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Volumn 42, Issue 5, 2014, Pages 1435-1440

Acute regulation of PDK1 by a complex interplay of molecular switches

Author keywords

Activation dynamics; Homodimerization; Phosphoinositide dependent kinase 1 (pdk1); Phosphorylation; Subcellular localization

Indexed keywords

HOMODIMER; PHOSPHOINOSITIDE DEPENDENT PROTEIN KINASE 1; 3 PHOSPHOINOSITIDE DEPENDENT PROTEIN KINASE; LIGAND; PDPK1 PROTEIN, HUMAN; SERINE; THREONINE; TUMOR PROTEIN; TYROSINE;

EID: 84907195505     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20140222     Document Type: Review
Times cited : (26)

References (44)
  • 1
    • 1342342993 scopus 로고    scopus 로고
    • PDK1, the master regulator of AGC kinase signal transduction
    • CrossRef PubMed
    • Mora, A., Komander, D., van Aalten, D.M. and Alessi, D.R. (2004) PDK1, the master regulator of AGC kinase signal transduction. Semin. Cell Dev. Biol. 15, 161-170 CrossRef PubMed
    • (2004) Semin. Cell Dev. Biol. , vol.15 , pp. 161-170
    • Mora, A.1    Komander, D.2    Van Aalten, D.M.3    Alessi, D.R.4
  • 3
    • 0032482374 scopus 로고    scopus 로고
    • Translocation of PDK-1 to the plasma membrane is important in allowing PDK-1 to activate protein kinase B
    • CrossRef PubMed
    • Anderson, K.E., Coadwell, J., Stephens, L.R. and Hawkins, P.T. (1998) Translocation of PDK-1 to the plasma membrane is important in allowing PDK-1 to activate protein kinase B. Curr. Biol. 8, 684-691 CrossRef PubMed
    • (1998) Curr. Biol. , vol.8 , pp. 684-691
    • Anderson, K.E.1    Coadwell, J.2    Stephens, L.R.3    Hawkins, P.T.4
  • 4
    • 0033912843 scopus 로고    scopus 로고
    • Effect of phosphoinositide-dependent kinase 1 on protein kinase B translocation and its subsequent activation
    • CrossRef PubMed
    • Filippa, N., Sable, C.L., Hemmings, B.A. and Van Obberghen, E. (2000) Effect of phosphoinositide-dependent kinase 1 on protein kinase B translocation and its subsequent activation. Mol. Cell. Biol. 20, 5712-5721 CrossRef PubMed
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5712-5721
    • Filippa, N.1    Sable, C.L.2    Hemmings, B.A.3    Van Obberghen, E.4
  • 6
    • 0042967831 scopus 로고    scopus 로고
    • In vivo role of the PIF-binding docking site of PDK1 defined by knock-in mutation
    • CrossRef PubMed
    • Collins, B.J., Deak, M., Arthur, J.S., Armit, L.J. and Alessi, D.R. (2003) In vivo role of the PIF-binding docking site of PDK1 defined by knock-in mutation. EMBO J. 22, 4202-4211 CrossRef PubMed
    • (2003) EMBO J. , vol.22 , pp. 4202-4211
    • Collins, B.J.1    Deak, M.2    Arthur, J.S.3    Armit, L.J.4    Alessi, D.R.5
  • 7
    • 84055188488 scopus 로고    scopus 로고
    • Multiple implications of 3-phosphoinositide-dependent protein kinase 1 in human cancer
    • CrossRef PubMed
    • Li, Y., Yang, K.J. and Park, J. (2010) Multiple implications of 3-phosphoinositide-dependent protein kinase 1 in human cancer. World J. Biol. Chem. 1, 239-247 CrossRef PubMed
    • (2010) World J. Biol. Chem. , vol.1 , pp. 239-247
    • Li, Y.1    Yang, K.J.2    Park, J.3
  • 8
    • 78651284004 scopus 로고    scopus 로고
    • Characterization of GSK2334470, a novel and highly specific inhibitor of PDK1
    • CrossRef PubMed
