Loss of TSC2 confers resistance to ceramide and nutrient deprivation

Nutrient stress that produces quiescence and catabolism in normal cells is lethal to cancer cells, because oncogenic mutations constitutively drive anabolism. One driver of biosynthesis in cancer cells is the mammalian target of rapamycin complex 1 (mTORC1) signaling complex. Activating mTORC1 by de...

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Published inOncogene Vol. 33; no. 14; pp. 1776 - 1787
Main Authors Guenther, G G, Liu, G, Ramirez, M U, McMonigle, R J, Kim, S M, McCracken, A N, Joo, Y, Ushach, I, Nguyen, N L, Edinger, A L
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 03.04.2014
Nature Publishing Group
Subjects
631/67
631/80/86/2369
692/420/755
692/699/67/395
Adenosine Triphosphate - chemistry
Amino acids
Animals
Apoptosis
Biological Transport
Biosynthesis
Cancer
Care and treatment
Cell Biology
Ceramide
Ceramides
Ceramides - pharmacology
Chemotherapy
Culture Media - chemistry
Drug resistance
Embryo fibroblasts
Fibroblasts - metabolism
Gene Deletion
Genetic aspects
Glucose
Glucose - metabolism
Glucose Transporter Type 1 - metabolism
Human Genetics
Hypersensitivity
Internal Medicine
Mechanistic Target of Rapamycin Complex 1
Medicine
Medicine & Public Health
Mice
Multiprotein Complexes - metabolism
Neoplastic processes
Oncology
Oncology, Experimental
original-article
Properties
Protein transport
Proteins
Rapamycin
ras Proteins - metabolism
Signal Transduction
Stress, Physiological
TOR protein
TOR Serine-Threonine Kinases - metabolism
Tuberous sclerosis
Tuberous Sclerosis Complex 2
Tumor Suppressor Proteins - genetics
Tumor Suppressor Proteins - metabolism
mTOR
GLUT1
TSC2
ceramide
nutrient transporters
4F2hc
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Abstract Nutrient stress that produces quiescence and catabolism in normal cells is lethal to cancer cells, because oncogenic mutations constitutively drive anabolism. One driver of biosynthesis in cancer cells is the mammalian target of rapamycin complex 1 (mTORC1) signaling complex. Activating mTORC1 by deleting its negative regulator tuberous sclerosis complex 2 (TSC2) leads to hypersensitivity to glucose deprivation. We have previously shown that ceramide kills cells in part by triggering nutrient transporter loss and restricting access to extracellular amino acids and glucose, suggesting that TSC2-deficient cells would be hypersensitive to ceramide. However, murine embryonic fibroblasts (MEFs) lacking TSC2 were highly resistant to ceramide-induced death. Consistent with the observation that ceramide limits access to both amino acids and glucose, TSC2 −/− MEFs also had a survival advantage when extracellular amino acids and glucose were both reduced. As TSC2 −/− MEFs were resistant to nutrient stress despite sustained mTORC1 activity, we assessed whether mTORC1 signaling might be beneficial under these conditions. In low amino acid and glucose medium, and following ceramide-induced nutrient transporter loss, elevated mTORC1 activity significantly enhanced the adaptive upregulation of new transporter proteins for amino acids and glucose. Strikingly, the introduction of oncogenic Ras abrogated the survival advantage of TSC2 −/− MEFs upon ceramide treatment most likely by increasing nutrient demand. These results suggest that, in the absence of oncogene-driven biosynthetic demand, mTORC1-dependent translation facilitates the adaptive cellular response to nutrient stress.
AbstractList Nutrient stress that produces quiescence and catabolism in normal cells is lethal to cancer cells, because oncogenic mutations constitutively drive anabolism. One driver of biosynthesis in cancer cells is the mammalian target of rapamycin complex 1 (mTORC1) signaling complex. Activating mTORC1 by deleting its negative regulator tuberous sclerosis complex 2 (TSC2) leads to hypersensitivity to glucose deprivation. We have previously shown that ceramide kills cells in part by triggering nutrient transporter loss and restricting access to extracellular amino acids and glucose, suggesting that TSC2-deficient cells would be hypersensitive to ceramide. However, murine embryonic fibroblasts (MEFs) lacking TSC2 were highly resistant to ceramide-induced death. Consistent with the observation that ceramide limits access to both amino acids and glucose, TSC2−/− MEFs also had a survival advantage when extracellular amino acids and glucose were both reduced. As TSC2−/− MEFs were resistant to nutrient stress despite sustained mTORC1 activity, we assessed whether mTORC1 signaling might be beneficial under these conditions. In low amino acid and glucose medium, and following ceramide-induced nutrient transporter loss, elevated mTORC1 activity significantly enhanced the adaptive upregulation of new transporter proteins for amino acids and glucose. Strikingly, the introduction of oncogenic Ras abrogated the survival advantage of TSC2−/− MEFs upon ceramide treatment most likely by increasing nutrient demand. These results suggest that, in the absence of oncogene-driven biosynthetic demand, mTORC1-dependent translation facilitates the adaptive cellular response to nutrient stress.
