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Volumn 99, Issue 1, 2014, Pages

Role of amino acid transporters in amino acid sensing

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID TRANSPORTER; LEUCINE; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; MEMBRANE PROTEIN; SOLUTE CARRIER 7A5; UNCLASSIFIED DRUG;

EID: 84891377474     PISSN: 00029165     EISSN: 19383207     Source Type: Journal    
DOI: 10.3945/ajcn.113.070086     Document Type: Article
Times cited : (187)

References (72)
  • 1
    • 38349170961 scopus 로고    scopus 로고
    • Amino acid transport across mammalian intestinal and renal epithelia
    • Bröer S. Amino acid transport across mammalian intestinal and renal epithelia. Physiol Rev 2008;88:249-86.
    • (2008) Physiol Rev , vol.88 , pp. 249-286
    • Bröer, S.1
  • 2
    • 23044474905 scopus 로고    scopus 로고
    • Amino acid transporters ASCT2 and LAT1 in cancer: Partners in crime?
    • Fuchs BC, Bode BP. Amino acid transporters ASCT2 and LAT1 in cancer: partners in crime? Semin Cancer Biol 2005;15:254-66.
    • (2005) Semin Cancer Biol , vol.15 , pp. 254-266
    • Fuchs, B.C.1    Bode, B.P.2
  • 6
    • 0035795114 scopus 로고    scopus 로고
    • Homologues of archaeal rhodopsins in plants, animals and fungi: Structural and functional predications for a putative fungal chaperone protein
    • Zhai Y, Heijne WHM, Smith DW, Saier MH Jr. Homologues of archaeal rhodopsins in plants, animals and fungi: structural and functional predications for a putative fungal chaperone protein. Biochim Biophys Acta Biomembr 2001;1511:206-23.
    • (2001) Biochim Biophys Acta Biomembr , vol.1511 , pp. 206-223
    • Zhai, Y.1    Heijne, W.H.M.2    Smith, D.W.3    Saier Jr., M.H.4
  • 7
    • 79956041076 scopus 로고    scopus 로고
    • The role of amino acid transporters in inherited and acquired diseases
    • Bröer S, Palacin M. The role of amino acid transporters in inherited and acquired diseases. Biochem J 2011;436:193-211.
    • (2011) Biochem J , vol.436 , pp. 193-211
    • Bröer, S.1    Palacin, M.2
  • 8
    • 0035503565 scopus 로고    scopus 로고
    • Cystinosin, the protein defective in cystinosis, is a H+-driven lysosomal cystine transporter
    • Kalatzis V, Cherqui S, Antignac C, Gasnier B. Cystinosin, the protein defective in cystinosis, is a H+-driven lysosomal cystine transporter. EMBO J 2001;20:5940-9.
    • (2001) EMBO J , vol.20 , pp. 5940-5949
    • Kalatzis, V.1    Cherqui, S.2    Antignac, C.3    Gasnier, B.4
  • 9
    • 0025095302 scopus 로고
    • Role of amino acid transport and countertransport in nutrition and metabolism
    • Christensen HN. Role of amino acid transport and countertransport in nutrition and metabolism. Physiol Rev 1990;70:43-77.
    • (1990) Physiol Rev , vol.70 , pp. 43-77
    • Christensen, H.N.1
  • 10
    • 65649152957 scopus 로고    scopus 로고
    • Amino acid transceptors: Gate keepers of nutrient exchange and regulators of nutrient signaling
    • Hundal HS, Taylor PM. Amino acid transceptors: gate keepers of nutrient exchange and regulators of nutrient signaling. Am J Physiol Endocrinol Metab 2009;296:E603-13.
    • (2009) Am J Physiol Endocrinol Metab , vol.296
    • Hundal, H.S.1    Taylor, P.M.2
  • 12
    • 84894486696 scopus 로고    scopus 로고
    • Nutrient regulation of the mTOR complex 1 signaling pathway
    • Kim SG, Buel G, Blenis J. Nutrient regulation of the mTOR complex 1 signaling pathway. Mol Cell 2013;35:463-73.
    • (2013) Mol Cell , vol.35 , pp. 463-473
    • Kim, S.G.1    Buel, G.2    Blenis, J.3
  • 13
    • 60149091189 scopus 로고    scopus 로고
    • Regulation of translation initiation in eukaryotes: Mechanisms and biological targets
    • Sonenberg N, Hinnebusch AG. Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell 2009;136:731-45.