    • Najafov, A., Sommer, E.M., Axten, J.M., Deyoung, M.P. and Alessi, D.R. (2011) Characterization of GSK2334470, a novel and highly specific inhibitor of PDK1. Biochem. J. 433, 357-369 CrossRef PubMed
    • (2011) Biochem. J. , vol.433 , pp. 357-369
    • Najafov, A.1    Sommer, E.M.2    Axten, J.M.3    Deyoung, M.P.4    Alessi, D.R.5
  • 9
    • 57549101230 scopus 로고    scopus 로고
    • Small-molecule inhibitors of PDK1
    • CrossRef PubMed
    • Peifer, C. and Alessi, D.R. (2008) Small-molecule inhibitors of PDK1. ChemMedChem 3, 1810-1838 CrossRef PubMed
    • (2008) ChemMedChem , vol.3 , pp. 1810-1838
    • Peifer, C.1    Alessi, D.R.2
  • 10
    • 84878819558 scopus 로고    scopus 로고
    • AGC protein kinases: From structural mechanism of regulation to allosteric drug development for the treatment of human diseases
    • CrossRef PubMed
    • Arencibia, J.M., Pastor-Flores, D., Bauer, A.F., Schulze, J.O. and Biondi, R.M. (2013) AGC protein kinases: from structural mechanism of regulation to allosteric drug development for the treatment of human diseases. Biochim. Biophys. Acta 1834, 1302-1321 CrossRef PubMed
    • (2013) Biochim. Biophys. Acta , vol.1834 , pp. 1302-1321
    • Arencibia, J.M.1    Pastor-Flores, D.2    Bauer, A.F.3    Schulze, J.O.4    Biondi, R.M.5
  • 11
    • 79959365543 scopus 로고    scopus 로고
    • Targeting PDK1 in cancer
    • CrossRef PubMed
    • Raimondi, C. and Falasca, M. (2011) Targeting PDK1 in cancer. Curr. Med. Chem. 18, 2763-2769 CrossRef PubMed
    • (2011) Curr. Med. Chem. , vol.18 , pp. 2763-2769
    • Raimondi, C.1    Falasca, M.2
  • 13
    • 0035797892 scopus 로고    scopus 로고
    • Insulin stimulates increased catalytic activity of phosphoinositide-dependent kinase-1 by a phosphorylation-dependent mechanism
    • CrossRef PubMed
    • Chen, H., Nystrom, F.H., Dong, L.Q., Li, Y., Song, S., Liu, F. and Quon, M.J. (2001) Insulin stimulates increased catalytic activity of phosphoinositide-dependent kinase-1 by a phosphorylation-dependent mechanism. Biochemistry 40, 11851-11859 CrossRef PubMed
    • (2001) Biochemistry , vol.40 , pp. 11851-11859
    • Chen, H.1    Nystrom, F.H.2    Dong, L.Q.3    Li, Y.4    Song, S.5    Liu, F.6    Quon, M.J.7
  • 14
    • 0037053364 scopus 로고    scopus 로고
    • 516with a negatively charged residue confers constitutive activity to mouse 3-phosphoinositide-dependent protein kinase-1 in cells
    • CrossRef PubMed
    • 516with a negatively charged residue confers constitutive activity to mouse 3-phosphoinositide-dependent protein kinase-1 in cells. J. Biol. Chem. 277, 16632-16638 CrossRef PubMed
    • (2002) J. Biol. Chem. , vol.277 , pp. 16632-16638
    • Wick, M.J.1    Wick, K.R.2    Chen, H.3    He, H.4    Dong, L.Q.5    Quon, M.J.6    Liu, F.7
  • 15
    • 80052275615 scopus 로고    scopus 로고
    • PI3K/Akt signaling requires spatial compartmentalization in plasma membrane microdomains
    • CrossRef PubMed
    • Gao, X., Lowry, P.R., Zhou, X., Depry, C., Wei, Z., Wong, G.W. and Zhang, J. (2011) PI3K/Akt signaling requires spatial compartmentalization in plasma membrane microdomains. Proc. Natl. Acad. Sci. U.S.A. 108, 14509-14514 CrossRef PubMed
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 14509-14514
    • Gao, X.1    Lowry, P.R.2    Zhou, X.3    Depry, C.4    Wei, Z.5    Wong, G.W.6    Zhang, J.7
  • 16
    • 0344270855 scopus 로고    scopus 로고
    • Nuclear translocation of 3′-phosphoinositide-dependent protein kinase 1 (PDK-1): A potential regulatory mechanism for PDK-1 function