Nutrient stress that produces quiescence and catabolism in normal cells is lethal to cancer cells, because oncogenic mutations constitutively drive anabolism. One driver of biosynthesis in cancer cells is the mammalian target of rapamycin complex 1 (mTORC1) signaling complex. Activating mTORC1 by deleting its negative regulator tuberous sclerosis complex 2 (TSC2) leads to hypersensitivity to glucose deprivation. We have previously shown that ceramide kills cells in part by triggering nutrient transporter loss and restricting access to extracellular amino acids and glucose, suggesting that TSC2-deficient cells would be hypersensitive to ceramide. However, murine embryonic fibroblasts (MEFs) lacking TSC2 were highly resistant to ceramide-induced death. Consistent with the observation that ceramide limits access to both amino acids and glucose, [TSC2.sup.-/-] MEFs also had a survival advantage when extracellular amino acids and glucose were both reduced. As [TSC2.sup.-/-] MEFs were resistant to nutrient stress despite sustained mTORC1 activity, we assessed whether mTORC1 signaling might be beneficial under these conditions. In low amino acid and glucose medium, and following ceramide-induced nutrient transporter loss, elevated mTORC1 activity significantly enhanced the adaptive upregulation of new transporter proteins for amino acids and glucose. Strikingly, the introduction of oncogenic Ras abrogated the survival advantage of [TSC2.sup.-/-] MEFs upon ceramide treatment most likely by increasing nutrient demand. These results suggest that, in the absence of oncogene-driven biosynthetic demand, mTORC1-dependent translation facilitates the adaptive cellular response to nutrient stress.
Nutrient stress that produces quiescence and catabolism in normal cells is lethal to cancer cells because oncogenic mutations constitutively drive anabolism. One driver of biosynthesis in cancer cells is the mTORC1 signaling complex. Activating mTORC1 by deleting its negative regulator TSC2 leads to hypersensitivity to glucose deprivation. We have previously shown that ceramide kills cells in part by triggering nutrient transporter loss and restricting access to extracellular amino acids and glucose suggesting that TSC2-deficient cells would be hypersensitive to ceramide. However, murine embryonic fibroblasts (MEFs) lacking TSC2 were highly resistant to ceramide-induced death. Consistent with the observation that ceramide limits access to both amino acids and glucose, TSC2 −/− MEFs also had a survival advantage when extracellular amino acids and glucose were both reduced. As TSC2 −/− MEFs were resistant to nutrient stress despite sustained mTORC1 activity, we assessed whether mTORC1 signaling might be beneficial under these conditions. In low amino acid and glucose medium and following ceramide-induced nutrient transporter loss, elevated mTORC1 activity significantly enhanced the adaptive up-regulation of new transporter proteins for amino acids and glucose. Strikingly, the introduction of oncogenic Ras abrogated the survival advantage of TSC2 −/− MEFs upon ceramide treatment most likely by increasing nutrient demand. These results suggest that, in the absence of oncogene-driven biosynthetic demand, mTORC1 dependent translation facilitates the adaptive cellular response to nutrient stress.
Nutrient stress that produces quiescence and catabolism in normal cells is lethal to cancer cells, because oncogenic mutations constitutively drive anabolism. One driver of biosynthesis in cancer cells is the mammalian target of rapamycin complex 1 (mTORC1) signaling complex. Activating mTORC1 by deleting its negative regulator tuberous sclerosis complex 2 (TSC2) leads to hypersensitivity to glucose deprivation. We have previously shown that ceramide kills cells in part by triggering nutrient transporter loss and restricting access to extracellular amino acids and glucose, suggesting that TSC2-deficient cells would be hypersensitive to ceramide. However, murine embryonic fibroblasts (MEFs) lacking TSC2 were highly resistant to ceramide-induced death. Consistent with the observation that ceramide limits access to both amino acids and glucose, [TSC2.sup.-/-] MEFs also had a survival advantage when extracellular amino acids and glucose were both reduced. As [TSC2.sup.-/-] MEFs were resistant to nutrient stress despite sustained mTORC1 activity, we assessed whether mTORC1 signaling might be beneficial under these conditions. In low amino acid and glucose medium, and following ceramide-induced nutrient transporter loss, elevated mTORC1 activity significantly enhanced the adaptive upregulation of new transporter proteins for amino acids and glucose. Strikingly, the introduction of oncogenic Ras abrogated the survival advantage of [TSC2.sup.-/-] MEFs upon ceramide treatment most likely by increasing nutrient demand. These results suggest that, in the absence of oncogene-driven biosynthetic demand, mTORC1-dependent translation facilitates the adaptive cellular response to nutrient stress. Oncogene (2014) 33, 1776-1787; doi: 10.1038/onc.2013.139; published online 22 April 2013 Keywords: TSC2; mTOR; nutrient transporters; 4F2hc; GLUT1; ceramide
