메뉴 건너뛰기




Volumn 468, Issue 2, 2015, Pages 203-214

Akt/PKB: One kinase, many modifications

Author keywords

Akt; Post translational modification; Protein function; Protein kinase B; Signal transduction

Indexed keywords

CYSTEINE; DEUBIQUITINASE; LYSINE; PROTEIN KINASE B; SERINE; THREONINE; TYROSINE;

EID: 84934903117     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20150041     Document Type: Review
Times cited : (156)

References (96)
  • 1
    • 84907220717 scopus 로고    scopus 로고
    • Signalling specificity in the Akt pathway in breast cancer
    • CrossRef PubMed
    • Clark, A.R. and Toker, A. (2014) Signalling specificity in the Akt pathway in breast cancer. Biochem. Soc. Trans. 42, 1349-1355 CrossRef PubMed
    • (2014) Biochem. Soc. Trans. , vol.42 , pp. 1349-1355
    • Clark, A.R.1    Toker, A.2
  • 2
    • 84876852762 scopus 로고    scopus 로고
    • Diverse mechanisms of AKT pathway activation in human malignancy
    • CrossRef PubMed
    • Cheung, M. and Testa, J.R. (2013) Diverse mechanisms of AKT pathway activation in human malignancy. Curr. Cancer Drug Targets 13, 234-244 CrossRef PubMed
    • (2013) Curr. Cancer Drug Targets , vol.13 , pp. 234-244
    • Cheung, M.1    Testa, J.R.2
  • 3
    • 27844445642 scopus 로고    scopus 로고
    • Perturbations of the AKT signaling pathway in human cancer
    • CrossRef PubMed
    • Altomare, D.A. and Testa, J.R. (2005) Perturbations of the AKT signaling pathway in human cancer. Oncogene 24, 7455-7464 CrossRef PubMed
    • (2005) Oncogene , vol.24 , pp. 7455-7464
    • Altomare, D.A.1    Testa, J.R.2
  • 4
    • 23944526062 scopus 로고    scopus 로고
    • Activation of AKT kinases in cancer: Implications for therapeutic targeting
    • CrossRef PubMed
    • Bellacosa, A., Kumar, C.C., Di Cristofano, A. and Testa, J.R. (2005) Activation of AKT kinases in cancer: implications for therapeutic targeting. Adv. Cancer Res. 94, 29-86 CrossRef PubMed
    • (2005) Adv. Cancer Res. , vol.94 , pp. 29-86
    • Bellacosa, A.1    Kumar, C.C.2    Di Cristofano, A.3    Testa, J.R.4
  • 5
    • 79960716001 scopus 로고    scopus 로고
    • Akt signalling in health and disease
    • CrossRef PubMed
    • Hers, I., Vincent, E.E. and Tavar é, J.M. (2011) Akt signalling in health and disease. Cell. Signal. 23, 1515-1527 CrossRef PubMed
    • (2011) Cell. Signal. , vol.23 , pp. 1515-1527
    • Hers, I.1    Vincent, E.E.2    Tavar É, J.M.3
  • 6
    • 34250788809 scopus 로고    scopus 로고
    • AKT/PKB signaling: Navigating downstream
    • CrossRef PubMed
    • Manning, B.D. and Cantley, L.C. (2007) AKT/PKB signaling: navigating downstream. Cell 129, 1261-1274 CrossRef PubMed
    • (2007) Cell , vol.129 , pp. 1261-1274
    • Manning, B.D.1    Cantley, L.C.2
  • 7
    • 77749292082 scopus 로고    scopus 로고
    • The Akt isoforms are present at distinct subcellular locations
    • CrossRef PubMed
    • Santi, S.A. and Lee, H. (2010) The Akt isoforms are present at distinct subcellular locations. Am. J. Physiol. Cell Physiol. 298, C580-C591 CrossRef PubMed
    • (2010) Am. J. Physiol. Cell Physiol. , vol.298 , pp. C580-C591
    • Santi, S.A.1    Lee, H.2
  • 8
    • 84862103119 scopus 로고    scopus 로고
    • PI3K-independent AKT activation in cancers: A treasure trove for novel therapeutics
    • CrossRef PubMed
    • Mahajan, K. and Mahajan, N.P. (2012) PI3K-independent AKT activation in cancers: a treasure trove for novel therapeutics. J. Cell. Physiol. 227, 3178-3184 CrossRef PubMed
    • (2012) J. Cell. Physiol. , vol.227 , pp. 3178-3184
    • Mahajan, K.1    Mahajan, N.P.2
  • 9
    • 1542328927 scopus 로고    scopus 로고
    • Structure, regulation and function of PKB/AKT: A major therapeutic target
    • CrossRef PubMed
    • Hanada, M., Feng, J. and Hemmings, B.A. (2004) Structure, regulation and function of PKB/AKT: a major therapeutic target. Biochim. Biophys. Acta 1697, 3-16 CrossRef PubMed
    • (2004) Biochim. Biophys. Acta , vol.1697 , pp. 3-16
    • Hanada, M.1    Feng, J.2    Hemmings, B.A.3
  • 12
    • 15944406764 scopus 로고    scopus 로고
    • PHLPP: A phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth
    • CrossRef PubMed
    • Gao, T., Furnari, F. and Newton, A.C. (2005) PHLPP: a phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth. Mol. Cell 18, 13-24 CrossRef PubMed
    • (2005) Mol. Cell , vol.18 , pp. 13-24
    • Gao, T.1    Furnari, F.2    Newton, A.C.3
  • 13
    • 0029942186 scopus 로고    scopus 로고
    • Activation and phosphorylation of a pleckstrin homology domain containing protein kinase (RAC-PK/PKB) promoted by serum and protein phosphatase inhibitors