    • (2009) Cell , vol.136 , pp. 731-745
    • Sonenberg, N.1    Hinnebusch, A.G.2
  • 14
    • 84870885054 scopus 로고    scopus 로고
    • Amino acid sensing in dietaryrestriction-mediated longevity: Roles of signal-transducing kinases GCN2 and TOR
    • Gallinetti J, Harputlugil E, Mitchell JR. Amino acid sensing in dietaryrestriction-mediated longevity: roles of signal-transducing kinases GCN2 and TOR. Biochem J 2013;449:1-10.
    • (2013) Biochem J , vol.449 , pp. 1-10
    • Gallinetti, J.1    Harputlugil, E.2    Mitchell, J.R.3
  • 15
  • 16
    • 80555143078 scopus 로고    scopus 로고
    • MTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H(+)-ATPase
    • Zoncu R, Bar-Peled L, Efeyan A, Wang S, Sancak Y, Sabatini DM. mTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H(+)-ATPase. Science 2011;334:678-83.
    • (2011) Science , vol.334 , pp. 678-683
    • Zoncu, R.1    Bar-Peled, L.2    Efeyan, A.3    Wang, S.4    Sancak, Y.5    Sabatini, D.M.6
  • 19
    • 80054682244 scopus 로고    scopus 로고
    • From transporter to transceptor: Signaling from transporters provokes re-evaluation of complex trafficking and regulatory controls
    • Kriel J, Haesendonckx S, Rubio-Texeira M, Van Zeebroeck G, Thevelein JM. From transporter to transceptor: signaling from transporters provokes re-evaluation of complex trafficking and regulatory controls. Bioessays 2011;33:870-9.
    • (2011) Bioessays , vol.33 , pp. 870-879
    • Kriel, J.1    Haesendonckx, S.2    Rubio-Texeira, M.3    Van Zeebroeck, G.4    Thevelein, J.M.5
  • 20
    • 84876514626 scopus 로고    scopus 로고
    • Control of amino-acid transport by antigen receptors coordinates the metabolic reprogramming essential for T cell differentiation
    • Sinclair LV, Rolf J, Emslie E, Shi Y-B, Taylor PM, Cantrell DA. Control of amino-acid transport by antigen receptors coordinates the metabolic reprogramming essential for T cell differentiation. Nat Immunol 2013;14:500-8.
    • (2013) Nat Immunol , vol.14 , pp. 500-508
    • Sinclair, L.V.1    Rolf, J.2    Emslie, E.3    Shi, Y.-B.4    Taylor, P.M.5    Cantrell, D.A.6
  • 21
    • 84864348386 scopus 로고    scopus 로고
    • Exercise and amino acid anabolic cell signaling and the regulation of skeletal muscle mass
    • Pasiakos SM. Exercise and amino acid anabolic cell signaling and the regulation of skeletal muscle mass. Nutrients 2012;4(7):740-58.
    • (2012) Nutrients , vol.4 , Issue.7 , pp. 740-758
    • Pasiakos, S.M.1
  • 22
    • 84862908818 scopus 로고    scopus 로고
    • AMPK and mTOR in cellular energy homeostasis and drug targets
    • Inoki K, Kim J, Guan K-L. AMPK and mTOR in cellular energy homeostasis and drug targets. Annu Rev Pharmacol Toxicol 2012;52: 381-400.
    • (2012) Annu Rev Pharmacol Toxicol , vol.52 , pp. 381-400
    • Inoki, K.1    Kim, J.2    Guan, K.-L.3
  • 23
    • 84865592978 scopus 로고    scopus 로고
    • Amino acids and mTORC1: From lysosomes to disease
    • Efeyan A, Zoncu R, Sabatini DM. Amino acids and mTORC1: from lysosomes to disease. Trends Mol Med 2012;18:524-33.
    • (2012) Trends Mol Med , vol.18 , pp. 524-533
    • Efeyan, A.1    Zoncu, R.2    Sabatini, D.M.3
  • 24
    • 77956556496 scopus 로고    scopus 로고
    • Control of translation initiation through integration of signals generated by hormones, nutrients, and exercise
    • Kimball SR, Jefferson LS. Control of translation initiation through integration of signals generated by hormones, nutrients, and exercise. J Biol Chem 2010;285:29027-32.