Nutrient stress that produces quiescence and catabolism in normal cells is lethal to cancer cells, because oncogenic mutations constitutively drive anabolism. One driver of biosynthesis in cancer cells is the mammalian target of rapamycin complex 1 (mTORC1) signaling complex. Activating mTORC1 by deleting its negative regulator tuberous sclerosis complex 2 (TSC2) leads to hypersensitivity to glucose deprivation. We have previously shown that ceramide kills cells in part by triggering nutrient transporter loss and restricting access to extracellular amino acids and glucose, suggesting that TSC2-deficient cells would be hypersensitive to ceramide. However, murine embryonic fibroblasts (MEFs) lacking TSC2 were highly resistant to ceramide-induced death. Consistent with the observation that ceramide limits access to both amino acids and glucose, TSC2(-/-) MEFs also had a survival advantage when extracellular amino acids and glucose were both reduced. As TSC2(-/-) MEFs were resistant to nutrient stress despite sustained mTORC1 activity, we assessed whether mTORC1 signaling might be beneficial under these conditions. In low amino acid and glucose medium, and following ceramide-induced nutrient transporter loss, elevated mTORC1 activity significantly enhanced the adaptive upregulation of new transporter proteins for amino acids and glucose. Strikingly, the introduction of oncogenic Ras abrogated the survival advantage of TSC2(-/-) MEFs upon ceramide treatment most likely by increasing nutrient demand. These results suggest that, in the absence of oncogene-driven biosynthetic demand, mTORC1-dependent translation facilitates the adaptive cellular response to nutrient stress. [PUBLICATION ABSTRACT]
Nutrient stress that produces quiescence and catabolism in normal cells is lethal to cancer cells, because oncogenic mutations constitutively drive anabolism. One driver of biosynthesis in cancer cells is the mammalian target of rapamycin complex 1 (mTORC1) signaling complex. Activating mTORC1 by deleting its negative regulator tuberous sclerosis complex 2 (TSC2) leads to hypersensitivity to glucose deprivation. We have previously shown that ceramide kills cells in part by triggering nutrient transporter loss and restricting access to extracellular amino acids and glucose, suggesting that TSC2-deficient cells would be hypersensitive to ceramide. However, murine embryonic fibroblasts (MEFs) lacking TSC2 were highly resistant to ceramide-induced death. Consistent with the observation that ceramide limits access to both amino acids and glucose, TSC2(-/-) MEFs also had a survival advantage when extracellular amino acids and glucose were both reduced. As TSC2(-/-) MEFs were resistant to nutrient stress despite sustained mTORC1 activity, we assessed whether mTORC1 signaling might be beneficial under these conditions. In low amino acid and glucose medium, and following ceramide-induced nutrient transporter loss, elevated mTORC1 activity significantly enhanced the adaptive upregulation of new transporter proteins for amino acids and glucose. Strikingly, the introduction of oncogenic Ras abrogated the survival advantage of TSC2(-/-) MEFs upon ceramide treatment most likely by increasing nutrient demand. These results suggest that, in the absence of oncogene-driven biosynthetic demand, mTORC1-dependent translation facilitates the adaptive cellular response to nutrient stress.
Nutrient stress that produces quiescence and catabolism in normal cells is lethal to cancer cells, because oncogenic mutations constitutively drive anabolism. One driver of biosynthesis in cancer cells is the mammalian target of rapamycin complex 1 (mTORC1) signaling complex. Activating mTORC1 by deleting its negative regulator tuberous sclerosis complex 2 (TSC2) leads to hypersensitivity to glucose deprivation. We have previously shown that ceramide kills cells in part by triggering nutrient transporter loss and restricting access to extracellular amino acids and glucose, suggesting that TSC2-deficient cells would be hypersensitive to ceramide. However, murine embryonic fibroblasts (MEFs) lacking TSC2 were highly resistant to ceramide-induced death. Consistent with the observation that ceramide limits access to both amino acids and glucose, TSC2 −/− MEFs also had a survival advantage when extracellular amino acids and glucose were both reduced. As TSC2 −/− MEFs were resistant to nutrient stress despite sustained mTORC1 activity, we assessed whether mTORC1 signaling might be beneficial under these conditions. In low amino acid and glucose medium, and following ceramide-induced nutrient transporter loss, elevated mTORC1 activity significantly enhanced the adaptive upregulation of new transporter proteins for amino acids and glucose. Strikingly, the introduction of oncogenic Ras abrogated the survival advantage of TSC2 −/− MEFs upon ceramide treatment most likely by increasing nutrient demand. These results suggest that, in the absence of oncogene-driven biosynthetic demand, mTORC1-dependent translation facilitates the adaptive cellular response to nutrient stress.
