메뉴 건너뛰기




Volumn 9, Issue 10, 2007, Pages 1199-1207

Akt phosphorylation regulates the tumour-suppressor merlin through ubiquitination and degradation

Author keywords

[No Author keywords available]

Indexed keywords

MERLIN; PROTEIN KINASE B; PROTEIN P70;

EID: 34848921532     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb1641     Document Type: Article
Times cited : (73)

References (28)
  • 1
    • 0033485979 scopus 로고    scopus 로고
    • Neurofibromatosis 2 tumor suppressor protein, merlin, forms two functionally important intramolecular associations
    • Gutmann, D. H., Haipek, C. A. & Hoang Lu, K. Neurofibromatosis 2 tumor suppressor protein, merlin, forms two functionally important intramolecular associations. J. Neurosci. Res. 58, 706-716 (1999).
    • (1999) J. Neurosci. Res , vol.58 , pp. 706-716
    • Gutmann, D.H.1    Haipek, C.A.2    Hoang Lu, K.3
  • 2
    • 0033607687 scopus 로고    scopus 로고
    • Interdomain interaction of merlin isoforms and its influence on intermolecular binding to NHE-RF
    • Gonzalez-Agosti, C., Wiederhold, T., Herndon, M. E., Gusella, J. & Ramesh, V. Interdomain interaction of merlin isoforms and its influence on intermolecular binding to NHE-RF. J. Biol. Chem. 274, 34438-34442 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 34438-34442
    • Gonzalez-Agosti, C.1    Wiederhold, T.2    Herndon, M.E.3    Gusella, J.4    Ramesh, V.5
  • 3
    • 0034670030 scopus 로고    scopus 로고
    • Interaction between two isoforms of the NF2 tumor suppressor protein, merlin, and between marlin and ezrin, suggests modulation of ERM proteins by merlin
    • Meng, J. J. et al. Interaction between two isoforms of the NF2 tumor suppressor protein, merlin, and between marlin and ezrin, suggests modulation of ERM proteins by merlin. J. Neurosci. Res. 62, 491-502 (2000).
    • (2000) J. Neurosci. Res , vol.62 , pp. 491-502
    • Meng, J.J.1
  • 4
    • 0037155916 scopus 로고    scopus 로고
    • Merlin phosphorylation by p21-activated kinase 2 and effects of phosphorylation on merlin localization
    • Kissil, J. L., Johnson, K. C., Eckman, M. S. & Jacks, T. Merlin phosphorylation by p21-activated kinase 2 and effects of phosphorylation on merlin localization. J. Biol. Chem. 277, 10394-10399 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 10394-10399
    • Kissil, J.L.1    Johnson, K.C.2    Eckman, M.S.3    Jacks, T.4
  • 5
    • 0037059807 scopus 로고    scopus 로고
    • p21-activated kinase links Rac/Cdc42 signaling to merlin
    • Xiao, G. H., Beeser, A., Chernoff, J. & Testa, J. R. p21-activated kinase links Rac/Cdc42 signaling to merlin. J. Biol. Chem. 277 883-886 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 883-886
    • Xiao, G.H.1    Beeser, A.2    Chernoff, J.3    Testa, J.R.4
  • 6
    • 0035871299 scopus 로고    scopus 로고
    • The NF2 tumor suppressor gene product, merlin, mediates contact inhibition of growth through interactions with CD44
    • Morrison, H. et al. The NF2 tumor suppressor gene product, merlin, mediates contact inhibition of growth through interactions with CD44. Genes Dev. 15, 968-980 (2001).
    • (2001) Genes Dev , vol.15 , pp. 968-980
    • Morrison, H.1
  • 7
    • 9144234897 scopus 로고    scopus 로고
    • Serine 518 phosphorylation modulates marlin intramolecular association and binding to critical effectors important for NF2 growth suppression
    • Rong, R., Surace, E. I., Haipek, C. A., Gutmann, D. H. & Ye, K. Serine 518 phosphorylation modulates marlin intramolecular association and binding to critical effectors important for NF2 growth suppression. Oncogene 23, 8447-8454 (2004).
    • (2004) Oncogene , vol.23 , pp. 8447-8454
    • Rong, R.1    Surace, E.I.2    Haipek, C.A.3    Gutmann, D.H.4    Ye, K.5
  • 8
    • 0032571272 scopus 로고    scopus 로고
    • Regulation of the neurofibromatosis type 2 tumor suppressor protein, merlin, by adhesion and growth arrest stimuli
    • Shaw, R. J., McClatchey, A. I. & Jacks, T. Regulation of the neurofibromatosis type 2 tumor suppressor protein, merlin, by adhesion and growth arrest stimuli. J. Biol. Chem. 273, 7757-7764 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 7757-7764
    • Shaw, R.J.1    McClatchey, A.I.2    Jacks, T.3
  • 9
