메뉴 건너뛰기




Volumn 287, Issue 32, 2012, Pages 27148-27157

Epidermal growth factor receptor protects proliferating cell nuclear antigen from cullin 4A protein-mediated proteolysis

Author keywords

[No Author keywords available]

Indexed keywords

CANCER CELLS; CELL SURFACE RECEPTORS; DNA SYNTHESISS; DOUBLE MUTANTS; DOWN-REGULATION; E3 LIGASE; EPIDERMAL GROWTH FACTOR RECEPTORS; ESSENTIAL COMPONENT; GROWTH STIMULATION; NUCLEAR DNA; POLYUBIQUITYLATION; PROLIFERATING CELL NUCLEAR ANTIGENS; REGULATORY MECHANISM; UBIQUITIN; UBIQUITIN LIGASES; UBIQUITYLATION;

EID: 84864563545     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.388843     Document Type: Article
Times cited : (26)

References (42)
  • 1
    • 0041885325 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen (PCNA): A dancer with many partners
    • Maga, G., and Hubscher, U. (2003) Proliferating cell nuclear antigen (PCNA): a dancer with many partners. J. Cell Sci. 116, 3051-3060
    • (2003) J. Cell Sci. , vol.116 , pp. 3051-3060
    • Maga, G.1    Hubscher, U.2
  • 2
    • 34249066085 scopus 로고    scopus 로고
    • PCNA, the maestro of the replication fork
    • Moldovan, G. L., Pfander, B., and Jentsch, S. (2007) PCNA, the maestro of the replication fork. Cell 129, 665-679
    • (2007) Cell , vol.129 , pp. 665-679
    • Moldovan, G.L.1    Pfander, B.2    Jentsch, S.3
  • 5
    • 38049123477 scopus 로고    scopus 로고
    • Eukaryotic DNA damage tolerance and translesion synthesis through covalent modifications of PCNA
    • Andersen, P. L., Xu, F., and Xiao, W. (2008) Eukaryotic DNA damage tolerance and translesion synthesis through covalent modifications of PCNA. Cell Res. 18, 162-173
    • (2008) Cell Res. , vol.18 , pp. 162-173
    • Andersen, P.L.1    Xu, F.2    Xiao, W.3
  • 6
    • 33746775293 scopus 로고    scopus 로고
    • Translesion synthesis in mammalian cells
    • Lehmann, A. R. (2006) Translesion synthesis in mammalian cells. Exp. Cell Res. 312, 2673-2676
    • (2006) Exp. Cell Res. , vol.312 , pp. 2673-2676
    • Lehmann, A.R.1
  • 7
    • 6344288785 scopus 로고    scopus 로고
    • Rad18 guides poleta to replication stalling sites through physical interaction and PCNA monoubiquitination
    • Watanabe, K., Tateishi, S., Kawasuji, M., Tsurimoto, T., Inoue, H., and Yamaizumi, M. (2004) Rad18 guides poleta to replication stalling sites through physical interaction and PCNA monoubiquitination. EMBO J. 23, 3886-3896
    • (2004) EMBO J. , vol.23 , pp. 3886-3896
    • Watanabe, K.1    Tateishi, S.2    Kawasuji, M.3    Tsurimoto, T.4    Inoue, H.5    Yamaizumi, M.6
  • 8
    • 2442417331 scopus 로고    scopus 로고
    • Interaction of human DNA polymerase η with monoubiquitinated PCNA: A possible mechanism for the polymerase switch in response to DNA damage
    • Kannouche, P. L., Wing, J., and Lehmann, A. R. (2004) Interaction of human DNA polymerase η with monoubiquitinated PCNA: a possible mechanism for the polymerase switch in response to DNA damage. Mol. Cell 14, 491-500
    • (2004) Mol. Cell , vol.14 , pp. 491-500
    • Kannouche, P.L.1    Wing, J.2    Lehmann, A.R.3
  • 9
    • 0141831006 scopus 로고    scopus 로고
    • Control of spontaneous and damageinduced mutagenesis by SUMO and ubiquitin conjugation
    • Stelter, P., and Ulrich, H. D. (2003) Control of spontaneous and damageinduced mutagenesis by SUMO and ubiquitin conjugation. Nature 425, 188-191
    • (2003) Nature , vol.425 , pp. 188-191
    • Stelter, P.1    Ulrich, H.D.2
  • 10
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege, C., Pfander, B., Moldovan, G. L., Pyrowolakis, G., and Jentsch, S. (2002) RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 419, 135-141
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 12
    • 0242551536 scopus 로고    scopus 로고
    • Ratchets and clocks: The cell cycle, ubiquitylation and protein turnover
