메뉴 건너뛰기




Volumn 4, Issue 8, 2009, Pages

The TCL1A oncoprotein interacts directly with the NF-κB inhibitor IκB

Author keywords

[No Author keywords available]

Indexed keywords

ANKYRIN; I KAPPA B; ONCOPROTEIN; PROTEIN KINASE B; RECOMBINANT PROTEIN; T CELL LEUKEMIA LYMPHOMA 1A ONCOPROTEIN; UNCLASSIFIED DRUG; I KAPPA B KINASE; TCL1A PROTEIN, HUMAN;

EID: 68749103462     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0006567     Document Type: Article
Times cited : (13)

References (28)
  • 1
    • 23144442026 scopus 로고    scopus 로고
    • The TCL1 family of oncoproteins: Co-activators of transformation
    • Teitell MA (2005) The TCL1 family of oncoproteins: co-activators of transformation. Nat Rev Cancer 5: 640-648.
    • (2005) Nat Rev Cancer , vol.5 , pp. 640-648
    • Teitell, M.A.1
  • 2
    • 34547795824 scopus 로고    scopus 로고
    • Proto-oncogene TCL1: More than just a coactivator for Akt
    • Noguchi M, Ropars V, Roumestand C, Suizu F (2007) Proto-oncogene TCL1: more than just a coactivator for Akt. Faseb J 21: 2273-2284.
    • (2007) Faseb J , vol.21 , pp. 2273-2284
    • Noguchi, M.1    Ropars, V.2    Roumestand, C.3    Suizu, F.4
  • 3
    • 0033636528 scopus 로고    scopus 로고
    • The protooncogene TCL1 is an Akt kinase coactivator
    • Laine J, Kunstle G, Obata T, Sha M, Noguchi M (2000) The protooncogene TCL1 is an Akt kinase coactivator. Mol Cell 6: 395-407.
    • (2000) Mol Cell , vol.6 , pp. 395-407
    • Laine, J.1    Kunstle, G.2    Obata, T.3    Sha, M.4    Noguchi, M.5
  • 4
  • 5
    • 4143057138 scopus 로고    scopus 로고
    • Structural basis for the co-activation of protein kinase B by T-cell leukemia-1 (TCL1) family proto-oncoproteins
    • Auguin D, Barthe P, Royer C, Stern MH, Noguchi M, et al. (2004) Structural basis for the co-activation of protein kinase B by T-cell leukemia-1 (TCL1) family proto-oncoproteins. J Biol Chem 279: 35890-35902.
    • (2004) J Biol Chem , vol.279 , pp. 35890-35902
    • Auguin, D.1    Barthe, P.2    Royer, C.3    Stern, M.H.4    Noguchi, M.5
  • 6
    • 34250788809 scopus 로고    scopus 로고
    • AKT/PKB signaling: Navigating downstream
    • Manning BD, Cantley LC (2007) AKT/PKB signaling: navigating downstream. Cell 129: 1261-1274.
    • (2007) Cell , vol.129 , pp. 1261-1274
    • Manning, B.D.1    Cantley, L.C.2
  • 7
    • 0033517189 scopus 로고    scopus 로고
    • NF-kappaB activation by tumour necrosis factor requires the Akt serine-threonine kinase
    • Ozes ON, Mayo LD, Gustin JA, Pfeffer SR, Pfeffer LM, et al. (1999) NF-kappaB activation by tumour necrosis factor requires the Akt serine-threonine kinase. Nature 401: 82-85.
    • (1999) Nature , vol.401 , pp. 82-85
    • Ozes, O.N.1    Mayo, L.D.2    Gustin, J.A.3    Pfeffer, S.R.4    Pfeffer, L.M.5
  • 8
    • 38849199203 scopus 로고    scopus 로고
    • Shared principles in NF-kappaB signaling
    • Hayden MS, Ghosh S (2008) Shared principles in NF-kappaB signaling. Cell 132: 344-362.
    • (2008) Cell , vol.132 , pp. 344-362
    • Hayden, M.S.1    Ghosh, S.2
  • 10
    • 58149376457 scopus 로고    scopus 로고
    • Tcl1 functions as a transcriptional regulator and is directly involved in the pathogenesis of CLL
    • Pekarsky Y, Palamarchuk A, Maximov V, Efanov A, Nazaryan N, et al. (2008) Tcl1 functions as a transcriptional regulator and is directly involved in the pathogenesis of CLL. Proc Natl Acad Sci U S A 105: 19643-19648.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 19643-19648
    • Pekarsky, Y.1    Palamarchuk, A.2    Maximov, V.3    Efanov, A.4    Nazaryan, N.5
  • 11
    • 0032217268 scopus 로고    scopus 로고