    • CrossRef PubMed
    • Andjelkovic, M., Jakubowicz, T., Cron, P., Ming, X.F., Han, J.W. and Hemmings, B.A. (1996) Activation and phosphorylation of a pleckstrin homology domain containing protein kinase (RAC-PK/PKB) promoted by serum and protein phosphatase inhibitors. Proc. Natl. Acad. Sci. U.S.A. 93, 5699-5704 CrossRef PubMed
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 5699-5704
    • Andjelkovic, M.1    Jakubowicz, T.2    Cron, P.3    Ming, X.F.4    Han, J.W.5    Hemmings, B.A.6
  • 15
    • 13844312400 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
    • CrossRef PubMed
    • Sarbassov, D.D., Guertin, D.A., Ali, S.M. and Sabatini, D.M. (2005) Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex. Science 307, 1098-1101 CrossRef PubMed
    • (2005) Science , vol.307 , pp. 1098-1101
    • Sarbassov, D.D.1    Guertin, D.A.2    Ali, S.M.3    Sabatini, D.M.4
  • 17
    • 77953408308 scopus 로고    scopus 로고
    • Physiological regulation of Akt activity and stability
    • PubMed
    • Liao, Y. and Hung, M.C. (2010) Physiological regulation of Akt activity and stability. Am. J. Transl. Res. 2, 19-42 PubMed
    • (2010) Am. J. Transl. Res. , vol.2 , pp. 19-42
    • Liao, Y.1    Hung, M.C.2
  • 18
    • 0029810181 scopus 로고    scopus 로고
    • Akt, a pleckstrin homology domain containing kinase, is activated primarily by phosphorylation
    • CrossRef PubMed
    • Kohn, A.D., Takeuchi, F. and Roth, R.A. (1996) Akt, a pleckstrin homology domain containing kinase, is activated primarily by phosphorylation. J. Biol. Chem. 271, 21920-21926 CrossRef PubMed
    • (1996) J. Biol. Chem. , vol.271 , pp. 21920-21926
    • Kohn, A.D.1    Takeuchi, F.2    Roth, R.A.3
  • 20
    • 67650092976 scopus 로고    scopus 로고
    • Peptidyl-prolyl cis/trans isomerase Pin1 is critical for the regulation of PKB/Akt stability and activation phosphorylation
    • CrossRef PubMed
    • Liao, Y., Wei, Y., Zhou, X., Yang, J.-Y., Dai, C., Chen, Y.-J., Agarwal, N.K., Sarbassov, D., Shi, D., Yu, D. et al. (2009) Peptidyl-prolyl cis/trans isomerase Pin1 is critical for the regulation of PKB/Akt stability and activation phosphorylation. Oncogene 28, 2436-2445 CrossRef PubMed
    • (2009) Oncogene , vol.28 , pp. 2436-2445
    • Liao, Y.1    Wei, Y.2    Zhou, X.3    Yang, J.-Y.4    Dai, C.5    Chen, Y.-J.6    Agarwal, N.K.7    Sarbassov, D.8    Shi, D.9    Yu, D.10
  • 21
    • 0037064005 scopus 로고    scopus 로고
    • Direct identification of tyrosine 474 as a regulatory phosphorylation site for the Akt protein kinase
    • CrossRef PubMed
    • Conus, N.M., Hannan, K.M., Cristiano, B.E., Hemmings, B.A. and Pearson, R.B. (2002) Direct identification of tyrosine 474 as a regulatory phosphorylation site for the Akt protein kinase. J. Biol. Chem. 277, 38021-38028 CrossRef PubMed
    • (2002) J. Biol. Chem. , vol.277 , pp. 38021-38028
    • Conus, N.M.1    Hannan, K.M.2    Cristiano, B.E.3    Hemmings, B.A.4    Pearson, R.B.5
  • 23
    • 70350502303 scopus 로고    scopus 로고
    • Dephosphorylation and inactivation of Akt/PKB is counteracted by protein kinase CK2 in HEK 293T cells
    • CrossRef PubMed
    • Di Maira, G., Brustolon, F., Pinna, L.A. and Ruzzene, M. (2009) Dephosphorylation and inactivation of Akt/PKB is counteracted by protein kinase CK2 in HEK 293T cells. Cell. Mol. Life Sci. 66, 3363-3373 CrossRef PubMed
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 3363-3373
    • Di Maira, G.1    Brustolon, F.2    Pinna, L.A.3    Ruzzene, M.4
  • 24
    • 84869185995 scopus 로고    scopus 로고
    • Inactivation of the enzyme GSK3α by the kinase IKKi promotes AKT-mTOR signaling pathway that mediates interleukin-1-induced Th17 cell maintenance
    • CrossRef PubMed
    • Gulen, M.F., Bulek, K., Xiao, H., Yu, M., Gao, J., Sun, L., Beurel, E., Kaidanovich-Beilin, O., Fox, P.L., DiCorleto, P.E. et al. (2012) Inactivation of the enzyme GSK3α by the kinase IKKi promotes AKT-mTOR signaling pathway that mediates interleukin-1-induced Th17 cell maintenance. Immunity 37, 800-812 CrossRef PubMed
    • (2012) Immunity , vol.37 , pp. 800-812
    • Gulen, M.F.1    Bulek, K.2    Xiao, H.3    Yu, M.4    Gao, J.5    Sun, L.6    Beurel, E.7    Kaidanovich-Beilin, O.8    Fox, P.L.9    DiCorleto, P.E.10
  • 25
    • 0032881288 scopus 로고    scopus 로고
    • AKT/PKB and other D3 phosphoinositide-regulated kinases: Kinase activation by phosphoinositide-dependent phosphorylation
    • CrossRef PubMed
    • Chan, T.O., Rittenhouse, S.E. and Tsichlis, P.N. (1999) AKT/PKB and other D3 phosphoinositide-regulated kinases: kinase activation by phosphoinositide-dependent phosphorylation. Annu. Rev. Biochem. 68, 965-1014 CrossRef PubMed
