechanistic Target of Rapamycin (mTOR)-dependent suppression of macroautophagy. Expression of Protein Kinase D (PKD), a negative regulator of SINGD, is reduced in diabetic β cells. Pharmacological activation of PKD counters SINGD and delays the onset of T2D. Conversely, inhibition of PKD exacerbates SINGD, mitigates insulin secretion and accelerates diabetes. Finally, reduced levels of lysosomal tetraspanin CD63 prevent SINGD, leading to increased insulin secretion. Overall, our findings implicate aberrant SINGD in the pathogenesis of diabetes and suggest new therapeutic strategies to prevent β cell failure.
MeSH term(s)	Animals ; Diabetes Mellitus, Type 2/genetics ; Diabetes Mellitus, Type 2/metabolism ; Diabetes Mellitus, Type 2/physiopathology ; Humans ; Insulin/chemistry ; Insulin/metabolism ; Insulin Secretion ; Insulin-Secreting Cells/cytology ; Insulin-Secreting Cells/metabolism ; Lysosomes/metabolism ; Macroautophagy ; Male ; Mice, Inbred C57BL ; Protein Kinase C/genetics ; Protein Kinase C/metabolism ; TOR Serine-Threonine Kinases/genetics ; TOR Serine-Threonine Kinases/metabolism
Chemical Substances	Insulin ; TOR Serine-Threonine Kinases (EC 2.7.1.1) ; protein kinase D (EC 2.7.10.-) ; Protein Kinase C (EC 2.7.11.13)
Language	English
Publishing date	2019-07-25
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/s41467-019-11170-4
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Article ; Online: Micro-MRI study of cerebral aging: ex vivo detection of hippocampal subfield reorganization, microhemorrhages and amyloid plaques in mouse lemur primates.

Bertrand, Anne / Pasquier, Adrien / Petiet, Alexandra / Wiggins, Christopher / Kraska, Audrey / Joseph-Mathurin, Nelly / Aujard, Fabienne / Mestre-Francés, Nadine / Dhenain, Marc

PloS one

2013 Volume 8, Issue 2, Page(s) e56593

Abstract: Mouse lemurs are non-human primate models of cerebral aging and neurodegeneration. Much smaller than other primates, they recapitulate numerous features of human brain aging, including progressive cerebral atrophy and correlation between regional atrophy ...

Abstract	Mouse lemurs are non-human primate models of cerebral aging and neurodegeneration. Much smaller than other primates, they recapitulate numerous features of human brain aging, including progressive cerebral atrophy and correlation between regional atrophy and cognitive impairments. Characterization of brain atrophy in mouse lemurs has been done by MRI measures of regional CSF volume and by MRI measures of regional atrophy. Here, we further characterize mouse lemur brain aging using ex vivo MR microscopy (31 µm in-plane resolution). First, we performed a non-biased, direct volumetric quantification of dentate gyrus and extended Ammon's horn. We show that both dentate gyrus and Ammon's horn undergo an age-related reorganization leading to a growth of the dentate gyrus and an atrophy of the Ammon's horn, even in the absence of global hippocampal atrophy. Second, on these first MR microscopic images of the mouse lemur brain, we depicted cortical and hippocampal hypointense spots. We demonstrated that their incidence increases with aging and that they correspond either to amyloid deposits or to cerebral microhemorrhages.
MeSH term(s)	Aging/pathology ; Animals ; Cerebral Cortex/pathology ; Cerebral Cortex/physiopathology ; Cheirogaleidae/physiology ; Hippocampus/pathology ; Hippocampus/physiopathology ; Humans ; Intracranial Hemorrhages/complications ; Intracranial Hemorrhages/pathology ; Intracranial Hemorrhages/physiopathology ; Magnetic Resonance Imaging ; Plaque, Amyloid/complications ; Plaque, Amyloid/pathology ; Plaque, Amyloid/physiopathology
Language	English
Publishing date	2013-02-27
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0056593
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Article ; Online: Insulin granules. Insulin secretory granules control autophagy in pancreatic β cells.

Goginashvili, Alexander / Zhang, Zhirong / Erbs, Eric / Spiegelhalter, Coralie / Kessler, Pascal / Mihlan, Michael / Pasquier, Adrien / Krupina, Ksenia / Schieber, Nicole / Cinque, Laura / Morvan, Joëlle / Sumara, Izabela / Schwab, Yannick / Settembre, Carmine / Ricci, Romeo

Science (New York, N.Y.)

2015 Volume 347, Issue 6224, Page(s) 878–882

Abstract: Pancreatic β cells lower insulin release in response to nutrient depletion. The question of whether starved β cells induce macroautophagy, a predominant mechanism maintaining energy homeostasis, remains poorly explored. We found that, in contrast to many ...