    • The crystal structure of the IkappaBalpha/NF-kappaB complex reveals mechanisms of NF-kappaB inactivation
    • Huxford T, Huang DB, Malek S, Ghosh G (1998) The crystal structure of the IkappaBalpha/NF-kappaB complex reveals mechanisms of NF-kappaB inactivation. Cell 95: 759-770.
    • (1998) Cell , vol.95 , pp. 759-770
    • Huxford, T.1    Huang, D.B.2    Malek, S.3    Ghosh, G.4
  • 12
    • 0032217264 scopus 로고    scopus 로고
    • Structure of an IkappaBalpha/NF-kappaB complex
    • Jacobs MD, Harrison SC (1998) Structure of an IkappaBalpha/NF-kappaB complex. Cell 95: 749-758.
    • (1998) Cell , vol.95 , pp. 749-758
    • Jacobs, M.D.1    Harrison, S.C.2
  • 13
    • 0345169163 scopus 로고    scopus 로고
    • Small-angle scattering: A view on the properties, structures and structural changes of biological macromolecules in solution
    • Koch MH, Vachette P, Svergun DI (2003) Small-angle scattering: a view on the properties, structures and structural changes of biological macromolecules in solution. Q Rev Biophys 36: 147-227.
    • (2003) Q Rev Biophys , vol.36 , pp. 147-227
    • Koch, M.H.1    Vachette, P.2    Svergun, D.I.3
  • 14
    • 0032519005 scopus 로고    scopus 로고
    • TCL1, an oncogene product involved in T-cell prolymphocytic leukemia, reveals a novel beta-barrel topology
    • TCL1, an oncogene product involved in T-cell prolymphocytic leukemia, reveals a novel beta-barrel topology. Structure 6: 147-155.
    • (1998) Structure , vol.6 , pp. 147-155
    • Hoh, F.1    Yang, Y.S.2    Guignard, L.3    Padilla, A.4    Stern, M.H.5
  • 15
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • Svergun DI, Petoukhov MV, Koch MH (2001) Determination of domain structure of proteins from X-ray solution scattering. Biophys J 80: 2946-2953.
    • (2001) Biophys J , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.3
  • 16
    • 0029185933 scopus 로고
    • CRYSOL - a Program to Evaluate X-ray Solution Scattering of Biological Macromolecules from Atomic Coordinates
    • Svergun DI, Barberato C, Koch MHJ (1995) CRYSOL - a Program to Evaluate X-ray Solution Scattering of Biological Macromolecules from Atomic Coordinates. J Appl Cryst 28: 768-773.
    • (1995) J Appl Cryst , vol.28 , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.J.3
  • 17
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov VV, Svergun DI (2003) Uniqueness of ab initio shape determination in small-angle scattering. J Appl Cryst. pp 860-864.
    • (2003) J Appl Cryst , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 18
    • 39649124274 scopus 로고    scopus 로고
    • The TCL1 oncoprotein inhibits activation-induced cell death by impairing PKCtheta and ERK pathways
    • Despouy G, Joiner M, Le Toriellec E, Weil R, Stern MH (2007) The TCL1 oncoprotein inhibits activation-induced cell death by impairing PKCtheta and ERK pathways. Blood 110: 4406-4416.
    • (2007) Blood , vol.110 , pp. 4406-4416
    • Despouy, G.1    Joiner, M.2    Le Toriellec, E.3    Weil, R.4    Stern, M.H.5
  • 19
    • 33745276259 scopus 로고    scopus 로고
    • Thermodynamics reveal that helix four in the NLS of NF-kappaB p65 anchors IkappaBalpha, forming a very stable complex
    • Bergqvist S, Croy CH, Kjaergaard M, Huxford T, Ghosh G, et al. (2006) Thermodynamics reveal that helix four in the NLS of NF-kappaB p65 anchors IkappaBalpha, forming a very stable complex. J Mol Biol 360: 421-434.
    • (2006) J Mol Biol , vol.360 , pp. 421-434
    • Bergqvist, S.1    Croy, C.H.2    Kjaergaard, M.3    Huxford, T.4    Ghosh, G.5
  • 20
    • 26944443968 scopus 로고    scopus 로고