    • 33746722720 scopus 로고    scopus 로고
    • Tumorigenic transformation by CPI-17 through inhibition at a merlin phosphatase
    • Jin, H., Sperka, T., Herrlich, P. & Morrison, H. Tumorigenic transformation by CPI-17 through inhibition at a merlin phosphatase. Nature 442, 576-579 (2006).
    • (2006) Nature , vol.442 , pp. 576-579
    • Jin, H.1    Sperka, T.2    Herrlich, P.3    Morrison, H.4
  • 10
    • 27144446343 scopus 로고    scopus 로고
    • Akt phosphorylates acinus and inhibits its proteolytic cleavage, preventing chromatin condensation
    • Hu, Y. et al. Akt phosphorylates acinus and inhibits its proteolytic cleavage, preventing chromatin condensation. EMBO J. 24, 3543-3554 (2005).
    • (2005) EMBO J , vol.24 , pp. 3543-3554
    • Hu, Y.1
  • 11
    • 13844312400 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Akt/PKB 'by the rictor-mTOR complex
    • Sarbassov, D. D., Guertin, D. A., Ali, S. M. & Sabatini, D. M. Phosphorylation and regulation of Akt/PKB 'by the rictor-mTOR complex. Science 307, 1098-1101 (2005).
    • (2005) Science , vol.307 , pp. 1098-1101
    • Sarbassov, D.D.1    Guertin, D.A.2    Ali, S.M.3    Sabatini, D.M.4
  • 12
    • 33646023695 scopus 로고    scopus 로고
    • Prolonged rapamycin treatment inhibits mTORC2 assembly and Akt/PKB
    • Sarbassav, D. D. et al. Prolonged rapamycin treatment inhibits mTORC2 assembly and Akt/PKB. Mol. Cell 22, 159-168 (2006).
    • (2006) Mol. Cell , vol.22 , pp. 159-168
    • Sarbassav, D.D.1
  • 13
    • 33748950810 scopus 로고    scopus 로고
    • Multiallelic disruption of the rictor gene in mice reveals that mTOR complex 2 is essential for fetal growth and viability
    • Shiota, C., Woo, J. T., Lindner, J., Shelton, K. D. & Magnuson, M. A. Multiallelic disruption of the rictor gene in mice reveals that mTOR complex 2 is essential for fetal growth and viability Dev. Cell 11, 583-589 (2006).
    • (2006) Dev. Cell , vol.11 , pp. 583-589
    • Shiota, C.1    Woo, J.T.2    Lindner, J.3    Shelton, K.D.4    Magnuson, M.A.5
  • 14
    • 33751348056 scopus 로고    scopus 로고
    • Ablation in mice of the mTORC components raptor, rictor, or mLST8 reveals that mTORC2 is required for signaling to Akt-FOXO and PKCalpha, but not S6K1
    • Guertin, D. A. et al. Ablation in mice of the mTORC components raptor, rictor, or mLST8 reveals that mTORC2 is required for signaling to Akt-FOXO and PKCalpha, but not S6K1. Dev. Cell 11, 859-871 (2006).
    • (2006) Dev. Cell , vol.11 , pp. 859-871
    • Guertin, D.A.1
  • 15
    • 11144229268 scopus 로고    scopus 로고
    • Neurofibromatosis 2 (NF2) tumor suppressor merlin inhibits phosphatidylinositol 3-kinase through binding to PIKE.-L
    • Rong, R., Tang, X., Gutmann, D. H. & Ye, K. Neurofibromatosis 2 (NF2) tumor suppressor merlin inhibits phosphatidylinositol 3-kinase through binding to PIKE.-L. Proc. Natl Acad. Sci. USA 101, 18200-18205 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 18200-18205
    • Rong, R.1    Tang, X.2    Gutmann, D.H.3    Ye, K.4
  • 16
    • 0034724536 scopus 로고    scopus 로고
    • Structure of the ERM protein moesin reveals the FEBM domain fold masked by an extended artin binding-tail domain
    • Pearson, M. A., Reczek, D., Bretscher, A. & Karplus, P. A. Structure of the ERM protein moesin reveals the FEBM domain fold masked by an extended artin binding-tail domain. Cell 101, 259-270 (2000).
    • (2000) Cell , vol.101 , pp. 259-270
    • Pearson, M.A.1    Reczek, D.2    Bretscher, A.3    Karplus, P.A.4
  • 17
    • 10744229026 scopus 로고    scopus 로고
    • Merlin neutralizes the inhibitory effect of Mdm2 on p53
    • Kim, H. et al. Merlin neutralizes the inhibitory effect of Mdm2 on p53. J. Biol. Chem. 279, 7812-7818 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 7812-7818
    • Kim, H.1
  • 18
    • 33644527303 scopus 로고    scopus 로고
    • Merlin facilitates ubiquitination and degradation of transactivation-responsive RNA-binding protein
    • Lee, J. Y. et al. Merlin facilitates ubiquitination and degradation of transactivation-responsive RNA-binding protein. Oncogene 25, 1143-1152 (2006).
    • (2006) Oncogene , vol.25 , pp. 1143-1152
    • Lee, J.Y.1
  • 19
    • 0035736487 scopus 로고    scopus 로고