    • CrossRef PubMed
    • Lim, M.A., Kikani, C.K., Wick, M.J. and Dong, L.Q. (2003) Nuclear translocation of 3′-phosphoinositide-dependent protein kinase 1 (PDK-1): a potential regulatory mechanism for PDK-1 function. Proc. Natl. Acad. Sci. U.S.A. 100, 14006-14011 CrossRef PubMed
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 14006-14011
    • Lim, M.A.1    Kikani, C.K.2    Wick, M.J.3    Dong, L.Q.4
  • 17
    • 0242384929 scopus 로고    scopus 로고
    • Mouse 3-phosphoinositide-dependent protein kinase-1 undergoes dimerization and trans-phosphorylation in the activation loop
    • CrossRef PubMed
    • Wick, M.J., Ramos, F.J., Chen, H., Quon, M.J., Dong, L.Q. and Liu, F. (2003) Mouse 3-phosphoinositide-dependent protein kinase-1 undergoes dimerization and trans-phosphorylation in the activation loop. J. Biol. Chem. 278, 42913-42919 CrossRef PubMed
    • (2003) J. Biol. Chem. , vol.278 , pp. 42913-42919
    • Wick, M.J.1    Ramos, F.J.2    Chen, H.3    Quon, M.J.4    Dong, L.Q.5    Liu, F.6
  • 19
    • 84876785084 scopus 로고    scopus 로고
    • Transition from heterotypic to homotypic PDK1 homodimerization is essential for TCR-mediated NF-κ B activation
    • CrossRef PubMed
    • Kang, J.A., Jeong, S.P., Park, D., Hayden, M.S., Ghosh, S. and Park, S.G. (2013) Transition from heterotypic to homotypic PDK1 homodimerization is essential for TCR-mediated NF-κ B activation. J. Immunol. 190, 4508-4515 CrossRef PubMed
    • (2013) J. Immunol. , vol.190 , pp. 4508-4515
    • Kang, J.A.1    Jeong, S.P.2    Park, D.3    Hayden, M.S.4    Ghosh, S.5    Park, S.G.6
  • 20
    • 0033199841 scopus 로고    scopus 로고
    • Phosphorylation of Ser-241 is essential for the activity of 3-phosphoinositide-dependent protein kinase-1: Identification of five sites of phosphorylation in vivo
    • CrossRef PubMed
    • Casamayor, A., Morrice, N.A. and Alessi, D.R. (1999) Phosphorylation of Ser-241 is essential for the activity of 3-phosphoinositide-dependent protein kinase-1: identification of five sites of phosphorylation in vivo. Biochem. J. 342, 287-292 CrossRef PubMed
    • (1999) Biochem. J. , vol.342 , pp. 287-292
    • Casamayor, A.1    Morrice, N.A.2    Alessi, D.R.3
  • 21
    • 0035813230 scopus 로고    scopus 로고
    • Identification of tyrosine phosphorylation sites on 3-phosphoinositide-dependent protein kinase-1 and their role in regulating kinase activity
    • CrossRef PubMed
    • Park, J., Hill, M.M., Hess, D., Brazil, D.P., Hofsteenge, J. and Hemmings, B.A. (2001) Identification of tyrosine phosphorylation sites on 3-phosphoinositide-dependent protein kinase-1 and their role in regulating kinase activity. J. Biol. Chem. 276, 37459-37471 CrossRef PubMed
    • (2001) J. Biol. Chem. , vol.276 , pp. 37459-37471
    • Park, J.1    Hill, M.M.2    Hess, D.3    Brazil, D.P.4    Hofsteenge, J.5    Hemmings, B.A.6
  • 22
    • 33745759303 scopus 로고    scopus 로고
    • Role of the PH domain in regulating in vitro autophosphorylation events required for reconstitution of PDK1 catalytic activity
    • CrossRef PubMed
    • Gao, X. and Harris, T.K. (2006) Role of the PH domain in regulating in vitro autophosphorylation events required for reconstitution of PDK1 catalytic activity. Bioorg. Chem. 34, 200-223 CrossRef PubMed
    • (2006) Bioorg. Chem. , vol.34 , pp. 200-223