    • Reed, S. I. (2003) Ratchets and clocks: the cell cycle, ubiquitylation and protein turnover. Nat. Rev. Mol. Cell Biol. 4, 855-864
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 855-864
    • Reed, S.I.1
  • 13
    • 0242525214 scopus 로고    scopus 로고
    • Radiation-mediated proteolysis of CDT1 by CUL4-ROC1 and CSN complexes constitutes a new checkpoint
    • Higa, L. A., Mihaylov, I. S., Banks, D. P., Zheng, J., and Zhang, H. (2003) Radiation-mediated proteolysis of CDT1 by CUL4-ROC1 and CSN complexes constitutes a new checkpoint. Nat. Cell Biol. 5, 1008-1015
    • (2003) Nat. Cell Biol. , vol.5 , pp. 1008-1015
    • Higa, L.A.1    Mihaylov, I.S.2    Banks, D.P.3    Zheng, J.4    Zhang, H.5
  • 14
    • 0037967230 scopus 로고    scopus 로고
    • CUL-4 ubiquitin ligase maintains genome stability by restraining DNA-replication licensing
    • Zhong, W., Feng, H., Santiago, F. E., and Kipreos, E. T. (2003) CUL-4 ubiquitin ligase maintains genome stability by restraining DNA-replication licensing. Nature 423, 885-889
    • (2003) Nature , vol.423 , pp. 885-889
    • Zhong, W.1    Feng, H.2    Santiago, F.E.3    Kipreos, E.T.4
  • 15
    • 5444274523 scopus 로고    scopus 로고
    • Targeted ubiquitination of CDT1 by the DDB1-CUL4A-ROC1 ligase in response to DNA damage
    • Hu, J., McCall, C. M., Ohta, T., and Xiong, Y. (2004) Targeted ubiquitination of CDT1 by the DDB1-CUL4A-ROC1 ligase in response to DNA damage. Nat. Cell Biol. 6, 1003-1009
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1003-1009
    • Hu, J.1    McCall, C.M.2    Ohta, T.3    Xiong, Y.4
  • 16
    • 34250318465 scopus 로고    scopus 로고
    • DCAFs, the missing link of the CUL4-DDB1 ubiquitin ligase
    • Lee, J., and Zhou, P. (2007) DCAFs, the missing link of the CUL4-DDB1 ubiquitin ligase. Mol. Cell 26, 775-780
    • (2007) Mol. Cell , vol.26 , pp. 775-780
    • Lee, J.1    Zhou, P.2
  • 17
    • 20744458539 scopus 로고    scopus 로고
    • Degradation of Cdt1 during S phase is Skp2-independent and is required for efficient progression of mammalian cells through S phase
    • Takeda, D. Y., Parvin, J. D., and Dutta, A. (2005) Degradation of Cdt1 during S phase is Skp2-independent and is required for efficient progression of mammalian cells through S phase. J. Biol. Chem. 280, 23416-23423
    • (2005) J. Biol. Chem. , vol.280 , pp. 23416-23423
    • Takeda, D.Y.1    Parvin, J.D.2    Dutta, A.3
  • 19
    • 33750361592 scopus 로고    scopus 로고
    • DDB1 maintains genome integrity through regulation of Cdt1
    • Lovejoy, C. A., Lock, K., Yenamandra, A., and Cortez, D. (2006) DDB1 maintains genome integrity through regulation of Cdt1. Mol. Cell. Biol. 26, 7977-7990
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 7977-7990
    • Lovejoy, C.A.1    Lock, K.2    Yenamandra, A.3    Cortez, D.4
  • 20
    • 0043234476 scopus 로고    scopus 로고
    • The SCF(Skp2) ubiquitin ligase complex interacts with the human replication licensing factor Cdt1 and regulates Cdt1 degradation
    • Li, X., Zhao, Q., Liao, R., Sun, P., and Wu, X. (2003) The SCF(Skp2) ubiquitin ligase complex interacts with the human replication licensing factor Cdt1 and regulates Cdt1 degradation. J. Biol. Chem. 278, 30854-30858
    • (2003) J. Biol. Chem. , vol.278 , pp. 30854-30858
    • Li, X.1    Zhao, Q.2    Liao, R.3    Sun, P.4    Wu, X.5
  • 21
    • 33645212112 scopus 로고    scopus 로고
    • An evolutionarily conserved function of proliferating cell nuclear antigen for Cdt1 degradation by the Cul4-Ddb1 ubiquitin ligase in response to DNA damage
    • Hu, J., and Xiong, Y. (2006) An evolutionarily conserved function of proliferating cell nuclear antigen for Cdt1 degradation by the Cul4-Ddb1 ubiquitin ligase in response to DNA damage. J. Biol. Chem. 281, 3753-3756
    • (2006) J. Biol. Chem. , vol.281 , pp. 3753-3756
    • Hu, J.1    Xiong, Y.2
  • 22
    • 33747831132 scopus 로고    scopus 로고