Nutrient stress that produces quiescence and catabolism in normal cells is lethal to cancer cells, because oncogenic mutations constitutively drive anabolism. One driver of biosynthesis in cancer cells is the mammalian target of rapamycin complex 1 (mTORC1) signaling complex. Activating mTORC1 by deleting its negative regulator tuberous sclerosis complex 2 (TSC2) leads to hypersensitivity to glucose deprivation. We have previously shown that ceramide kills cells in part by triggering nutrient transporter loss and restricting access to extracellular amino acids and glucose, suggesting that TSC2-deficient cells would be hypersensitive to ceramide. However, murine embryonic fibroblasts (MEFs) lacking TSC2 were highly resistant to ceramide-induced death. Consistent with the observation that ceramide limits access to both amino acids and glucose, TSC2 super(-/-) MEFs also had a survival advantage when extracellular amino acids and glucose were both reduced. As TSC2 super(-/-) MEFs were resistant to nutrient stress despite sustained mTORC1 activity, we assessed whether mTORC1 signaling might be beneficial under these conditions. In low amino acid and glucose medium, and following ceramide-induced nutrient transporter loss, elevated mTORC1 activity significantly enhanced the adaptive upregulation of new transporter proteins for amino acids and glucose. Strikingly, the introduction of oncogenic Ras abrogated the survival advantage of TSC2 super(-/-) MEFs upon ceramide treatment most likely by increasing nutrient demand. These results suggest that, in the absence of oncogene-driven biosynthetic demand, mTORC1-dependent translation facilitates the adaptive cellular response to nutrient stress.
Audience Academic
Author McMonigle, R J
Guenther, G G
Liu, G
Nguyen, N L
Ushach, I
Ramirez, M U
Edinger, A L
McCracken, A N
Joo, Y
Kim, S M
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  organization: Department of Developmental and Cell Biology, University of California
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  organization: Department of Developmental and Cell Biology, University of California
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/23604129$$D View this record in MEDLINE/PubMed
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COPYRIGHT 2014 Nature Publishing Group
Copyright Nature Publishing Group Apr 3, 2014
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Sat Oct 05 05:35:11 EDT 2024
Thu Oct 10 17:01:31 EDT 2024
Thu Oct 10 18:30:15 EDT 2024
Thu Feb 22 23:28:36 EST 2024
Fri Feb 02 04:24:05 EST 2024
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Sat Sep 28 08:03:01 EDT 2024
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Issue 14
Keywords mTOR
GLUT1
TSC2
ceramide
nutrient transporters
4F2hc
Language English
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content type line 23
These authors contributed equally to this work.
OpenAccessLink https://www.nature.com/articles/onc2013139.pdf
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Snippet Nutrient stress that produces quiescence and catabolism in normal cells is lethal to cancer cells, because oncogenic mutations constitutively drive anabolism....
Nutrient stress that produces quiescence and catabolism in normal cells is lethal to cancer cells because oncogenic mutations constitutively drive anabolism....
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StartPage 1776
SubjectTerms 631/67
631/80/86/2369
692/420/755
692/699/67/395
Adenosine Triphosphate - chemistry
Amino acids
Animals
Apoptosis
Biological Transport
Biosynthesis
Cancer
Care and treatment
Cell Biology
Ceramide
Ceramides
Ceramides - pharmacology
Chemotherapy
Culture Media - chemistry
Drug resistance
Embryo fibroblasts
Fibroblasts - metabolism
Gene Deletion
Genetic aspects
Glucose
Glucose - metabolism
Glucose Transporter Type 1 - metabolism
Human Genetics
Hypersensitivity
Internal Medicine
Mechanistic Target of Rapamycin Complex 1
Medicine
Medicine & Public Health
Mice
Multiprotein Complexes - metabolism
Neoplastic processes
Oncology
Oncology, Experimental
original-article
Properties
Protein transport
Proteins
Rapamycin
ras Proteins - metabolism
Signal Transduction
Stress, Physiological
TOR protein
TOR Serine-Threonine Kinases - metabolism
Tuberous sclerosis
Tuberous Sclerosis Complex 2
Tumor Suppressor Proteins - genetics
Tumor Suppressor Proteins - metabolism
Title Loss of TSC2 confers resistance to ceramide and nutrient deprivation
URI https://link.springer.com/article/10.1038/onc.2013.139
https://www.ncbi.nlm.nih.gov/pubmed/23604129
https://www.proquest.com/docview/1512342302
https://www.proquest.com/docview/2641525461
https://search.proquest.com/docview/1516757007
https://pubmed.ncbi.nlm.nih.gov/PMC3858574
Volume 33
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