    • Gao, X.1    Harris, T.K.2
  • 25
    • 77449129447 scopus 로고    scopus 로고
    • Reciprocal negative regulation of PDK1 and ASK1 signaling by direct interaction and phosphorylation
    • CrossRef PubMed
    • Seong, H.A., Jung, H., Ichijo, H. and Ha, H. (2010) Reciprocal negative regulation of PDK1 and ASK1 signaling by direct interaction and phosphorylation. J. Biol. Chem. 285, 2397-2414 CrossRef PubMed
    • (2010) J. Biol. Chem. , vol.285 , pp. 2397-2414
    • Seong, H.A.1    Jung, H.2    Ichijo, H.3    Ha, H.4
  • 26
    • 84862294248 scopus 로고    scopus 로고
    • 354by murine protein serine-threonine kinase 38 contributes to negative regulation of PDK1 protein activity
    • CrossRef PubMed
    • 354by murine protein serine-threonine kinase 38 contributes to negative regulation of PDK1 protein activity. J. Biol. Chem. 287, 20811-20822 CrossRef PubMed
    • (2012) J. Biol. Chem. , vol.287 , pp. 20811-20822
    • Seong, H.A.1    Jung, H.2    Manoharan, R.3    Ha, H.4
  • 27
    • 12444299997 scopus 로고    scopus 로고
    • RET/PTC (rearranged in transformation/papillary thyroid carcinomas) tyrosine kinase phosphorylates and activates phosphoinositide-dependent kinase 1 (PDK1): An alternative phosphatidylinositol 3-kinase-independent pathway to activate PDK1
    • CrossRef PubMed
    • Kim, D.W., Hwang, J.H., Suh, J.M., Kim, H., Song, J.H., Hwang, E.S., Hwang, I.Y., Park, K.C., Chung, H.K., Kim, J.M. et al. (2003) RET/PTC (rearranged in transformation/papillary thyroid carcinomas) tyrosine kinase phosphorylates and activates phosphoinositide-dependent kinase 1 (PDK1): an alternative phosphatidylinositol 3-kinase-independent pathway to activate PDK1. Mol. Endocrinol. 17, 1382-1394 CrossRef PubMed
    • (2003) Mol. Endocrinol. , vol.17 , pp. 1382-1394
    • Kim, D.W.1    Hwang, J.H.2    Suh, J.M.3    Kim, H.4    Song, J.H.5    Hwang, E.S.6    Hwang, I.Y.7    Park, K.C.8    Chung, H.K.9    Kim, J.M.10
  • 28
    • 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
  • 29
    • 0034161251 scopus 로고    scopus 로고
    • Identification of a pocket in the PDK1 kinase domain that interacts with PIF and the C-terminal residues of PKA
    • CrossRef PubMed
    • Biondi, R.M., Cheung, P.C., Casamayor, A., Deak, M., Currie, R.A. and Alessi, D.R. (2000) Identification of a pocket in the PDK1 kinase domain that interacts with PIF and the C-terminal residues of PKA. EMBO J. 19, 979-988 CrossRef PubMed
    • (2000) EMBO J. , vol.19 , pp. 979-988
    • Biondi, R.M.1    Cheung, P.C.2    Casamayor, A.3    Deak, M.4    Currie, R.A.5    Alessi, D.R.6
  • 30
    • 38349168971 scopus 로고    scopus 로고
    • Regulation of 3-phosphoinositide-dependent protein kinase-1 (PDK1) by Src involves tyrosine phosphorylation of PDK1 and Src homology 2 domain binding
    • CrossRef PubMed
    • Yang, K.J., Shin, S., Piao, L., Shin, E., Li, Y., Park, K.A., Byun, H.S., Won, M., Hong, J., Kweon, G.R. et al. (2008) Regulation of 3-phosphoinositide-dependent protein kinase-1 (PDK1) by Src involves tyrosine phosphorylation of PDK1 and Src homology 2 domain binding. J. Biol. Chem. 283, 1480-1491 CrossRef PubMed
    • (2008) J. Biol. Chem. , vol.283 , pp. 1480-1491
    • Yang, K.J.1    Shin, S.2    Piao, L.3    Shin, E.4    Li, Y.5    Park, K.A.6    Byun, H.S.7    Won, M.8    Hong, J.9    Kweon, G.R.10
  • 31