    • HER-2/neu induces p53 ubiquitination via Akt-mediated MDM2 phosphorylation
    • Zhou, B. P. et al. HER-2/neu induces p53 ubiquitination via Akt-mediated MDM2 phosphorylation. Nature Cell Biol. 3, 973-982 (2001).
    • (2001) Nature Cell Biol , vol.3 , pp. 973-982
    • Zhou, B.P.1
  • 20
    • 0036849331 scopus 로고    scopus 로고
    • PKB binding proteins. Getting in on the Akt
    • Brazil, D. P., Park, J. & Hemmings, B. A. PKB binding proteins. Getting in on the Akt. Cell 111, 293-303 (2002).
    • (2002) Cell , vol.111 , pp. 293-303
    • Brazil, D.P.1    Park, J.2    Hemmings, B.A.3
  • 21
    • 0037199912 scopus 로고    scopus 로고
    • Mutant products of the NF2 tumor suppressor gene are degraded by the ubiquitin-proteasome pathway
    • Gautreau, A. et al. Mutant products of the NF2 tumor suppressor gene are degraded by the ubiquitin-proteasome pathway. J. Biol. Chem. 277, 31279-31282 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 31279-31282
    • Gautreau, A.1
  • 22
    • 2442629479 scopus 로고    scopus 로고
    • Cyclic AMP-dependent protein kinase phosphorylates Merlin at serine 518 independently of P21-activated kinase and promotes Merlin-Ezrin heterodimerization
    • Alfthan, K., Heiska, L., Gronholm, M., Renkema, G. H. & Carpen, O. Cyclic AMP-dependent protein kinase phosphorylates Merlin at serine 518 independently of P21-activated kinase and promotes Merlin-Ezrin heterodimerization. J. Biol. Chem. (2004).
    • (2004) J. Biol. Chem
    • Alfthan, K.1    Heiska, L.2    Gronholm, M.3    Renkema, G.H.4    Carpen, O.5
  • 23
    • 0031896691 scopus 로고    scopus 로고
    • Neurofibromatosis 2 tumour suppressor schwannomin interacts with betall-spectrin
    • Scoles, D. R. et al. Neurofibromatosis 2 tumour suppressor schwannomin interacts with betall-spectrin. Nature Genet. 18 354-359 (1998).
    • (1998) Nature Genet , vol.18 , pp. 354-359
    • Scoles, D.R.1
  • 24
    • 0035884301 scopus 로고    scopus 로고
    • Binding of the merlin-I product of the neurofibromatosis type 2 tumour suppressor gene to a novel site in beta-fodrin is regulated by association between merlin domains
    • Neill, G.W. & Crompton, M. R. Binding of the merlin-I product of the neurofibromatosis type 2 tumour suppressor gene to a novel site in beta-fodrin is regulated by association between merlin domains. Biochem. J. 358, 727-735 (2001).
    • (2001) Biochem. J , vol.358 , pp. 727-735
    • Neill, G.W.1    Crompton, M.R.2
  • 25
    • 0034808728 scopus 로고    scopus 로고
    • A novel isoform of beta-spectrin II localizes to cerebellar Purkinje-cell bodies and interacts with neurofibromatosis type 2 gene product schwannomin
    • Chen, Y., Yu, P., Lu, D., Tagle, D. A. & Cai, T. A novel isoform of beta-spectrin II localizes to cerebellar Purkinje-cell bodies and interacts with neurofibromatosis type 2 gene product schwannomin. J. Mol. Neurosci. 17, 59-70 (2001).
    • (2001) J. Mol. Neurosci , vol.17 , pp. 59-70
    • Chen, Y.1    Yu, P.2    Lu, D.3    Tagle, D.A.4    Cai, T.5
  • 26
    • 0035949431 scopus 로고    scopus 로고
    • Erythrocyte spectrin is an E2 ubiquitin conjugating enzyme
    • Kakhniashvili, D. G. et al. Erythrocyte spectrin is an E2 ubiquitin conjugating enzyme. Biochemistry 40, 11630-11642 (2001).
    • (2001) Biochemistry , vol.40 , pp. 11630-11642
    • Kakhniashvili, D.G.1
  • 27
    • 0037443055 scopus 로고    scopus 로고
    • Dynamic regulation of the Ras pathway via proteolysis of the NF1 tumor suppressor
    • Cichowski, K., Santiago, S., Jardim, M., Johnson, B. W. & Jacks, T. Dynamic regulation of the Ras pathway via proteolysis of the NF1 tumor suppressor. Genes Dev. 17, 449-454 (2003).
    • (2003) Genes Dev , vol.17 , pp. 449-454
    • Cichowski, K.1    Santiago, S.2    Jardim, M.3    Johnson, B.W.4    Jacks, T.5
  • 28
    • 33646759590 scopus 로고    scopus 로고
    • Nuclear Akt associates with PKC-phosphorylated Ebp1, preventing DNA fragmentation by inhibition of caspase-activated DNase
    • Ahn, J. Y. et al. Nuclear Akt associates with PKC-phosphorylated Ebp1, preventing DNA fragmentation by inhibition of caspase-activated DNase. EMBO J. 25, 2083-2095 (2006).
    • (2006) EMBO J , vol.25 , pp. 2083-2095
    • Ahn, J.Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.