    • Distinct roles of IkappaB proteins in regulating constitutive NF-kappaB activity
    • Tergaonkar V, Correa RG, Ikawa M, Verma IM (2005) Distinct roles of IkappaB proteins in regulating constitutive NF-kappaB activity. Nat Cell Biol 7: 921-923.
    • (2005) Nat Cell Biol , vol.7 , pp. 921-923
    • Tergaonkar, V.1    Correa, R.G.2    Ikawa, M.3    Verma, I.M.4
  • 21
    • 9044231763 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vpr protein binds to the uracil DNA glycosylase DNA repair enzyme
    • Bouhamdan M, Benichou S, Rey F, Navarro JM, Agostini I, et al. (1996) Human immunodeficiency virus type 1 Vpr protein binds to the uracil DNA glycosylase DNA repair enzyme. J Virol 70: 697-704.
    • (1996) J Virol , vol.70 , pp. 697-704
    • Bouhamdan, M.1    Benichou, S.2    Rey, F.3    Navarro, J.M.4    Agostini, I.5
  • 22
    • 0037458624 scopus 로고    scopus 로고
    • Cyclin D3 is a cofactor of retinoic acid receptors, modulating their activity in the presence of cellular retinoic acid-binding protein II
    • Despouy G, Bastie JN, Deshaies S, Balitrand N, Mazharian A, et al. (2003) Cyclin D3 is a cofactor of retinoic acid receptors, modulating their activity in the presence of cellular retinoic acid-binding protein II. J Biol Chem 278: 6355-6362.
    • (2003) J Biol Chem , vol.278 , pp. 6355-6362
    • Despouy, G.1    Bastie, J.N.2    Deshaies, S.3    Balitrand, N.4    Mazharian, A.5
  • 23
    • 0034693271 scopus 로고    scopus 로고
    • Preparation and crystallization of dynamic NF-kappa B.Ikappa B complexes
    • Huxford T, Malek S, Ghosh G (2000) Preparation and crystallization of dynamic NF-kappa B.Ikappa B complexes. J Biol Chem 275: 32800-32806.
    • (2000) J Biol Chem , vol.275 , pp. 32800-32806
    • Huxford, T.1    Malek, S.2    Ghosh, G.3
  • 24
    • 0037462725 scopus 로고    scopus 로고
    • Post-activation turn-off of NF-kappa B-dependent transcription is regulated by acetylation of p65
    • Kiernan R, Bres V, Ng RW, Coudart MP, El Messaoudi S, et al. (2003) Post-activation turn-off of NF-kappa B-dependent transcription is regulated by acetylation of p65. J Biol Chem 278: 2758-2766.
    • (2003) J Biol Chem , vol.278 , pp. 2758-2766
    • Kiernan, R.1    Bres, V.2    Ng, R.W.3    Coudart, M.P.4    El Messaoudi, S.5
  • 25
    • 1242263882 scopus 로고    scopus 로고
    • Solution structure and backbone dynamics of the pleckstrin homology domain of the human protein kinase B (PKB/Akt). Interaction with inositol phosphates
    • Auguin D, Barthe P, Auge-Senegas MT, Stern MH, Noguchi M, et al. (2004) Solution structure and backbone dynamics of the pleckstrin homology domain of the human protein kinase B (PKB/Akt). Interaction with inositol phosphates. J Biomol NMR 28: 137-155.
    • (2004) J Biomol NMR , vol.28 , pp. 137-155
    • Auguin, D.1    Barthe, P.2    Auge-Senegas, M.T.3    Stern, M.H.4    Noguchi, M.5
  • 27
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • Petoukhov MV, Svergun DI (2005) Global rigid body modeling of macromolecular complexes against small-angle scattering data. Biophys J 89: 1237-1250.
    • (2005) Biophys J , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 28
    • 0026910457 scopus 로고
    • Determination of the Regularization Parameter in Indirect-Transform Methods Using Perceptual Criteria
    • Svergun DI (1992) Determination of the Regularization Parameter in Indirect-Transform Methods Using Perceptual Criteria. J Appl Cryst 25: 495-503.
    • (1992) J Appl Cryst , vol.25 , pp. 495-503
    • Svergun, D.I.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.