    • 0037131334 scopus 로고    scopus 로고
    • Regulation of kinase activity of 3-phosphoinositide-dependent protein kinase-1 by binding to 14-3-3
    • CrossRef PubMed
    • Sato, S., Fujita, N. and Tsuruo, T. (2002) Regulation of kinase activity of 3-phosphoinositide-dependent protein kinase-1 by binding to 14-3-3. J. Biol. Chem. 277, 39360-39367 CrossRef PubMed
    • (2002) J. Biol. Chem. , vol.277 , pp. 39360-39367
    • Sato, S.1    Fujita, N.2    Tsuruo, T.3
  • 32
    • 0026664393 scopus 로고
    • High constitutive expression of heat shock protein 90á in human acute leukemia cells
    • CrossRef PubMed
    • Yufu, Y., Nishimura, J. and Nawata, H. (1992) High constitutive expression of heat shock protein 90á in human acute leukemia cells. Leuk. Res. 16, 597-605 CrossRef PubMed
    • (1992) Leuk. Res. , vol.16 , pp. 597-605
    • Yufu, Y.1    Nishimura, J.2    Nawata, H.3
  • 33
    • 0037155901 scopus 로고    scopus 로고
    • Involvement of Hsp90 in signaling and stability of 3-phosphoinositide-dependent kinase-1
    • CrossRef PubMed
    • Fujita, N., Sato, S., Ishida, A. and Tsuruo, T. (2002) Involvement of Hsp90 in signaling and stability of 3-phosphoinositide-dependent kinase-1. J. Biol. Chem. 277, 10346-10353 CrossRef PubMed
    • (2002) J. Biol. Chem. , vol.277 , pp. 10346-10353
    • Fujita, N.1    Sato, S.2    Ishida, A.3    Tsuruo, T.4
  • 34
    • 30044434463 scopus 로고    scopus 로고
    • Regulation of transforming growth factor-beta signaling and PDK1 kinase activity by physical interaction between PDK1 and serine-threonine kinase receptor-associated protein
    • CrossRef PubMed
    • Seong, H.A., Jung, H., Choi, H.S., Kim, K.T. and Ha, H. (2005) Regulation of transforming growth factor-beta signaling and PDK1 kinase activity by physical interaction between PDK1 and serine-threonine kinase receptor-associated protein. J. Biol. Chem. 280, 42897-42908 CrossRef PubMed
    • (2005) J. Biol. Chem. , vol.280 , pp. 42897-42908
    • Seong, H.A.1    Jung, H.2    Choi, H.S.3    Kim, K.T.4    Ha, H.5
  • 36
    • 50149086076 scopus 로고    scopus 로고
    • TUSC4/NPRL2, a novel PDK1-interacting protein, inhibits PDK1 tyrosine phosphorylation and its downstream signaling
    • PubMed
    • Kurata, A., Katayama, R., Watanabe, T., Tsuruo, T. and Fujita, N. (2008) TUSC4/NPRL2, a novel PDK1-interacting protein, inhibits PDK1 tyrosine phosphorylation and its downstream signaling. Cancer Sci. 99, 1827-1834 PubMed
    • (2008) Cancer Sci. , vol.99 , pp. 1827-1834
    • Kurata, A.1    Katayama, R.2    Watanabe, T.3    Tsuruo, T.4    Fujita, N.5
  • 37
    • 4444229881 scopus 로고    scopus 로고
    • The adaptor protein Grb14 regulates the localization of 3-phosphoinositide-dependent kinase-1
    • CrossRef PubMed
    • King, C.C. and Newton, A.C. (2004) The adaptor protein Grb14 regulates the localization of 3-phosphoinositide-dependent kinase-1. J. Biol. Chem. 279, 37518-37527 CrossRef PubMed
    • (2004) J. Biol. Chem. , vol.279 , pp. 37518-37527
    • King, C.C.1    Newton, A.C.2
  • 38
    • 57349145336 scopus 로고    scopus 로고
    • Spatiotemporal analysis of differential Akt regulation in plasma membrane microdomains
    • CrossRef PubMed
    • Gao, X. and Zhang, J. (2008) Spatiotemporal analysis of differential Akt regulation in plasma membrane microdomains. Mol. Biol. Cell 19, 4366-4373 CrossRef PubMed