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 965-1014
    • Chan, T.O.1    Rittenhouse, S.E.2    Tsichlis, P.N.3
  • 26
    • 0035936653 scopus 로고    scopus 로고
    • PDK2: A complex tail in one Akt
    • PubMed
    • Chan, T.O. and Tsichlis, P.N. (2001) PDK2: a complex tail in one Akt. Sci. STKE 2001, pe1 PubMed
    • (2001) Sci. STKE , vol.2001 , pp. pe1
    • Chan, T.O.1    Tsichlis, P.N.2
  • 27
    • 70349239101 scopus 로고    scopus 로고
    • New insights into mTOR signaling: MTORC2 and beyond
    • CrossRef PubMed
    • Alessi, D.R., Pearce, L.R. and García-Martínez, J.M. (2009) New insights into mTOR signaling: mTORC2 and beyond. Sci. Signal. 2, pe27 CrossRef PubMed
    • (2009) Sci. Signal. , vol.2 , pp. pe27
    • Alessi, D.R.1    Pearce, L.R.2    García-Martínez, J.M.3
  • 28
    • 47949104258 scopus 로고    scopus 로고
    • Essential function of TORC2 in PKC and Akt turn motif phosphorylation, maturation and signalling
    • CrossRef PubMed
    • Ikenoue, T., Inoki, K., Yang, Q., Zhou, X. and Guan, K.-L. (2008) Essential function of TORC2 in PKC and Akt turn motif phosphorylation, maturation and signalling. EMBO J. 27, 1919-1931 CrossRef PubMed
    • (2008) EMBO J , vol.27 , pp. 1919-1931
    • Ikenoue, T.1    Inoki, K.2    Yang, Q.3    Zhou, X.4    Guan, K.-L.5
  • 29
    • 47949125486 scopus 로고    scopus 로고
    • The mammalian target of rapamycin complex 2 controls folding and stability of Akt and protein kinase C
    • CrossRef PubMed
    • Facchinetti, V., Ouyang, W., Wei, H., Soto, N., Lazorchak, A., Gould, C., Lowry, C., Newton, A.C., Mao, Y., Miao, R.Q. et al. (2008) The mammalian target of rapamycin complex 2 controls folding and stability of Akt and protein kinase C. EMBO J. 27, 1932-1943 CrossRef PubMed
    • (2008) EMBO J , vol.27 , pp. 1932-1943
    • Facchinetti, V.1    Ouyang, W.2    Wei, H.3    Soto, N.4    Lazorchak, A.5    Gould, C.6    Lowry, C.7    Newton, A.C.8    Mao, Y.9    Miao, R.Q.10
  • 30
    • 78649712949 scopus 로고    scopus 로고
    • MTORC2 can associate with ribosomes to promote cotranslational phosphorylation and stability of nascent Akt polypeptide
    • CrossRef PubMed
    • Oh, W.J., Wu, C.C., Kim, S.J., Facchinetti, V., Julien, L.A., Finlan, M., Roux, P.P., Su, B. and Jacinto, E. (2010) mTORC2 can associate with ribosomes to promote cotranslational phosphorylation and stability of nascent Akt polypeptide. EMBO J. 29, 3939-3951 CrossRef PubMed
    • (2010) EMBO J , vol.29 , pp. 3939-3951
    • Oh, W.J.1    Wu, C.C.2    Kim, S.J.3    Facchinetti, V.4    Julien, L.A.5    Finlan, M.6    Roux, P.P.7    Su, B.8    Jacinto, E.9
  • 31
    • 33644841906 scopus 로고    scopus 로고
    • C-Jun N-terminal kinases mediate reactivation of Akt and cardiomyocyte survival after hypoxic injury in vitro and in vivo
    • CrossRef PubMed
    • Shao, Z., Bhattacharya, K., Hsich, E., Park, L., Walters, B., Germann, U., Wang, Y.M., Kyriakis, J., Mohanlal, R., Kuida, K. et al. (2006) c-Jun N-terminal kinases mediate reactivation of Akt and cardiomyocyte survival after hypoxic injury in vitro and in vivo. Circ. Res. 98, 111-118 CrossRef PubMed
    • (2006) Circ. Res. , vol.98 , pp. 111-118
    • Shao, Z.1    Bhattacharya, K.2    Hsich, E.3    Park, L.4    Walters, B.5    Germann, U.6    Wang, Y.M.7    Kyriakis, J.8    Mohanlal, R.9    Kuida, K.10
  • 32
    • 79954606507 scopus 로고    scopus 로고
    • C-Jun N-terminal kinase (JNK-1) confers protection against brief but not extended ischemia during acute myocardial infarction
    • CrossRef PubMed
    • Wei, J., Wang, W., Chopra, I., Li, H.F., Dougherty, C.J., Adi, J., Adi, N., Wang, H. and Webster, K.A. (2011) c-Jun N-terminal kinase (JNK-1) confers protection against brief but not extended ischemia during acute myocardial infarction. J. Biol. Chem. 286, 13995-14006 CrossRef PubMed
    • (2011) J. Biol. Chem. , vol.286 , pp. 13995-14006
    • Wei, J.1    Wang, W.2    Chopra, I.3    Li, H.F.4    Dougherty, C.J.5    Adi, J.6    Adi, N.7    Wang, H.8    Webster, K.A.9
  • 33
    • 84899484738 scopus 로고    scopus 로고
    • Cell-cycle-regulated activation of Akt kinase by phosphorylation at its carboxyl terminus
    • CrossRef PubMed
    • Liu, P., Begley, M., Michowski, W., Inuzuka, H., Ginzberg, M., Gao, D., Tsou, P., Gan, W., Papa, A., Kim, B.M. et al. (2014) Cell-cycle-regulated activation of Akt kinase by phosphorylation at its carboxyl terminus. Nature 508, 541-545 CrossRef PubMed
    • (2014) Nature , vol.508 , pp. 541-545
