본문 바로가기
KERD
논문KCI 등재

Nutrient sensors and their crosstalk

Han Jung Min|Sung Yulseung|Yu Ya Chun
생화학분자생물학회 (Korean Society Of Biochemistry And Molecular Biology)|2023.12|Experimental and Molecular Medicine|제55권 |pp. 1076-1089|DOI 10.1038/s12276-023-01006-z

1

조회

0

다운로드

0

인용

0

참고문헌

주제분류생화학

초록

The macronutrients glucose, lipids, and amino acids are the major components that maintain life. The ability of cells to sense and respond to fluctuations in these nutrients is a crucial feature for survival. Nutrient-sensing pathways are thus developed to govern cellular energy and metabolic homeostasis and regulate diverse biological processes. Accordingly, perturbations in these sensing pathways are associated with a wide variety of pathologies, especially metabolic diseases. Molecular sensors are the core within these sensing pathways and have a certain degree of specificity and affinity to sense the intracellular fluctuation of each nutrient either by directly binding to that nutrient or indirectly binding to its surrogate molecules. Once the changes in nutrient levels are detected, sensors trigger signaling cascades to fine-tune cellular processes for energy and metabolic homeostasis, for example, by controlling uptake, de novo synthesis or catabolism of that nutrient. In this review, we summarize the major discoveries on nutrient-sensing pathways and explain how those sensors associated with each pathway respond to intracellular nutrient availability and how these mechanisms control metabolic processes. Later, we further discuss the crosstalk between these sensing pathways for each nutrient, which are intertwined to regulate overall intracellular nutrient/metabolic homeostasis.

Abstract

The macronutrients glucose, lipids, and amino acids are the major components that maintain life. The ability of cells to sense and respond to fluctuations in these nutrients is a crucial feature for survival. Nutrient-sensing pathways are thus developed to govern cellular energy and metabolic homeostasis and regulate diverse biological processes. Accordingly, perturbations in these sensing pathways are associated with a wide variety of pathologies, especially metabolic diseases. Molecular sensors are the core within these sensing pathways and have a certain degree of specificity and affinity to sense the intracellular fluctuation of each nutrient either by directly binding to that nutrient or indirectly binding to its surrogate molecules. Once the changes in nutrient levels are detected, sensors trigger signaling cascades to fine-tune cellular processes for energy and metabolic homeostasis, for example, by controlling uptake, de novo synthesis or catabolism of that nutrient. In this review, we summarize the major discoveries on nutrient-sensing pathways and explain how those sensors associated with each pathway respond to intracellular nutrient availability and how these mechanisms control metabolic processes. Later, we further discuss the crosstalk between these sensing pathways for each nutrient, which are intertwined to regulate overall intracellular nutrient/metabolic homeostasis.

참고문헌 (147)