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4366-4373
    • Gao, X.1    Zhang, J.2
  • 40
    • 84868623830 scopus 로고    scopus 로고
    • Proliferative and antiapoptotic signaling stimulated by nuclear-localized PDK1 results in oncogenesis
    • CrossRef PubMed
    • Kikani, C.K., Verona, E.V., Ryu, J., Shen, Y., Ye, Q., Zheng, L., Qian, Z., Sakaue, H., Nakamura, K., Du, J. et al. (2012) Proliferative and antiapoptotic signaling stimulated by nuclear-localized PDK1 results in oncogenesis. Sci. Signal. 5, ra80 CrossRef PubMed
    • (2012) Sci. Signal. , vol.5 , pp. ra80
    • Kikani, C.K.1    Verona, E.V.2    Ryu, J.3    Shen, Y.4    Ye, Q.5    Zheng, L.6    Qian, Z.7    Sakaue, H.8    Nakamura, K.9    Du, J.10
  • 41
    • 69049117141 scopus 로고    scopus 로고
    • The nuclear localization of 3′-phosphoinositide-dependent kinase-1 is dependent on its association with the protein tyrosine phosphatase SHP-1
    • CrossRef PubMed
    • Sephton, C.F., Zhang, D., Lehmann, T.M., Pennington, P.R., Scheid, M.P. and Mousseau, D.D. (2009) The nuclear localization of 3′-phosphoinositide-dependent kinase-1 is dependent on its association with the protein tyrosine phosphatase SHP-1. Cell Signal. 21, 1634-1644 CrossRef PubMed
    • (2009) Cell Signal. , vol.21 , pp. 1634-1644
    • Sephton, C.F.1    Zhang, D.2    Lehmann, T.M.3    Pennington, P.R.4    Scheid, M.P.5    Mousseau, D.D.6
  • 42
    • 14844357714 scopus 로고    scopus 로고
    • Phosphoinositide-dependent phosphorylation of PDK1 regulates nuclear translocation
    • CrossRef PubMed
    • Scheid, M.P., Parsons, M. and Woodgett, J.R. (2005) Phosphoinositide-dependent phosphorylation of PDK1 regulates nuclear translocation. Mol. Cell. Biol. 25, 2347-2363 CrossRef PubMed
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 2347-2363
    • Scheid, M.P.1    Parsons, M.2    Woodgett, J.R.3
  • 43
    • 84880534471 scopus 로고    scopus 로고
    • The PH domain of phosphoinositide-dependent kinase-1 exhibits a novel, phospho-regulated monomer-dimer equilibrium with important implications for kinase domain activation: Single-molecule and ensemble studies
    • CrossRef PubMed
    • Ziemba, B.P., Pilling, C., Calleja, V., Larijani, B. and Falke, J.J. (2013) The PH domain of phosphoinositide-dependent kinase-1 exhibits a novel, phospho-regulated monomer-dimer equilibrium with important implications for kinase domain activation: single-molecule and ensemble studies. Biochemistry 52, 4820-4829 CrossRef PubMed
    • (2013) Biochemistry , vol.52 , pp. 4820-4829
    • Ziemba, B.P.1    Pilling, C.2    Calleja, V.3    Larijani, B.4    Falke, J.J.5
  • 44
    • 84886094611 scopus 로고    scopus 로고
    • Characterization of fragmented 3-phosphoinsitide-dependent protein kinase-1 (PDK1) by phosphosite-specific antibodies
    • CrossRef PubMed
    • Park, J., Li, Y., Kim, S.H., Kong, G., Shrestha, R., Tran, Q., Hong, J., Hur, G.M., Hemmings, B.A., Koo, B.S. and Park, J. (2013) Characterization of fragmented 3-phosphoinsitide-dependent protein kinase-1 (PDK1) by phosphosite-specific antibodies. Life Sci. 93, 700-706 CrossRef PubMed
    • (2013) Life Sci. , vol.93 , pp. 700-706
    • Park, J.1    Li, Y.2    Kim, S.H.3    Kong, G.4    Shrestha, R.5    Tran, Q.6    Hong, J.7    Hur, G.M.8    Hemmings, B.A.9    Koo, B.S.10    Park, J.11


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