    • Liu, P.1    Begley, M.2    Michowski, W.3    Inuzuka, H.4    Ginzberg, M.5    Gao, D.6    Tsou, P.7    Gan, W.8    Papa, A.9    Kim, B.M.10
  • 34
    • 84904512846 scopus 로고    scopus 로고
    • Phosphorylation of Akt at the C-terminal tail triggers Akt activation
    • CrossRef PubMed
    • Liu, P., Wang, Z. and Wei, W. (2014) Phosphorylation of Akt at the C-terminal tail triggers Akt activation. Cell Cycle 13, 2162-2164 CrossRef PubMed
    • (2014) Cell Cycle , vol.13 , pp. 2162-2164
    • Liu, P.1    Wang, Z.2    Wei, W.3
  • 36
    • 0029807471 scopus 로고    scopus 로고
    • Akt is a direct target of the phosphatidylinositol 3-kinase: Activation by growth factors, v-src and v-Ha-ras, in Sf9 and mammalian cells
    • CrossRef PubMed
    • Datta, K., Bellacosaf, A., Chan, T.O. and Tsichlis, P.N. (1996) Akt is a direct target of the phosphatidylinositol 3-kinase: Activation by growth factors, v-src and v-Ha-ras, in Sf9 and mammalian cells. J. Biol. Chem. 271, 30835-30839 CrossRef PubMed
    • (1996) J. Biol. Chem. , vol.271 , pp. 30835-30839
    • Datta, K.1    Bellacosaf, A.2    Chan, T.O.3    Tsichlis, P.N.4
  • 37
    • 0033393957 scopus 로고    scopus 로고
    • TRANCE, a TNF family member, activates Akt/PKB through a signaling complex involving TRAF6 and c-Src
    • Wong, B.R., Besser, D., Kim, N., Arron, J.R., Vologodskaia, M., Hanafusa, H. and Choi, Y. (1999) TRANCE, a TNF family member, activates Akt/PKB through a signaling complex involving TRAF6 and c-Src. Mol. Cell 4, 1041-1049
    • (1999) Mol. Cell , vol.4 , pp. 1041-1049
    • Wong, B.R.1    Besser, D.2    Kim, N.3    Arron, J.R.4    Vologodskaia, M.5    Hanafusa, H.6    Choi, Y.7
  • 39
    • 0037938847 scopus 로고    scopus 로고
    • Interaction between Src and a C-terminal proline-rich motif of Akt is required for Akt activation
    • CrossRef PubMed
    • Jiang, T. and Qiu, Y. (2003) Interaction between Src and a C-terminal proline-rich motif of Akt is required for Akt activation. J. Biol. Chem. 278, 15789-15793 CrossRef PubMed
    • (2003) J. Biol. Chem. , vol.278 , pp. 15789-15793
    • Jiang, T.1    Qiu, Y.2
  • 40
    • 61349130027 scopus 로고    scopus 로고
    • Deficiency of a β -arrestin-2 signal complex contributes to insulin resistance
    • CrossRef PubMed
    • Luan, B., Zhao, J., Wu, H., Duan, B., Shu, G., Wang, X., Li, D., Jia, W., Kang, J. and Pei, G. (2009) Deficiency of a β -arrestin-2 signal complex contributes to insulin resistance. Nature 457, 1146-1149 CrossRef PubMed
    • (2009) Nature , vol.457 , pp. 1146-1149
    • Luan, B.1    Zhao, J.2    Wu, H.3    Duan, B.4    Shu, G.5    Wang, X.6    Li, D.7    Jia, W.8    Kang, J.9    Pei, G.10
  • 41
    • 77956620778 scopus 로고    scopus 로고
    • Protein tyrosine kinase 6 directly phosphorylates AKT and promotes AKT activation in response to epidermal growth factor
    • CrossRef PubMed
    • Zheng, Y., Peng, M., Wang, Z., Asara, J.M. and Tyner, A.L. (2010) Protein tyrosine kinase 6 directly phosphorylates AKT and promotes AKT activation in response to epidermal growth factor. Mol. Cell. Biol. 30, 4280-4292 CrossRef PubMed
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 4280-4292
    • Zheng, Y.1    Peng, M.2    Wang, Z.3    Asara, J.M.4    Tyner, A.L.5
  • 42
    • 0033594480 scopus 로고    scopus 로고
    • PDK1 acquires PDK2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK2
    • CrossRef PubMed
    • Balendran, A., Casamayor, A., Deak, M., Paterson, A., Gaffney, P., Currie, R., Downes, C.P. and Alessi, D.R. (1999) PDK1 acquires PDK2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK2. Curr. Biol. 9, 393-404 CrossRef PubMed
    • (1999) Curr. Biol. , vol.9 , pp. 393-404
    • Balendran, A.1    Casamayor, A.2    Deak, M.3    Paterson, A.4    Gaffney, P.5    Currie, R.6    Downes, C.P.7    Alessi, D.R.8
  • 43
    • 80054804471 scopus 로고    scopus 로고
    • IKBKE protein activates Akt independent of phosphatidylinositol 3-kinase/PDK1/mTORC2 and the pleckstrin homology domain to sustain malignant transformation
    • CrossRef PubMed
    • Guo, J.P., Coppola, D. and Cheng, J.Q. (2011) IKBKE protein activates Akt independent of phosphatidylinositol 3-kinase/PDK1/mTORC2 and the pleckstrin homology domain to sustain malignant transformation. J. Biol. Chem. 286, 37389-37398 CrossRef PubMed
    • (2011) J. Biol. Chem. , vol.286 , pp. 37389-37398
    • Guo, J.P.1    Coppola, D.2    Cheng, J.Q.3
  • 44
    • 79251542927 scopus 로고    scopus 로고
    • Akt contributes to activation of the TRIF-dependent signaling pathways of TLRs by interacting with TANK-binding kinase 1
    • CrossRef PubMed