Abstract	Pancreatic β cells lower insulin release in response to nutrient depletion. The question of whether starved β cells induce macroautophagy, a predominant mechanism maintaining energy homeostasis, remains poorly explored. We found that, in contrast to many mammalian cells, macroautophagy in pancreatic β cells was suppressed upon starvation. Instead, starved β cells induced lysosomal degradation of nascent secretory insulin granules, which was controlled by protein kinase D (PKD), a key player in secretory granule biogenesis. Starvation-induced nascent granule degradation triggered lysosomal recruitment and activation of mechanistic target of rapamycin that suppressed macroautophagy. Switching from macroautophagy to insulin granule degradation was important to keep insulin secretion low upon fasting. Thus, β cells use a PKD-dependent mechanism to adapt to nutrient availability and couple autophagy flux to secretory function.
MeSH term(s)	Animals ; Autophagy ; Cells, Cultured ; Fasting ; Humans ; Insulin/metabolism ; Insulin Secretion ; Insulin-Secreting Cells/metabolism ; Insulin-Secreting Cells/physiology ; Insulin-Secreting Cells/ultrastructure ; Mice ; Mice, Mutant Strains ; Mice, Transgenic ; Mitogen-Activated Protein Kinase 13/genetics ; Protein Kinase C/physiology ; Secretory Vesicles/metabolism ; Secretory Vesicles/physiology
Chemical Substances	Insulin ; Mitogen-Activated Protein Kinase 13 (EC 2.7.1.-) ; protein kinase D (EC 2.7.10.-) ; Protein Kinase C (EC 2.7.11.13)
Language	English
Publishing date	2015-01-05
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	128410-1
ISSN	1095-9203 ; 0036-8075
ISSN (online)	1095-9203
ISSN	0036-8075
DOI	10.1126/science.aaa2628
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Article ; Online: Protein kinase D at the Golgi controls NLRP3 inflammasome activation.

Zhang, Zhirong / Meszaros, Gergö / He, Wan-Ting / Xu, Yanfang / de Fatima Magliarelli, Helena / Mailly, Laurent / Mihlan, Michael / Liu, Yansheng / Puig Gámez, Marta / Goginashvili, Alexander / Pasquier, Adrien / Bielska, Olga / Neven, Bénédicte / Quartier, Pierre / Aebersold, Rudolf / Baumert, Thomas F / Georgel, Philippe / Han, Jiahuai / Ricci, Romeo

The Journal of experimental medicine

2017 Volume 214, Issue 9, Page(s) 2671–2693

Abstract: The inflammasomes are multiprotein complexes sensing tissue damage and infectious agents to initiate innate immune responses. Different inflammasomes containing distinct sensor molecules exist. The NLRP3 inflammasome is unique as it detects a variety of ... ...

Abstract	The inflammasomes are multiprotein complexes sensing tissue damage and infectious agents to initiate innate immune responses. Different inflammasomes containing distinct sensor molecules exist. The NLRP3 inflammasome is unique as it detects a variety of danger signals. It has been reported that NLRP3 is recruited to mitochondria-associated endoplasmic reticulum membranes (MAMs) and is activated by MAM-derived effectors. Here, we show that in response to inflammasome activators, MAMs localize adjacent to Golgi membranes. Diacylglycerol (DAG) at the Golgi rapidly increases, recruiting protein kinase D (PKD), a key effector of DAG. Upon PKD inactivation, self-oligomerized NLRP3 is retained at MAMs adjacent to Golgi, blocking assembly of the active inflammasome. Importantly, phosphorylation of NLRP3 by PKD at the Golgi is sufficient to release NLRP3 from MAMs, resulting in assembly of the active inflammasome. Moreover, PKD inhibition prevents inflammasome autoactivation in peripheral blood mononuclear cells from patients carrying NLRP3 mutations. Hence, Golgi-mediated PKD signaling is required and sufficient for NLRP3 inflammasome activation.
MeSH term(s)	Animals ; Diglycerides/metabolism ; Endoplasmic Reticulum/physiology ; Golgi Apparatus/physiology ; Humans ; Inflammasomes/physiology ; Leukocytes, Mononuclear/metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; NLR Family, Pyrin Domain-Containing 3 Protein/physiology ; Phosphorylation ; Protein Kinase C/physiology
Chemical Substances	Diglycerides ; Inflammasomes ; NLR Family, Pyrin Domain-Containing 3 Protein ; Nlrp3 protein, mouse ; protein kinase D (EC 2.7.10.-) ; Protein Kinase C (EC 2.7.11.13)
Language	English
Publishing date	2017-07-17
Publishing country	United States
Document type	Journal Article
ZDB-ID	218343-2
ISSN	1540-9538 ; 0022-1007
ISSN (online)	1540-9538
ISSN	0022-1007
DOI	10.1084/jem.20162040
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