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1.
Proc Natl Acad Sci U S A ; 114(17): E3434-E3443, 2017 04 25.
Article in English | MEDLINE | ID: mdl-28396387

ABSTRACT

Oncogenic PIK3CA mutations are found in a significant fraction of human cancers, but therapeutic inhibition of PI3K has only shown limited success in clinical trials. To understand how mutant PIK3CA contributes to cancer cell proliferation, we used genome scale loss-of-function screening in a large number of genomically annotated cancer cell lines. As expected, we found that PIK3CA mutant cancer cells require PIK3CA but also require the expression of the TCA cycle enzyme 2-oxoglutarate dehydrogenase (OGDH). To understand the relationship between oncogenic PIK3CA and OGDH function, we interrogated metabolic requirements and found an increased reliance on glucose metabolism to sustain PIK3CA mutant cell proliferation. Functional metabolic studies revealed that OGDH suppression increased levels of the metabolite 2-oxoglutarate (2OG). We found that this increase in 2OG levels, either by OGDH suppression or exogenous 2OG treatment, resulted in aspartate depletion that was specifically manifested as auxotrophy within PIK3CA mutant cells. Reduced levels of aspartate deregulated the malate-aspartate shuttle, which is important for cytoplasmic NAD+ regeneration that sustains rapid glucose breakdown through glycolysis. Consequently, because PIK3CA mutant cells exhibit a profound reliance on glucose metabolism, malate-aspartate shuttle deregulation leads to a specific proliferative block due to the inability to maintain NAD+/NADH homeostasis. Together these observations define a precise metabolic vulnerability imposed by a recurrently mutated oncogene.


Subject(s)
Class I Phosphatidylinositol 3-Kinases , Ketoglutarate Dehydrogenase Complex , Mutation , Neoplasm Proteins , Neoplasms , Animals , Cell Line, Tumor , Citric Acid Cycle/genetics , Class I Phosphatidylinositol 3-Kinases/genetics , Class I Phosphatidylinositol 3-Kinases/metabolism , Glycolysis/genetics , Humans , Ketoglutarate Dehydrogenase Complex/biosynthesis , Ketoglutarate Dehydrogenase Complex/genetics , Mice , Mice, Nude , Neoplasm Proteins/genetics , Neoplasm Proteins/metabolism , Neoplasms/enzymology , Neoplasms/genetics , Neoplasms/pathology
2.
Cancer Discov ; 3(9): 1044-57, 2013 Sep.
Article in English | MEDLINE | ID: mdl-23764425

ABSTRACT

UNLABELLED: 3q26 is frequently amplified in several cancer types with a common amplified region containing 20 genes. To identify cancer driver genes in this region, we interrogated the function of each of these genes by loss- and gain-of-function genetic screens. Specifically, we found that TLOC1 (SEC62) was selectively required for the proliferation of cell lines with 3q26 amplification. Increased TLOC1 expression induced anchorage-independent growth, and a second 3q26 gene, SKIL (SNON), facilitated cell invasion in immortalized human mammary epithelial cells. Expression of both TLOC1 and SKIL induced subcutaneous tumor growth. Proteomic studies showed that TLOC1 binds to DDX3X, which is essential for TLOC1-induced transformation and affected protein translation. SKIL induced invasion through upregulation of SLUG (SNAI2) expression. Together, these studies identify TLOC1 and SKIL as driver genes at 3q26 and more broadly suggest that cooperating genes may be coamplified in other regions with somatic copy number gain. SIGNIFICANCE: These studies identify TLOC1 and SKIL as driver genes in 3q26. These observations provide evidence that regions of somatic copy number gain may harbor cooperating genes of different but complementary functions.


Subject(s)
Chromosomes, Human, Pair 3/genetics , Intracellular Signaling Peptides and Proteins/genetics , Membrane Transport Proteins/genetics , Neoplasm Invasiveness/genetics , Neoplasms/genetics , Proto-Oncogene Proteins/genetics , Breast Neoplasms/genetics , Carcinoma, Non-Small-Cell Lung/genetics , Cell Line, Tumor , Cell Proliferation , DEAD-box RNA Helicases/metabolism , DNA Copy Number Variations/genetics , Epithelial-Mesenchymal Transition/genetics , Female , Gene Amplification/genetics , Gene Expression Regulation, Neoplastic , Humans , Intracellular Signaling Peptides and Proteins/metabolism , Lung Neoplasms/genetics , Mammary Glands, Human/cytology , Membrane Transport Proteins/metabolism , Ovarian Neoplasms/genetics , Protein Binding , Proto-Oncogene Proteins/metabolism , RNA Interference , RNA, Small Interfering , Snail Family Transcription Factors , Transcription Factors/biosynthesis
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