    • Joung, S.M., Park, Z.-Y., Rani, S., Takeuchi, O., Akira, S. and Lee, J.Y. (2011) Akt contributes to activation of the TRIF-dependent signaling pathways of TLRs by interacting with TANK-binding kinase 1. J. Immunol. 186, 499-507 CrossRef PubMed
    • (2011) J. Immunol. , vol.186 , pp. 499-507
    • Joung, S.M.1    Park, Z.-Y.2    Rani, S.3    Takeuchi, O.4    Akira, S.5    Lee, J.Y.6
  • 45
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • CrossRef PubMed
    • Choudhary, C., Kumar, C., Gnad, F., Nielsen, M.L., Rehman, M., Walther, T.C., Olsen, J.V. and Mann, M. (2009) Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 325, 834-840 CrossRef PubMed
    • (2009) Science , vol.325 , pp. 834-840
    • Choudhary, C.1    Kumar, C.2    Gnad, F.3    Nielsen, M.L.4    Rehman, M.5    Walther, T.C.6    Olsen, J.V.7    Mann, M.8
  • 48
    • 84872831805 scopus 로고    scopus 로고
    • Cysteine oxidative posttranslational modifications: Emerging regulation in the cardiovascular system
    • CrossRef PubMed
    • Chung, H.S., Wang, S.-B., Venkatraman, V., Murray, C.I. and Van Eyk, J.E. (2013) Cysteine oxidative posttranslational modifications: emerging regulation in the cardiovascular system. Circ. Res. 112, 382-392 CrossRef PubMed
    • (2013) Circ. Res. , vol.112 , pp. 382-392
    • Chung, H.S.1    Wang, S.-B.2    Venkatraman, V.3    Murray, C.I.4    Van Eyk, J.E.5
  • 49
    • 79960286223 scopus 로고    scopus 로고
    • Signal transduction by reactive oxygen species
    • CrossRef PubMed
    • Finkel, T. (2011) Signal transduction by reactive oxygen species. J. Cell Biol. 194, 7-15 CrossRef PubMed
    • (2011) J. Cell Biol. , vol.194 , pp. 7-15
    • Finkel, T.1
  • 51
    • 80053458043 scopus 로고    scopus 로고
    • Oxidation of Akt2 kinase promotes cell migration and regulates G1 -S transition in the cell cycle
    • CrossRef PubMed
    • Wani, R., Bharathi, N.S., Field, J., Tsang, A.W. and Furdui, C.M. (2011) Oxidation of Akt2 kinase promotes cell migration and regulates G1 -S transition in the cell cycle. Cell Cycle 10, 3263-3268 CrossRef PubMed
    • (2011) Cell Cycle , vol.10 , pp. 3263-3268
    • Wani, R.1    Bharathi, N.S.2    Field, J.3    Tsang, A.W.4    Furdui, C.M.5
  • 52
    • 79959381299 scopus 로고    scopus 로고
    • Cross talk between O-GlcNAcylation and phosphorylation: Roles in signaling, transcription, and chronic disease
    • CrossRef PubMed
    • Hart, G.W., Slawson, C., Ramirez-Correa, G. and Lagerlof, O. (2011) Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease. Annu. Rev. Biochem. 80, 825-858 CrossRef PubMed
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 825-858
    • Hart, G.W.1    Slawson, C.2    Ramirez-Correa, G.3    Lagerlof, O.4
  • 53
    • 72449187655 scopus 로고    scopus 로고
    • The intersections between O-GlcNAcylation and phosphorylation: Implications for multiple signaling pathways
    • CrossRef PubMed
    • Zeidan, Q. and Hart, G.W. (2010) The intersections between O-GlcNAcylation and phosphorylation: implications for multiple signaling pathways. J. Cell Sci. 123, 13-22 CrossRef PubMed
    • (2010) J. Cell Sci. , vol.123 , pp. 13-22
    • Zeidan, Q.1    Hart, G.W.2
  • 54
    • 22244471058 scopus 로고    scopus 로고
    • O-GlcNAc modification on IRS-1 and Akt2 by PUGNAc inhibits their phosphorylation and induces insulin resistance in rat primary adipocytes
    • CrossRef PubMed
    • Park, S.Y., Ryu, J. and Lee, W. (2005) O-GlcNAc modification on IRS-1 and Akt2 by PUGNAc inhibits their phosphorylation and induces insulin resistance in rat primary adipocytes. Exp. Mol. Med. 37, 220-229 CrossRef PubMed
    • (2005) Exp. Mol. Med. , vol.37 , pp. 220-229
    • Park, S.Y.1    Ryu, J.2    Lee, W.3
  • 55
    • 33646581015 scopus 로고    scopus 로고
    • Akt1 is dynamically modified with O-GlcNAc following treatments with PUGNAc and insulin-like growth factor-1
    • CrossRef PubMed
    • Gandy, J.C., Rountree, A.E. and Bijur, G.N. (2006) Akt1 is dynamically modified with O-GlcNAc following treatments with PUGNAc and insulin-like growth factor-1. FEBS Lett. 580, 3051-3058 CrossRef PubMed
    • (2006) FEBS Lett , vol.580 , pp. 3051-3058
    • Gandy, J.C.1    Rountree, A.E.2    Bijur, G.N.3
  • 56
    • 52049120841 scopus 로고    scopus 로고
    • Regulation of the O-linked β -N-acetylglucosamine transferase by insulin signaling
    • CrossRef PubMed
    • Whelan, S.A., Lane, M.D. and Hart, G.W. (2008) Regulation of the O-linked β -N-acetylglucosamine transferase by insulin signaling. J. Biol. Chem. 283, 21411-21417 CrossRef PubMed
    • (2008) J. Biol. Chem. , vol.283 , pp. 21411-21417