  1. Efeyan, A., "Nutrient-sensing mechanisms and pathways", Nature, 517, pp.302~310 (2015)
  2. Hardie, D. G., "AMPK : a nutrient and energy sensor that maintains energy homeostasis", Nat. Rev. Mol. Cell Biol, 13, pp.251~262 (2012)
  3. Yuan, H. X., "Nutrient sensing, metabolism, and cell growth control", Mol. Cell, 49, pp.379~387 (2013)
  4. Witkowska Nery, E., "Electrochemical glucose sensing: is there still room for improvement?", Anal. Chem, 88, pp.11271~11282 (2016)
  5. Oliver, N. S., "Glucose sensors : a review of current and emerging technology", Diabet. Med, 26, pp.197~210 (2009)
  6. Rosario, W., "The brain–to–pancreatic Islet neuronal map reveals differential glucose regulation from distinct hypothalamic regions", Diabet, 65, pp.2711~2723 (2016)
  7. Han, J. M., "Leucyl-tRNA Synthetase Is an Intracellular Leucine Sensor for the mTORC1-Signaling Pathway", Cell, 149, pp.410~424 (2012)
  8. Sung Yulseung, "Functional and pathologic association of aminoacyl-tRNA synthetases with cancer", Experimental and Molecular Medicine, 54, pp.1~14 (2022), 생화학분자생물학회[DOI]
  9. Mulukutla, B. C., "Glucose metabolism in mammalian cell culture: new insights for tweaking vintage pathways", Trends Biotechnol, 28, pp.476~484 (2010)
  10. Metallo, C. M., "Reductive glutamine metabolism by IDH1 mediates lipogenesis under hypoxia", Nature, 481, pp.380~384 (2012)
  11. Yoo, H. C., "A variant of SLC1A5 is a mitochondrial glutamine transporter for metabolic reprogramming in cancer cells", Cell Metab, 31, pp.267~283 (2020)
  12. Bouché, C., "The cellular fate of glucose and its relevance in type 2 diabetes", Endocr. Rev, 25, pp.807~830 (2004)
  13. Schuit, F., "Metabolic fate of glucose in purified Islet cells : glucose-regulated anaplerosis in beta cells", J. Biol. Chem, 272, pp.18572~18579 (1997)
  14. Printz, R. L., "Mammalian glucokinase", Annu. Rev. Nutr, 13, pp.463~496 (1993)
  15. Nordlie, R. C., "Regulation of glucose production by the liver", Annu. Rev. Nutr, 19, pp.379~406 (1999)
  16. Sternisha, S. M., "Molecular and cellular regulation of human glucokinase", Arch. Biochem. Biophys, 663, pp.199~213 (2019)
  17. Rexford, A., "Biochemical and biophysical investigations of the interaction between human glucokinase and pro-apoptotic BAD", PLoS One, 12, pp.e0171587~ (2017)
  18. Murphy, R., "Glucokinase, the pancreatic glucose sensor, is not the gut glucose sensor", Diabetologia, 52, pp.154~159 (2009)
  19. Ogunnowo-Bada, E. O., "Brain glucose sensing, glucokinase and neural control of metabolism and islet function", Diabetes Obes. Metab, 16, pp.26~32 (2014)
  20. De Vos, A., "Human and rat beta cells differ in glucose transporter but not in glucokinase gene expression", J. Clin. Invest, 96, pp.2489~2495 (1995)
  21. Santer, R., "Mutations in GLUT2, the gene for the liver-type glucose transporter, in patients with Fanconi-Bickel syndrome", Nat. Genet, 17, pp.324~326 (1997)
  22. Zhang, C. -S., "Fructose-1, 6-bisphosphate and aldolase mediate glucose sensing by AMPK", Nature, 548, pp.112~116 (2017)
  23. Lin, S. -C., "AMPK : sensing glucose as well as cellular energy status", Cell Metab, 27, pp.299~313 (2018)
  24. Li, M., "Aldolase is a sensor for both low and high glucose, linking to AMPK and mTORC1", Cell Res, 31, pp.478~481 (2021)
  25. Li, M., "Transient receptor potential V channels are essential for glucose sensing by aldolase and AMPK", Cell Metab, 30, pp.508~524 (2019)
  26. Zhang, C. -S., "The lysosomal v-ATPase-ragulator complex is a common activator for AMPK and mTORC1, acting as a switch between catabolism and anabolism", Cell Metab, 20, pp.526~540 (2014)
  27. Yan, K., "Amelioration of type 1 diabetes by recombinant fructose-1, 6-bisphosphate aldolase and cystatin derived from Schistosoma japonicum in a murine model", Parasitol. Res, 119, pp.203~214 (2020)
  28. Ahn, B. Y., "Identification of an anti-aldolase autoantibody as a diagnostic marker for diabetic retinopathy by immunoproteomic analysis", Proteomics, 6, pp.1200~1209 (2006)
  29. Goberdhan, D. C., "Amino acid sensing by mTORC1 : intracellular transporters mark the spot", Cell Metab, 23, pp.580~589 (2016)
  30. Seibert, M., "Amino acid sensory complex proteins in mTORC1 and macroautophagy regulation", Matrix Biol, 100-101, pp.65~83 (2021)
  31. Kim, E., "Regulation of TORC1by Rag GTPases in nutrient response", Nat. Cell Biol, 10, pp.935~945 (2008)