    • (2010) J Biol Chem , vol.285 , pp. 29027-29032
    • Kimball, S.R.1    Jefferson, L.S.2
  • 26
    • 84863045210 scopus 로고    scopus 로고
    • Roles of the mammalian target of rapamycin, mTOR, in controlling ribosome biogenesis and protein synthesis
    • Iadevaia V, Huo Y, Zhang Z, Foster LJ, Proud CG. Roles of the mammalian target of rapamycin, mTOR, in controlling ribosome biogenesis and protein synthesis. Biochem Soc Trans 2012;40:168-72.
    • (2012) Biochem Soc Trans , vol.40 , pp. 168-172
    • Iadevaia, V.1    Huo, Y.2    Zhang, Z.3    Foster, L.J.4    Proud, C.G.5
  • 27
    • 84856453804 scopus 로고    scopus 로고
    • Regulation of TOR by small GTPases
    • Durán RV, Hall MN. Regulation of TOR by small GTPases. EMBO Rep 2012;13:121-8.
    • (2012) EMBO Rep , vol.13 , pp. 121-128
    • Durán, R.V.1    Hall, M.N.2
  • 28
    • 77951768486 scopus 로고    scopus 로고
    • Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids
    • Sancak Y, Bar-Peled L, Zoncu R, Markhard AL, Nada S, Sabatini DM. Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids. Cell 2010;141:290-303.
    • (2010) Cell , vol.141 , pp. 290-303
    • Sancak, Y.1    Bar-Peled, L.2    Zoncu, R.3    Markhard, A.L.4    Nada, S.5    Sabatini, D.M.6
  • 29
    • 84866431363 scopus 로고    scopus 로고
    • Ragulator is a GEF for the Rag GTPases that signal amino acid levels to mTORC1
    • Bar-Peled L, Schweitzer Lawrence D, Zoncu R, Sabatini David M. Ragulator is a GEF for the Rag GTPases that signal amino acid levels to mTORC1. Cell 2012;150:1196-208.
    • (2012) Cell , vol.150 , pp. 1196-1208
    • Bar-Peled, L.1    Schweitzer Lawrence, D.2    Zoncu, R.3    Sabatini David, M.4
  • 32
    • 84872687720 scopus 로고    scopus 로고
    • Glutamine stimulates mTORC1 independent of the cell content of essential amino acids
    • Chiu M, Tardito S, Barilli A, Bianchi M, Dall'Asta V, Bussolati O. Glutamine stimulates mTORC1 independent of the cell content of essential amino acids. Amino Acids 2012;43:2561-7.
    • (2012) Amino Acids , vol.43 , pp. 2561-2567
    • Chiu, M.1    Tardito, S.2    Barilli, A.3    Bianchi, M.4    Dall'asta, V.5    Bussolati, O.6
  • 35
    • 32544452111 scopus 로고    scopus 로고
    • System B0,+ amino acid transport regulates the penetration stage of blastocyst implantation with possible long-term developmental consequences through adulthood
    • Van Winkle LJ, Tesch JK, Shah A, Campione AL. System B0,+ amino acid transport regulates the penetration stage of blastocyst implantation with possible long-term developmental consequences through adulthood. Hum Reprod Update 2006;12:145-57.
    • (2006) Hum Reprod Update , vol.12 , pp. 145-157
    • Van Winkle, L.J.1    Tesch, J.K.2    Shah, A.3    Campione, A.L.4
  • 36
    • 0038050529 scopus 로고    scopus 로고
    • Interorgan amino acid transport and its regulation
    • Brosnan JT. Interorgan amino acid transport and its regulation. J Nutr 2003;133(suppl 1):2068S-72S.
    • (2003) J Nutr , vol.133 , Issue.SUPPL. 1
    • Brosnan, J.T.1
  • 37
    • 69049097269 scopus 로고    scopus 로고
    • Tertiary active transport of amino acids reconstituted by coexpression of system A and L transporters in Xenopus oocytes
    • Baird FE, Bett KJ, Maclean C, Tee AR, Hundal HS, Taylor PM. Tertiary active transport of amino acids reconstituted by coexpression of system A and L transporters in Xenopus oocytes. Am J Physiol Endocrinol Metab 2009;297:E822-9.