    • Whelan, S.A.1    Lane, M.D.2    Hart, G.W.3
  • 57
    • 33644698706 scopus 로고    scopus 로고
    • Identification of the major site of O-linked β -N-acetylglucosamine modification in the C terminus of insulin receptor substrate-1
    • CrossRef PubMed
    • Ball, L.E., Berkaw, M.N. and Buse, M.G. (2006) Identification of the major site of O-linked β -N-acetylglucosamine modification in the C terminus of insulin receptor substrate-1. Mol. Cell. Proteomics 5, 313-323 CrossRef PubMed
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 313-323
    • Ball, L.E.1    Berkaw, M.N.2    Buse, M.G.3
  • 58
    • 72449170135 scopus 로고    scopus 로고
    • O-linked N-acetylglucosamine modification of insulin receptor substrate-1 occurs in close proximity to multiple SH2 domain binding motifs
    • CrossRef PubMed
    • Klein, A.L., Berkaw, M.N., Buse, M.G. and Ball, L.E. (2009) O-linked N-acetylglucosamine modification of insulin receptor substrate-1 occurs in close proximity to multiple SH2 domain binding motifs. Mol. Cell. Proteomics 8, 2733-2745 CrossRef PubMed
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 2733-2745
    • Klein, A.L.1    Berkaw, M.N.2    Buse, M.G.3    Ball, L.E.4
  • 59
    • 0037117511 scopus 로고    scopus 로고
    • Elevated nucleocytoplasmic glycosylation by O-GlcNAc results in insulin resistance associated with defects in Akt activation in 3T3-L1 adipocytes
    • CrossRef PubMed
    • Vosseller, K., Wells, L., Lane, M.D. and Hart, G.W. (2002) Elevated nucleocytoplasmic glycosylation by O-GlcNAc results in insulin resistance associated with defects in Akt activation in 3T3-L1 adipocytes. Proc. Natl. Acad. Sci. U.S.A. 99, 5313-5318 CrossRef PubMed
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 5313-5318
    • Vosseller, K.1    Wells, L.2    Lane, M.D.3    Hart, G.W.4
  • 61
    • 84861306218 scopus 로고    scopus 로고
    • Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates Akt signaling
    • CrossRef PubMed
    • Wang, S., Huang, X., Sun, D., Xin, X., Pan, Q., Peng, S., Liang, Z., Luo, C., Yang, Y., Jiang, H. et al. (2012) Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates Akt signaling. PLoS ONE 7, e37427 CrossRef PubMed
    • (2012) PLoS ONE , vol.7 , pp. e37427
    • Wang, S.1    Huang, X.2    Sun, D.3    Xin, X.4    Pan, Q.5    Peng, S.6    Liang, Z.7    Luo, C.8    Yang, Y.9    Jiang, H.10
  • 62
    • 45149112314 scopus 로고    scopus 로고
    • O-GlcNAc modulation at Akt1 Ser473 correlates with apoptosis of murine pancreatic β cells
    • CrossRef PubMed
    • Kang, E.-S., Han, D., Park, J., Kwak, T.K., Oh, M.-A., Lee, S.-A., Choi, S., Park, Z.Y., Kim, Y. and Lee, J.W. (2008) O-GlcNAc modulation at Akt1 Ser473 correlates with apoptosis of murine pancreatic β cells. Exp. Cell Res. 314, 2238-2248 CrossRef PubMed
    • (2008) Exp. Cell Res. , vol.314 , pp. 2238-2248
    • Kang, E.-S.1    Han, D.2    Park, J.3    Kwak, T.K.4    Oh, M.-A.5    Lee, S.-A.6    Choi, S.7    Park, Z.Y.8    Kim, Y.9    Lee, J.W.10
  • 63
    • 84897559222 scopus 로고    scopus 로고
    • Activation of AKT by O-linked N-acetylglucosamine induces vascular calcification in diabetes mellitus
    • CrossRef PubMed
    • Heath, J.M., Sun, Y., Yuan, K., Bradley, W.E., Litovsky, S., Dell'Italia, L.J., Chatham, J.C., Wu, H. and Chen, Y. (2014) Activation of AKT by O-linked N-acetylglucosamine induces vascular calcification in diabetes mellitus. Circ. Res. 114, 1094-1102 CrossRef PubMed
    • (2014) Circ. Res. , vol.114 , pp. 1094-1102
    • Heath, J.M.1    Sun, Y.2    Yuan, K.3    Bradley, W.E.4    Litovsky, S.5    Dell'Italia, L.J.6    Chatham, J.C.7    Wu, H.8    Chen, Y.9
  • 64
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • CrossRef PubMed
    • Finley, D. (2009) Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu. Rev. Biochem. 78, 477-513 CrossRef PubMed
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 477-513
    • Finley, D.1
  • 65
    • 0037131187 scopus 로고    scopus 로고
    • Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function
    • CrossRef PubMed
    • Basso, A.D., Solit, D.B., Chiosis, G., Giri, B., Tsichlis, P. and Rosen, N. (2002) Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function. J. Biol. Chem. 277, 39858-39866 CrossRef PubMed
    • (2002) J. Biol. Chem. , vol.277 , pp. 39858-39866
    • Basso, A.D.1    Solit, D.B.2    Chiosis, G.3    Giri, B.4    Tsichlis, P.5    Rosen, N.6
  • 68
    • 80051469504 scopus 로고    scopus 로고
    • Akt phosphorylation at Thr308 and Ser473 is required for CHIP-mediated ubiquitination of the kinase
    • CrossRef PubMed