  32. Sancak, Y., "The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1", Science, 320, pp.1496~1501 (2008)
  33. Potier, M., "Protein, amino acids and the control of food intake", Curr. Opin. Clin. Nutr. Metab. Care, 12, pp.54~58 (2009)
  34. Panten, U., "Studies on the mechanism of L-leucine-and alpha-ketoisocaproic acid-induced insulin release from perifused isolated pancreatic islets", Diabetologia, 10, pp.149~154 (1974)
  35. Greiwe, J. S., "Leucine and insulin activate p70 S6 kinase through different pathways in human skeletal muscle", Am. J. Physiol. Endocrinol. Metab, 281, pp.E466~E471 (2001)
  36. Efeyan, A., "Nutrients and growth factors in mTORC1 activation", Biochem Soc. Trans, 41, pp.902~905 (2013)
  37. Dibble, C. C., "Signal integration by mTORC1 coordinates nutrient input with biosynthetic output", Nat. Cell Biol, 15, pp.555~564 (2013)
  38. Conrad, M., "Nutrient sensing and signaling in the yeast Saccharomyces cerevisiae", FEMS Microbiol. Rev, 38, pp.254~299 (2014)
  39. Bonfils, G., "Leucyl-tRNA synthetase controls TORC1 via the EGO complex", Mol. Cell, 46, pp.105~110 (2012)
  40. Choi, H., "Leucine-induced localization of Leucyl-tRNA synthetase in lysosome membrane", Biochem. Biophys. Res. Commun, 493, pp.1129~1135 (2017)
  41. Kim, S., "Leucine-sensing mechanism of leucyl-tRNA synthetase 1 for mTORC1 activation", Cell Rep, 35, pp.109031~ (2021)
  42. Yoon, M. S., "Leucyl-tRNA synthetase activates Vps34 in amino acid-sensing mTORC1 signaling", Cell Rep, 16, pp.1510~1517 (2016)
  43. Wolfson, R. L., "Sestrin2 is a leucine sensor for the mTORC1 pathway", Science, 351, pp.43~48 (2016)
  44. Saxton, R. A., "Structural basis for leucine sensing by the Sestrin2-mTORC1pathway", Science, 351, pp.53~58 (2016)
  45. Bar-Peled, L., "A Tumor suppressor complex with GAP activity for the Rag GTPases that signal amino acid sufficiency to mTORC1", Science, 340, pp.1100~1106 (2013)
  46. Qu, J., "A paradoxical role for sestrin 2 protein in tumor suppression and tumorigenesis", Cancer Cell Int, 21, pp.606~ (2021)
  47. Zhao, Y., "Advances in the role of Leucine-sensing in the regulation of protein synthesis in aging skeletal muscle", Front. Cell Dev. Biol, 9, pp.646482~ (2021)
  48. Saxton, R. A., "The apo-structure of the leucine sensor Sestrin2 is still elusive", Sci. Signal, pp.ra92~ra92 (2016)
  49. Lee, M., "Coordination of the leucine-sensing Rag GTPase cycle by leucyltRNA synthetase in the mTORC1 signaling pathway", PNAS, 115, pp.E5279~E5288 (2018)
  50. Kim, J. H., "Control of leucine-dependent mTORC1 pathway through chemical intervention of leucyl-tRNA synthetase and RagD interaction", Nat. Comm, 8, pp.732~ (2017)
  51. Yu, Y. C., "Aminoacyl-tRNA synthetases and amino acid signaling", Biochim. Biophys. Acta Mol. Cell Res, 1868, pp.118889~ (2021)
  52. Kwon, N. H., "Aminoacyl-tRNA synthetases as therapeutic targets", Nat. Rev. Drug. Discov, 18, pp.629~650 (2019)
  53. Gu, X., "SAMTOR is an S-adenosylmethionine sensor for the mTORC1pathway", Science, 358, pp.813~818 (2017)
  54. Ouyang, Y., "S-adenosylmethionine : a metabolite critical to the regulation of autophagy", Cell Prolif, 53, pp.e12891~ (2020)
  55. Lauinger, L., "Sensing and signaling of methionine metabolism", Metabolites, 11, pp.83~ (2021)
  56. Peng, M., "SZT2 dictates GATOR control of mTORC1 signalling", Nature, 543, pp.433~437 (2017)
  57. Wolfson, R. L., "KICSTOR recruits GATOR1 to the lysosome and is necessary for nutrients to regulate mTORC1", Nature, 543, pp.438~442 (2017)
  58. Kitada, M., "Mechanism of activation of mechanistic target of rapamycin complex 1 by methionine", Front. Cell Dev. Biol, 8, pp.715~ (2020)
  59. Szefel, J., "Metabolic pathways of L-arginine and therapeutic consequences in tumors", Adv. Med. Sci, 64, pp.104~110 (2019)
  60. Saxton, R. A., "Mechanism of arginine sensing by CASTOR1 upstream of mTORC1", Nature, 536, pp.229~233 (2016)
  61. Chantranupong, L., "The CASTOR proteins are arginine sensors for the mTORC1 pathway", Cell, 165, pp.153~164 (2016)
  62. Gai, Z., "Structural mechanism for the arginine sensing and regulation of CASTOR1 in the mTORC1 signaling pathway", Cell Disco, 2, pp.16051~ (2016)
  63. Shen, K., "Ragulator and SLC38A9 activate the Rag GTPases through noncanonical GEF mechanisms", PNAS, 115, pp.9545~9550 (2018)