    • (2009) Am J Physiol Endocrinol Metab , vol.297
    • Baird, F.E.1    Bett, K.J.2    MacLean, C.3    Tee, A.R.4    Hundal, H.S.5    Taylor, P.M.6
  • 39
    • 84876782429 scopus 로고    scopus 로고
    • Cellular signaling of amino acids towards mTORC1 activation in impaired human leucine catabolism
    • Schriever SC, Deutsch MJ, Adamski J, Roscher AA, Ensenauer R. Cellular signaling of amino acids towards mTORC1 activation in impaired human leucine catabolism. J Nutr Biochem 2013;24:824-31.
    • (2013) J Nutr Biochem , vol.24 , pp. 824-831
    • Schriever, S.C.1    Deutsch, M.J.2    Adamski, J.3    Roscher, A.A.4    Ensenauer, R.5
  • 40
    • 33846444928 scopus 로고    scopus 로고
    • The cationic amino acid transporters CAT1 and CAT3 mediate NMDA receptor activation-dependent changes in elaboration of neuronal processes via the mammalian target of rapamycin mTOR pathway
    • Huang Y, Kang BN, Tian J, Liu Y, Luo HR, Hester L, Snyder SH. The cationic amino acid transporters CAT1 and CAT3 mediate NMDA receptor activation-dependent changes in elaboration of neuronal processes via the mammalian target of rapamycin mTOR pathway. J Neurosci 2007; 27:449-58.
    • (2007) J Neurosci , vol.27 , pp. 449-458
    • Huang, Y.1    Kang, B.N.2    Tian, J.3    Liu, Y.4    Luo, H.R.5    Hester, L.6    Snyder, S.H.7
  • 42
    • 84875161720 scopus 로고    scopus 로고
    • Evolutionary origin of amino acid transporter families SLC32, SLC36 and SLC38 and physiological, pathological and therapeutic aspects
    • Schiöth HB, Roshanbin S, Hägglund MGA, Fredriksson R. Evolutionary origin of amino acid transporter families SLC32, SLC36 and SLC38 and physiological, pathological and therapeutic aspects. Mol Aspects Med 2013;34:571-85.
    • (2013) Mol Aspects Med , vol.34 , pp. 571-585
    • Schiöth, H.B.1    Roshanbin, S.2    Hägglund, M.G.A.3    Fredriksson, R.4
  • 43
    • 77954757143 scopus 로고    scopus 로고
    • Proton-assisted amino-acid transporters are conserved regulators of proliferation and amino-acid-dependent mTORC1 activation
    • Heublein S, Kazi S, Ogmundsdottir MH, Attwood EV, Kala S, Boyd CA, Wilson C, Goberdhan DC. Proton-assisted amino-acid transporters are conserved regulators of proliferation and amino-acid-dependent mTORC1 activation. Oncogene 2010;29:4068-79.
    • (2010) Oncogene , vol.29 , pp. 4068-4079
    • Heublein, S.1    Kazi, S.2    Ogmundsdottir, M.H.3    Attwood, E.V.4    Kala, S.5    Boyd, C.A.6    Wilson, C.7    Goberdhan, D.C.8
  • 46
    • 0025746712 scopus 로고
    • The transport systems of mammalian lysosomes
    • Pisoni RL, Thoene JG. The transport systems of mammalian lysosomes. Biochim Biophys Acta 1991;1071:351-73.
    • (1991) Biochim Biophys Acta , vol.1071 , pp. 351-373
    • Pisoni, R.L.1    Thoene, J.G.2
  • 47
    • 0025300663 scopus 로고
    • Characterization of lysosomal monoiodotyrosine transport in rat thyroid cells: Evidence for transport by system h
    • Andersson HC, Kohn LD, Bernardini I, Blom HJ, Tietze F, Gahl WA. Characterization of lysosomal monoiodotyrosine transport in rat thyroid cells: evidence for transport by system h. J Biol Chem 1990;265: 10950-4.