    • Su, C.H., Wang, C.Y., Lan, K.H., Li, C.P., Chao, Y., Lin, H.C., Lee, S.D. and Lee, W.P. (2011) Akt phosphorylation at Thr308 and Ser473 is required for CHIP-mediated ubiquitination of the kinase. Cell. Signal. 23, 1824-1830 CrossRef PubMed
    • (2011) Cell. Signal. , vol.23 , pp. 1824-1830
    • Su, C.H.1    Wang, C.Y.2    Lan, K.H.3    Li, C.P.4    Chao, Y.5    Lin, H.C.6    Lee, S.D.7    Lee, W.P.8
  • 72
    • 84861552793 scopus 로고    scopus 로고
    • The Skp2-SCF E3 ligase regulates Akt ubiquitination, glycolysis, herceptin sensitivity, and tumorigenesis
    • CrossRef PubMed
    • Chan, C.H., Li, C.F., Yang, W.L., Gao, Y., Lee, S.W., Feng, Z., Huang, H.Y., Tsai, K.K., Flores, L.G., Shao, Y. et al. (2012) The Skp2-SCF E3 ligase regulates Akt ubiquitination, glycolysis, herceptin sensitivity, and tumorigenesis. Cell 149, 1098-1111 CrossRef PubMed
    • (2012) Cell , vol.149 , pp. 1098-1111
    • Chan, C.H.1    Li, C.F.2    Yang, W.L.3    Gao, Y.4    Lee, S.W.5    Feng, Z.6    Huang, H.Y.7    Tsai, K.K.8    Flores, L.G.9    Shao, Y.10
  • 73
    • 84872736566 scopus 로고    scopus 로고
    • Ubiquitin-dependent regulation of phospho-AKT dynamics by the ubiquitin E3 ligase, NEDD4-1, in the insulin-like growth factor-1 response
    • CrossRef PubMed
    • Fan, C.-D., Lum, M.A., Xu, C., Black, J.D. and Wang, X. (2013) Ubiquitin-dependent regulation of phospho-AKT dynamics by the ubiquitin E3 ligase, NEDD4-1, in the insulin-like growth factor-1 response. J. Biol. Chem. 288, 1674-1684 CrossRef PubMed
    • (2013) J. Biol. Chem. , vol.288 , pp. 1674-1684
    • Fan, C.-D.1    Lum, M.A.2    Xu, C.3    Black, J.D.4    Wang, X.5
  • 74
    • 84860284249 scopus 로고    scopus 로고
    • CYLD negatively regulates transforming growth factor-β -signalling via deubiquitinating Akt
    • CrossRef PubMed
    • Lim, J.H., Jono, H., Komatsu, K., Woo, C.-H., Lee, J., Miyata, M., Matsuno, T., Xu, X., Huang, Y., Zhang, W. et al. (2012) CYLD negatively regulates transforming growth factor-β -signalling via deubiquitinating Akt. Nat. Commun. 3, 771 CrossRef PubMed
    • (2012) Nat. Commun. , vol.3 , pp. 771
    • Lim, J.H.1    Jono, H.2    Komatsu, K.3    Woo, C.-H.4    Lee, J.5    Miyata, M.6    Matsuno, T.7    Xu, X.8    Huang, Y.9    Zhang, W.10
  • 75
    • 84872566774 scopus 로고    scopus 로고
    • Cycles of ubiquitination and deubiquitination critically regulate growth factor-mediated activation of Akt signaling
    • PubMed
    • Yang, W.-L., Jin, G., Li, C.-F., Jeong, Y.S., Moten, A., Xu, D., Feng, Z., Chen, W., Cai, Z., Darnay, B. et al. (2013) Cycles of ubiquitination and deubiquitination critically regulate growth factor-mediated activation of Akt signaling. Sci. Signal. 6, ra3 PubMed
    • (2013) Sci. Signal. , vol.6 , pp. ra3
    • Yang, W.-L.1    Jin, G.2    Li, C.-F.3    Jeong, Y.S.4    Moten, A.5    Xu, D.6    Feng, Z.7    Chen, W.8    Cai, Z.9    Darnay, B.10
  • 77
    • 45849153870 scopus 로고    scopus 로고
    • The HECT family of E3 ubiquitin ligases: Multiple players in cancer development
    • CrossRef PubMed
    • Bernassola, F., Karin, M., Ciechanover, A. and Melino, G. (2008) The HECT family of E3 ubiquitin ligases: multiple players in cancer development. Cancer Cell 14, 10-21 CrossRef PubMed
    • (2008) Cancer Cell , vol.14 , pp. 10-21
    • Bernassola, F.1    Karin, M.2    Ciechanover, A.3    Melino, G.4
  • 78
    • 67649964217 scopus 로고    scopus 로고
    • RING domain E3 ubiquitin ligases
    • CrossRef PubMed
    • Deshaies, R.J. and Joazeiro, C.A. (2009) RING domain E3 ubiquitin ligases. Annu. Rev. Biochem. 78, 399-434 CrossRef PubMed
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 399-434
    • Deshaies, R.J.1    Joazeiro, C.A.2
  • 79
    • 84884761456 scopus 로고    scopus 로고
    • Akt SUMOylation regulates cell proliferation and tumorigenesis
    • CrossRef PubMed
    • Li, R., Wei, J., Jiang, C., Liu, D., Deng, L., Zhang, K. and Wang, P. (2013) Akt SUMOylation regulates cell proliferation and tumorigenesis. Cancer Res. 73, 5742-5753 CrossRef PubMed
    • (2013) Cancer Res , vol.73 , pp. 5742-5753
    • Li, R.1    Wei, J.2    Jiang, C.3    Liu, D.4    Deng, L.5    Zhang, K.6    Wang, P.7
  • 80
    • 84886683522 scopus 로고    scopus 로고
    • Modification of Akt by SUMO conjugation regulates alternative splicing and cell cycle
    • CrossRef PubMed
    • Risso, G., Pelisch, F., Pozzi, B., Mammi, P., Blaustein, M., Colman-Lerner, A. and Srebrow, A. (2013) Modification of Akt by SUMO conjugation regulates alternative splicing and cell cycle. Cell Cycle 12, 3165-3174 CrossRef PubMed
    • (2013) Cell Cycle , vol.12 , pp. 3165-3174