  64. Wyant, G. A., "mTORC1 activator SLC38A9 is required to efflux essential amino acids from lysosomes and use protein as a nutrient", Cell, 171, pp.642~654 (2017)
  65. Wang, S., "Metabolism. Lysosomal amino acid transporter SLC38A9 signals arginine sufficiency to mTORC1", Science, 347, pp.188~194 (2015)
  66. Jung, J. W., "Transmembrane 4 L six family member 5 senses arginine for mTORC1 signaling", Cell Metab, 29, pp.1306~1319 (2019)
  67. Tang, Q., "Physiological functions of threonine in animals : beyond nutrition metabolism", Nutrients, 13, pp.2592~ (2021)
  68. Ma, Q., "Threonine, but not lysine and methionine, reduces fat accumulation by regulating lipid metabolism in obese mice", J. Agric. Food Chem, 68, pp.4876~4883 (2020)
  69. Kim, S. H., "Mitochondrial threonyl-tRNA synthetase TARS2 is required for threonine-sensitive mTORC1 activation", Mol. Cell, 81, pp.398~407 (2021)
  70. 유희찬, "Glutamine reliance in cell metabolism", Experimental and Molecular Medicine, 52, pp.1~21 (2020), 생화학분자생물학회[DOI]
  71. Durán, R. V., "Glutaminolysis activates Rag-mTORC1 signaling", Mol. Cell, 47, pp.349~358 (2012)
  72. Jewell, J. L., "Differential regulation of mTORC1 by leucine and glutamine", Science, 347, pp.194~198 (2015)
  73. Meng, D., "Glutamine and asparagine activate mTORC1 independently of Rag GTPases", J. Biol. Chem, 295, pp.2890~2899 (2020)
  74. Bernfeld, E., "Phospholipase D–dependent mTOR complex 1(mTORC1)activation by glutamine", J. Biol. Chem, 293, pp.16390~16401 (2018)
  75. Kwon, N. H., "Stabilization of cyclin-dependent kinase 4 by methionyl-tRNA synthetase in p16INK4a-negative cancer", ACS Pharmacol. Transl. Sci, 1, pp.21~31 (2018)
  76. Wang, H., "C", EBPα triggers proteasome-dependent degradation of cdk4 during growth arrest, 2002, pp.21, 930~941
  77. Dorrell, R., "Endoscopic management of malignant biliary stricture", Diagnostics(Basel), 10, pp.390~ (2020)
  78. Jang, S. I., "Clinical utility of methionyl-tRNA synthetase 1 immunostaining in cytologic brushings of indeterminate biliary strictures: a multicenter prospective study", Gastrointest. Endosc, 94, pp.733~741 (2021)
  79. Kim, M. H., "The roles of glutamine in the intestine and its implication in intestinal diseases", Int. J. Mol. Sci, 18, pp.1051~ (2017)
  80. Chen, L., "Targeting glutamine induces apoptosis : a cancer therapy approach", Int. J. Mol. Sci, 16, pp.22830~22855 (2015)
  81. Yang, L., "Glutaminolysis : a hallmark of cancer metabolism", Annu Rev. Biomed. Eng, 19, pp.163~194 (2017)
  82. Ko, Y. -G., "Glutamine-dependent antiapoptotic interaction of human glutaminyl-tRNA synthetase with apoptosis signal-regulating kinase 1*", J. Biol. Chem, 276, pp.6030~6036 (2001)
  83. Woolf, L. I., "The early history of PKU", Int. J. Neonatal Screen, 6, pp.59~ (2020)
  84. Roberts, K. M., "Activation of phenylalanine hydroxylase by phenylalanine does not require binding in the active site", Biochemistry, 53, pp.7846~7853 (2014)
  85. Li, J, "Regulation of phenylalanine hydroxylase:conformational changes upon phenylalanine binding detected by hydrogen", deuterium exchange and mass spectrometry, 2010, pp.49, 3327~3335
  86. Li, J., "Direct evidence for a phenylalanine site in the regulatory domain of phenylalanine hydroxylase", Arch. Biochem. Biophys, 505, pp.250~255 (2011)
  87. Bjørgo, E., "A comparison of kinetic and regulatory properties of the tetrameric and dimeric forms of wild-type and Thr427–>pro mutant human phenylalanine hydroxylase : contribution of the flexible hinge region Asp425-Gln429 to the tetramerization and cooperative substrate binding", Eur. J. Biochem, 268, pp.997~1005 (2001)
  88. Stipanuk, M. H., "Mammalian cysteine metabolism: new insights into regulation of cysteine metabolism", J. Nutr, 136, pp.1652S~1659S (2006)
  89. Yuan, M., "CARS senses cysteine deprivation to activate AMPK for cell survival", EMBO J, 40, pp.e108028~ (2021)
  90. Raynor, J. L., "LCK senses asparagine for T cell activation", Nat. Cell Biol, 23, pp.7~8 (2021)
  91. Berthonneau, E., "A gene fusion event in the evolution of aminoacyl-tRNA synthetases", FEBS Let, 470, pp.300~304 (2000)
  92. Song, D. G., "Glutamyl-prolyl-tRNA synthetase induces fibrotic extracellular matrix via both transcriptional and translational mechanisms", FASEB J, 33, pp.4341~4354 (2019)