    • (1990) J Biol Chem , vol.265 , pp. 10950-10954
    • Andersson, H.C.1    Kohn, L.D.2    Bernardini, I.3    Blom, H.J.4    Tietze, F.5    Gahl, W.A.6
  • 50
    • 33646228377 scopus 로고    scopus 로고
    • Characterization of the amino acid response element within the human sodiumcoupled neutral amino acid transporter 2 (SNAT2) system A transporter gene
    • Palii SS, Thiaville MM, Pan Y-X, Zhong C, Kilberg MS. Characterization of the amino acid response element within the human sodiumcoupled neutral amino acid transporter 2 (SNAT2) system A transporter gene. Biochem J 2006;395:517-27.
    • (2006) Biochem J , vol.395 , pp. 517-527
    • Palii, S.S.1    Thiaville, M.M.2    Pan, Y.-X.3    Zhong, C.4    Kilberg, M.S.5
  • 51
    • 33745838924 scopus 로고    scopus 로고
    • Amino acid starvation induces the SNAT2 neutral amino acid transporter by a mechanism that involves eukaryotic initiation factor 2alpha phosphorylation and CAP-independent translation
    • Gaccioli F, Huang CC, Wang C, Bevilacqua E, Franchi-Gazzola R, Gazzola GC, Bussolati O, Snider MD, Hatzoglou M. Amino acid starvation induces the SNAT2 neutral amino acid transporter by a mechanism that involves eukaryotic initiation factor 2alpha phosphorylation and CAP-independent translation. J Biol Chem 2006;281:17929-40.
    • (2006) J Biol Chem , vol.281 , pp. 17929-17940
    • Gaccioli, F.1    Huang, C.C.2    Wang, C.3    Bevilacqua, E.4    Franchi-Gazzola, R.5    Gazzola, G.C.6    Bussolati, O.7    Snider, M.D.8    Hatzoglou, M.9
  • 52
    • 34547124353 scopus 로고    scopus 로고
    • Distinct sensor pathways in the hierarchical control of SNAT2, a putative amino acid transceptor, by amino acid availability
    • Hyde R, Cwiklinski EL, Macaulay K, Taylor PM, Hundal HS. Distinct sensor pathways in the hierarchical control of SNAT2, a putative amino acid transceptor, by amino acid availability. J Biol Chem 2007;282: 19788-98.
    • (2007) J Biol Chem , vol.282 , pp. 19788-19798
    • Hyde, R.1    Cwiklinski, E.L.2    MacAulay, K.3    Taylor, P.M.4    Hundal, H.S.5
  • 53
    • 84868155380 scopus 로고    scopus 로고
    • The brain's response to an essential amino aciddeficient diet and the circuitous route to a better meal
    • Gietzen DW, Aja SM. The brain's response to an essential amino aciddeficient diet and the circuitous route to a better meal. Mol Neurobiol 2012;46:332-48.
    • (2012) Mol Neurobiol , vol.46 , pp. 332-348
    • Gietzen, D.W.1    Aja, S.M.2
  • 54
    • 84863997137 scopus 로고    scopus 로고
    • LAAT-1 is the lysosomal lysine/arginine transporter that maintains amino acid homeostasis
    • Liu B, Du H, Rutkowski R, Gartner A, Wang X. LAAT-1 is the lysosomal lysine/arginine transporter that maintains amino acid homeostasis. Science 2012;337:351-4.
    • (2012) Science , vol.337 , pp. 351-354
    • Liu, B.1    Du, H.2    Rutkowski, R.3    Gartner, A.4    Wang, X.5
  • 58
    • 83255164815 scopus 로고    scopus 로고
    • The competitive advantage of a dual-transporter system
    • Levy S, Kafri M, Carmi M, Barkai N. The competitive advantage of a dual-transporter system. Science 2011;334:1408-12.
    • (2011) Science , vol.334 , pp. 1408-1412
    • Levy, S.1    Kafri, M.2    Carmi, M.3    Barkai, N.4
  • 59
    • 84355166527 scopus 로고    scopus 로고
    • Leucine and arginine regulate trophoblast motility through mTOR-dependent and independent pathways in the preimplantation mouse embryo
    • González IM, Martin PM, Burdsal C, Sloan JL, Mager S, Harris T, Sutherland AE. Leucine and arginine regulate trophoblast motility through mTOR-dependent and independent pathways in the preimplantation mouse embryo. Dev Biol 2012;361:286-300.