    • Risso, G.1    Pelisch, F.2    Pozzi, B.3    Mammi, P.4    Blaustein, M.5    Colman-Lerner, A.6    Srebrow, A.7
  • 83
    • 84863336040 scopus 로고    scopus 로고
    • SUMO1 modification of PTEN regulates tumorigenesis by controlling its association with the plasma membrane
    • CrossRef PubMed
    • Huang, J., Yan, J., Zhang, J., Zhu, S., Wang, Y., Shi, T., Zhu, C., Chen, C., Liu, X., Cheng, J. et al. (2012) SUMO1 modification of PTEN regulates tumorigenesis by controlling its association with the plasma membrane. Nat. Commun. 3, 911 CrossRef PubMed
    • (2012) Nat. Commun. , vol.3 , pp. 911
    • Huang, J.1    Yan, J.2    Zhang, J.3    Zhu, S.4    Wang, Y.5    Shi, T.6    Zhu, C.7    Chen, C.8    Liu, X.9    Cheng, J.10
  • 86
    • 84869091913 scopus 로고    scopus 로고
    • Protein group modification and synergy in the SUMO pathway as exemplified in DNA repair
    • CrossRef PubMed
    • Psakhye, I. and Jentsch, S. (2012) Protein group modification and synergy in the SUMO pathway as exemplified in DNA repair. Cell 151, 807-820 CrossRef PubMed
    • (2012) Cell , vol.151 , pp. 807-820
    • Psakhye, I.1    Jentsch, S.2
  • 87
    • 84878944582 scopus 로고    scopus 로고
    • Sumoylation: A regulatory protein modification in health and disease
    • CrossRef PubMed
    • Flotho, A. and Melchior, F. (2013) Sumoylation: a regulatory protein modification in health and disease. Annu. Rev. Biochem. 82, 357-385 CrossRef PubMed
    • (2013) Annu. Rev. Biochem. , vol.82 , pp. 357-385
    • Flotho, A.1    Melchior, F.2
  • 88
    • 84856264773 scopus 로고    scopus 로고
    • A two-dimensional ERK-AKT signaling code for an NGF-triggered cell-fate decision
    • CrossRef PubMed
    • Chen, J.-Y., Lin, J.-R., Cimprich, K.A. and Meyer, T. (2012) A two-dimensional ERK-AKT signaling code for an NGF-triggered cell-fate decision. Mol. Cell 45, 196-209 CrossRef PubMed
    • (2012) Mol. Cell , vol.45 , pp. 196-209
    • Chen, J.-Y.1    Lin, J.-R.2    Cimprich, K.A.3    Meyer, T.4
  • 89
    • 34249016897 scopus 로고    scopus 로고
    • Akt up- and down-regulation in response to endoplasmic reticulum stress
    • CrossRef PubMed
    • Hosoi, T., Hyoda, K., Okuma, Y., Nomura, Y. and Ozawa, K. (2007) Akt up- and down-regulation in response to endoplasmic reticulum stress. Brain Res. 1152, 27-31 CrossRef PubMed
    • (2007) Brain Res , vol.1152 , pp. 27-31
    • Hosoi, T.1    Hyoda, K.2    Okuma, Y.3    Nomura, Y.4    Ozawa, K.5
  • 92
    • 84927591752 scopus 로고    scopus 로고
    • Phosphorylation of the translation initiation factor eIF2α at serine 51 determines the cell fate decisions of Akt in response to oxidative stress
    • CrossRef PubMed
    • Rajesh, K., Krishnamoorthy, J., Kazimierczak, U., Tenkerian, C., Papadakis, A.I., Wang, S., Huang, S. and Koromilas, A.E. (2015) Phosphorylation of the translation initiation factor eIF2α at serine 51 determines the cell fate decisions of Akt in response to oxidative stress. Cell Death Dis. 6, e1591 CrossRef PubMed
    • (2015) Cell Death Dis , vol.6 , pp. e1591
    • Rajesh, K.1    Krishnamoorthy, J.2    Kazimierczak, U.3    Tenkerian, C.4    Papadakis, A.I.5    Wang, S.6    Huang, S.7    Koromilas, A.E.8
  • 93
    • 33644840939 scopus 로고    scopus 로고
    • Prime time for JNK-mediated Akt reactivation in hypoxia-reoxygenation
    • CrossRef PubMed
    • Shaw, J. and Kirshenbaum, L.A. (2006) Prime time for JNK-mediated Akt reactivation in hypoxia-reoxygenation. Circ. Res. 98, 7-9 CrossRef PubMed
    • (2006) Circ. Res. , vol.98 , pp. 7-9
    • Shaw, J.1    Kirshenbaum, L.A.2
  • 94
    • 77952257945 scopus 로고    scopus 로고
    • Patterns of basal signaling heterogeneity can distinguish cellular populations with different drug sensitivities
    • CrossRef PubMed
    • Singh, D.K., Ku, C.-J., Wichaidit, C., Steininger, R.J., Wu, L.F. and Altschuler, S.J. (2010) Patterns of basal signaling heterogeneity can distinguish cellular populations with different drug sensitivities. Mol. Syst. Biol. 6, 369 CrossRef PubMed
    • (2010) Mol. Syst. Biol. , vol.6 , pp. 369
    • Singh, D.K.1    Ku, C.-J.2    Wichaidit, C.3    Steininger, R.J.4    Wu, L.F.5    Altschuler, S.J.6
  • 95
    • 84874765320 scopus 로고    scopus 로고
    • Encoding and decoding cellular information through signaling dynamics
    • CrossRef PubMed
    • Purvis, J.E. and Lahav, G. (2013) Encoding and decoding cellular information through signaling dynamics. Cell 152, 945-56 CrossRef PubMed
    • (2013) Cell , vol.152 , pp. 945-956
    • Purvis, J.E.1    Lahav, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.