  93. Sajish, M., "Trp-tRNA synthetase bridges DNA-PKcs to PARP-1 to link IFN-γand p53 signaling", Nat. Chem. Biol, 8, pp.547~554 (2012)
  94. Rafice, S. A., "Oxidation of L-tryptophan in biology : a comparison between tryptophan 2, 3-dioxygenase and indoleamine 2, 3-dioxygenase", Biochem Soc. Trans, 37, pp.408~412 (2009)
  95. Klaessens, S., "Tryptophanemia is controlled by a tryptophan-sensing mechanism ubiquitinating tryptophan 2, 3-dioxygenase", Proc. Natl Acad. Sci. USA, 118, pp.e2022447118~ (2021)
  96. Brown, M. S., "Retrospective on cholesterol homeostasis : the central role of scap", Annu. Rev. Biochem, 87, pp.783~807 (2018)
  97. Sakai, J., "Identification of complexes between the COOH-terminal domains of sterol regulatory element-binding proteins(SREBPs)and SREBP cleavageactivating protein", J. Biol. Chem, 272, pp.20213~20221 (1997)
  98. Sakai, J., "Cleavage of sterol regulatory element-binding proteins (SREBPs) at site-1 requires interaction with SREBP cleavage-activating protein. Evidence from in vivo competition studies", J. Biol. Chem, 273, pp.5785~5793 (1998)
  99. Brown, A. J., "Cholesterol addition to ER membranes alters conformation of SCAP, the SREBP escort protein that regulates cholesterol metabolism", Mol. Cell, 10, pp.237~245 (2002)
  100. Radhakrishnan, A., "Direct binding of cholesterol to the purified membrane region of SCAP: mechanism for a sterol-sensing domain", Mol. Cell, 15, pp.259~268 (2004)
  101. Yang, T., "Crucial step in cholesterol homeostasis : sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER", Cell, 110, pp.489~500 (2002)
  102. Radhakrishnan, A., "Switch-like control of SREBP-2 transport triggered by small changes in ER cholesterol : a delicate balance", Cell Metab, 8, pp.512~521 (2008)
  103. Motamed, M., "Identification of luminal Loop 1 of Scap protein as the sterol sensor that maintains cholesterol homeostasis", J. Biol. Chem, 286, pp.18002~18012 (2011)
  104. Schumacher, M. M., "Posttranslational regulation of HMG CoA reductase, the rate-limiting enzyme in synthesis of cholesterol", Annu. Rev. Biochem, 90, pp.659~679 (2021)
  105. Sever, N., "Accelerated degradation of HMG CoA reductase mediated by binding of insig-1 to its sterolsensing domain", Mol. Cell, 11, pp.25~33 (2003)
  106. Song, B. L., "Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase", Mol. Cell, 19, pp.829~840 (2005)
  107. DeBose-Boyd, R. A., "Feedback regulation of cholesterol synthesis : sterolaccelerated ubiquitination and degradation of HMG CoA reductase", Cell Res, 18, pp.609~621 (2008)
  108. Glatz, J. C., "Dynamic role of the transmembrane glycoprotein CD36(SR-B2)in cellular fatty acid uptake and utilization", J. Lipid Res, 59, pp.1084~1093 (2018)
  109. Pepino, M. Y., "Structure-function of CD36 and importance of fatty acid signal transduction in fat metabolism", Annu. Rev. Nutr, 34, pp.281~303 (2014)
  110. Poulsen, Ll. C., "PPARs : Fatty acid sensors controlling metabolism", Semin. Cell Dev. Biol, 23, pp.631~639 (2012)
  111. Vacca, M., "Lipid-sensing nuclear receptors in the pathophysiology and treatment of the metabolic syndrome", Wiley Interdiscip. Rev. Syst. Biol. Med, 3, pp.562~587 (2011)
  112. Xu, H. E., "Molecular recognition of fatty acids by peroxisome proliferatoractivated receptors", Mol. Cell, 3, pp.397~403 (1999)
  113. Schupp, M., "Endogenous ligands for nuclear receptors : digging deeper", J. Biol. Chem, 285, pp.40409~40415 (2010)
  114. Lamas Bervejillo, M., "A FABP4-PPARγ signaling axis regulates human monocyte responses to electrophilic fatty acid nitroalkenes", Redox Biol, 29, pp.101376~ (2020)
  115. Monroy-Ramirez, H. C., "PPARs as metabolic sensors and therapeutic targets in liver diseases", Int. J. Mol. Sci, 22, pp.8298~ (2021)
  116. Saddik, M., "Acetyl-CoA carboxylase regulation of fatty acid oxidation in the heart", J. Biol. Chem, 268, pp.25836~25845 (1993)
  117. Luiken, J. J., "Etomoxir-induced partial carnitine palmitoyltransferase-I(CPT-I)inhibition in vivo does not alter cardiac long-chain fatty acid uptake and oxidation rates", Biochem J, 419, pp.447~455 (2009)
  118. Glatz, J. F., "Regulation of the subcellular trafficking of CD36, a major determinant of cardiac fatty acid utilization", Biochim Biophys. Acta, 1861, pp.1461~1471 (2016)
  119. McGarry, J. D., "A possible role for malonyl-CoA in the regulation of hepatic fatty acid oxidation and ketogenesis", J. Clin. Invest, 60, pp.265~270 (1977)