    • (2012) Dev Biol , vol.361 , pp. 286-300
    • González, I.M.1    Martin, P.M.2    Burdsal, C.3    Sloan, J.L.4    Mager, S.5    Harris, T.6    Sutherland, A.E.7
  • 60
  • 61
    • 34347211057 scopus 로고    scopus 로고
    • Mammalian target of rapamycin in the human placenta regulates leucine transport and is down-regulated in restricted fetal growth
    • Roos S, Jansson N, Palmberg I, Säljö K, Powell TL, Jansson T. Mammalian target of rapamycin in the human placenta regulates leucine transport and is down-regulated in restricted fetal growth. J Physiol 2007;582:449-59.
    • (2007) J Physiol , vol.582 , pp. 449-459
    • Roos, S.1    Jansson, N.2    Palmberg, I.3    Säljö, K.4    Powell, T.L.5    Jansson, T.6
  • 62
    • 84862757927 scopus 로고    scopus 로고
    • Insulin resistance and the metabolism of branched-chain amino acids in humans
    • Adeva MM, Calvino J, Souto G, Donapetry C. Insulin resistance and the metabolism of branched-chain amino acids in humans. Amino Acids 2012;43:171-81.
    • (2012) Amino Acids , vol.43 , pp. 171-181
    • Adeva, M.M.1    Calvino, J.2    Souto, G.3    Donapetry, C.4
  • 65
    • 84872369332 scopus 로고    scopus 로고
    • The mTORC1 signaling repressors REDD1/2 are rapidly induced and activation of p70S6K1 by leucine is defective in skeletal muscle of an immobilized rat hindlimb
    • Kelleher AR, Kimball SR, Dennis MD, Schilder RJ, Jefferson LS. The mTORC1 signaling repressors REDD1/2 are rapidly induced and activation of p70S6K1 by leucine is defective in skeletal muscle of an immobilized rat hindlimb. Am J Physiol Endocrinol Metab 2013;304:E229-36.
    • (2013) Am J Physiol Endocrinol Metab , vol.304
    • Kelleher, A.R.1    Kimball, S.R.2    Dennis, M.D.3    Schilder, R.J.4    Jefferson, L.S.5
  • 66
    • 64249113497 scopus 로고    scopus 로고
    • Dietary guidelines should reflect new understandings about adult protein needs
    • Layman DK. Dietary guidelines should reflect new understandings about adult protein needs. Nutr Metab 2009;6:12.
    • (2009) Nutr Metab , vol.6 , pp. 12
    • Layman, D.K.1
  • 69
    • 25444457577 scopus 로고    scopus 로고
    • HVps34 is a nutrient-regulated lipid kinase required for activation of p70 S6 kinase
    • Byfield MP, Murray JT, Backer JM. hVps34 is a nutrient-regulated lipid kinase required for activation of p70 S6 kinase. J Biol Chem 2005;280:33076-82.
    • (2005) J Biol Chem , vol.280 , pp. 33076-33082
    • Byfield, M.P.1    Murray, J.T.2    Backer, J.M.3
  • 71
    • 58049216316 scopus 로고    scopus 로고
    • RalA functions as an indispensable signal mediator for the nutrientsensing system
    • Maehama T, Tanaka M, Nishina H, Murakami M, Kanaho Y, Hanada K. RalA functions as an indispensable signal mediator for the nutrientsensing system. J Biol Chem 2008;283:35053-9.
    • (2008) J Biol Chem , vol.283 , pp. 35053-35059
    • Maehama, T.1    Tanaka, M.2    Nishina, H.3    Murakami, M.4    Kanaho, Y.5    Hanada, K.6
  • 72
    • 77954671228 scopus 로고    scopus 로고
    • Role of N-end rule ubiquitin ligases UBR1 and UBR2 in regulating the leucine-mTOR signaling pathway
    • Kume K, Iizumi Y, Shimada M, Ito Y, Kishi T, Yamaguchi Y, Handa H. Role of N-end rule ubiquitin ligases UBR1 and UBR2 in regulating the leucine-mTOR signaling pathway. Genes Cells 2010;15:339-49.
    • (2010) Genes Cells , vol.15 , pp. 339-349
    • Kume, K.1    Iizumi, Y.2    Shimada, M.3    Ito, Y.4    Kishi, T.5    Yamaguchi, Y.6    Handa, H.7


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