  120. Fadó, R., "The return of malonyl-CoA to the brain : cognition and other stories", Prog. Lipid Res, 81, pp.101071~ (2021)
  121. Yoon, I., "Glucose-dependent control of leucine metabolism by leucyl-tRNA synthetase 1", Science, 367, pp.205~210 (2020)
  122. Kim, K., "O-GlcNAc modification of leucyl-tRNA synthetase 1 integrates leucine and glucose availability to regulate mTORC1 and the metabolic fate of leucine", Nat. Comm, 13, pp.2904~ (2022)
  123. Bond, M. R., "A little sugar goes a long way : the cell biology of O-GlcNAc", J. Cell Biol, 208, pp.869~880 (2015)
  124. Taylor, R. P., "Glucose deprivation stimulates O-GlcNAc modification of proteins through up-regulation of O-linked N-acetylglucosaminyltransferase", J. Biol. Chem, 283, pp.6050~6057 (2008)
  125. Cheung, W. D., "AMP-activated protein kinase and p38 MAPK activate O-GlcNAcylation of neuronal proteins during glucose deprivation", J. Biol. Chem, 283, pp.13009~13020 (2008)
  126. Taylor, R. P., "Up-regulation of O-GlcNAc transferase with glucose deprivation in HepG2 cells is mediated by decreased hexosamine pathway flux", J. Biol. Chem, 284, pp.3425~3432 (2009)
  127. Kang, J. G., "O-GlcNAc protein modification in cancer cells increases in response to glucose deprivation through glycogen degradation", J. Biol. Chem, 284, pp.34777~34784 (2009)
  128. Kim, K.-H., "Current Topics in Cellular Regulation Vol. 22", pp.143~176 (1983), Academic Press
  129. López, M., "Hypothalamic fatty acid metabolism mediates the orexigenic action of ghrelin", Cell Metab, 7, pp.389~399 (2008)
  130. Zhuang, W., "CPT1 regulates the proliferation of pulmonary artery smooth muscle cells through the AMPK-p53-p21 pathway in pulmonary arterial hypertension", Mol. Cell. Biochem, 455, pp.169~183 (2019)
  131. Oda, H., "Functions of sulfur-containing amino acids in lipid metabolism", J. Nutr, 136, pp.1666S~1669S (2006)
  132. Currie, E., "Cellular fatty acid metabolism and cancer", Cell Metab, 18, pp.153~161 (2013)
  133. Wise, D. R., "Hypoxia promotes isocitrate dehydrogenase-dependent carboxylation of α-ketoglutarate to citrate to support cell growth and viability", PNAS, 108, pp.19611~19616 (2011)
  134. Mullen, A. R., "Reductive carboxylation supports growth in tumour cells with defective mitochondria", Nature, 481, pp.385~388 (2012)
  135. Halama, A., "Accelerated lipid catabolism and autophagy are cancer survival mechanisms under inhibited glutaminolysis", Cancer Lett, 430, pp.133~147 (2018)
  136. Reis, L. M. D., "Dual inhibition of glutaminase and carnitine palmitoyltransferase decreases growth and migration of glutaminase inhibition-resistant triple-negative breast cancer cells", J. Biol. Chem, 294, pp.9342~9357 (2019)
  137. Boone, A. N., "Bimodal activation of Acetyl-CoA carboxylase by glutamate*", J. Biol. Chem, 275, pp.10819~10825 (2000)
  138. Kowluru, A., "Activation of Acetyl-CoA carboxylase by a glutamate-and magnesium-sensitive protein phosphatase in the Islet β-cell", Diabet, 50, pp.1580~1587 (2001)
  139. Wang, Y., "Acetyl-CoA carboxylases and diseases", Front. Oncol, 12, pp.836058~ (2022)
  140. Liu, F., "Long non-coding RNA SNHG6 couples cholesterol sensing with mTORC1 activation in hepatocellular carcinoma", Nat. Metabol, 4, pp.1022~1040 (2022)
  141. Luo, J., "Mechanisms and regulation of cholesterol homeostasis", Nat. Rev. Mol. Cell Biol, 21, pp.225~245 (2020)
  142. Kim, H., "UAS domain of Ubxd8 and FAF1 polymerizes upon interaction with long-chain unsaturated fatty acids", J. Lipid Res, 54, pp.2144~2152 (2013)
  143. Ershov, P., "Enzymes in the cholesterol synthesis pathway : interactomics in the cancer context", Biomedicines, 9, pp.895~ (2021)
  144. Zhu, M., "Monomethyl branched-chain fatty acid mediates amino acid sensing upstream of mTORC1", Dev. Cell, 56, pp.2692~2702 (2021)
  145. Chitwood, D. J., "The glycosylceramides of the nematode Caenorhabditis elegans contain an unusual, branched-chain sphingoid base", Lipids, 30, pp.567~573 (1995)
  146. Zhu, H., "A novel sphingolipid-TORC1 pathway critically promotes postembryonic development in Caenorhabditis elegans", eLife, 2, pp.e00429~ (2013)
  147. Green, C. R., "Branched-chain amino acid catabolism fuels adipocyte differentiation and lipogenesis", Nat. Chem. Biol, 12, pp.15~21 (2016)

이 간행물의 다른 논문 (225건)

Endothelial senescence in vascular diseases: current understanding and future opportunities in senotherapeutics김성영, Han Yeaeunpp. 1-12Grave-to-cradle: human embryonic lineage tracing from the postmortem bodyKu Eu Jeong, Choi Seock Hwan, Choi Yujin Angelina, Oh Ji Wonpp. 13-21Chromatin and noncoding RNA-mediated mechanisms of gastric tumorigenesisKim Tae-Hee, Loe Adrian Kwan Ho, Zhu Lexinpp. 22-31TPX2 prompts mitotic survival via the induction of BCL2L1 through YAP1 protein stabilization in human embryonic stem cellsCha Hyuk-Jin, Kim Yun-Jeong, Go Young-Hyun, 정호창, Kwon Eun-Ji, Kim Seong-Min, Cheong Hyun Sub, Kim Wantae, Shin Hyoung Doo, Lee Haeseungpp. 32-42ZBTB7A suppresses glioblastoma tumorigenesis through the transcriptional repression of EPB41L5Nam Hae Yun, 김성학, 김승후, 최경철, Park Seung-Ho, Song Ji-Hye, Jeong Ji-Hoon, Kim Hyunhee, Jeong Minseok, Kong Min-Jeong, Son Jihyun, Jeong Ji-Eunpp. 43-54
원문 보기