    • L2DTL/CDT2 interacts with the CUL4/DDB1 complex andPCNA and regulates CDT1 proteolysis in response to DNA damage
    • Higa, L. A., Banks, D., Wu, M., Kobayashi, R., Sun, H., and Zhang, H. (2006) L2DTL/CDT2 interacts with the CUL4/DDB1 complex andPCNA and regulates CDT1 proteolysis in response to DNA damage. Cell Cycle 5, 1675-1680
    • (2006) Cell Cycle , vol.5 , pp. 1675-1680
    • Higa, L.A.1    Banks, D.2    Wu, M.3    Kobayashi, R.4    Sun, H.5    Zhang, H.6
  • 23
    • 11844273174 scopus 로고    scopus 로고
    • Replication-dependent destruction of Cdt1 limitsDNAreplication to a single round per cell cycle in Xenopus egg extracts
    • Arias, E. E., and Walter, J. C. (2005) Replication-dependent destruction of Cdt1 limitsDNAreplication to a single round per cell cycle in Xenopus egg extracts. Genes Dev. 19, 114-126
    • (2005) Genes Dev. , vol.19 , pp. 114-126
    • Arias, E.E.1    Walter, J.C.2
  • 24
    • 30344455639 scopus 로고    scopus 로고
    • PCNA functions as a molecular platform to trigger Cdt1 destruction and prevent re-replication
    • Arias, E. E., and Walter, J. C. (2006) PCNA functions as a molecular platform to trigger Cdt1 destruction and prevent re-replication. Nat. Cell Biol. 8, 84-90
    • (2006) Nat. Cell Biol. , vol.8 , pp. 84-90
    • Arias, E.E.1    Walter, J.C.2
  • 25
    • 33747873322 scopus 로고    scopus 로고
    • A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is required for S phase destruction of the replication factor Cdt1
    • Jin, J., Arias, E. E., Chen, J., Harper, J. W., and Walter, J. C. (2006) A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is required for S phase destruction of the replication factor Cdt1. Mol. Cell 23, 709-721
    • (2006) Mol. Cell , vol.23 , pp. 709-721
    • Jin, J.1    Arias, E.E.2    Chen, J.3    Harper, J.W.4    Walter, J.C.5
  • 26
    • 33646504727 scopus 로고    scopus 로고
    • PCNA is a cofactor for Cdt1 degradation by CUL4/DDB1-mediated N-terminal ubiquitination
    • Senga, T., Sivaprasad, U., Zhu, W., Park, J. H., Arias, E. E., Walter, J. C., and Dutta, A. (2006) PCNA is a cofactor for Cdt1 degradation by CUL4/DDB1-mediated N-terminal ubiquitination. J. Biol. Chem. 281, 6246-6252
    • (2006) J. Biol. Chem. , vol.281 , pp. 6246-6252
    • Senga, T.1    Sivaprasad, U.2    Zhu, W.3    Park, J.H.4    Arias, E.E.5    Walter, J.C.6    Dutta, A.7
  • 27
    • 80053583606 scopus 로고    scopus 로고
    • A genome-wide screen identifies p97 as an essential regulator of DNA damage-dependent CDT1 destruction
    • Raman, M., Havens, C. G., Walter, J. C., and Harper, J. W. (2011) A genome-wide screen identifies p97 as an essential regulator of DNA damage-dependent CDT1 destruction. Molecular Cell 44, 72-84
    • (2011) Molecular Cell , vol.44 , pp. 72-84
    • Raman, M.1    Havens, C.G.2    Walter, J.C.3    Harper, J.W.4
  • 28
    • 77956635549 scopus 로고    scopus 로고
    • The CRL4Cdt2 ubiquitin ligase mediates the proteolysis of cyclin-dependent kinase inhibitor Xic1 through a direct association with PCNA
    • Kim, D. H., Budhavarapu, V. N., Herrera, C. R., Nam, H. W., Kim, Y. S., and Yew, P. R. (2010) The CRL4Cdt2 ubiquitin ligase mediates the proteolysis of cyclin-dependent kinase inhibitor Xic1 through a direct association with PCNA. Mol. Cell. Biol. 30, 4120-4133
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 4120-4133
    • Kim, D.H.1    Budhavarapu, V.N.2    Herrera, C.R.3    Nam, H.W.4    Kim, Y.S.5    Yew, P.R.6
  • 29
    • 51949098691 scopus 로고    scopus 로고
    • PCNA-dependent regulation of p21 ubiquitylation and degradation via the CRL4Cdt2 ubiquitin ligase complex
    • Abbas, T., Sivaprasad, U., Terai, K., Amador, V., Pagano, M., and Dutta, A. (2008) PCNA-dependent regulation of p21 ubiquitylation and degradation via the CRL4Cdt2 ubiquitin ligase complex. Genes Dev. 22, 2496-2506
    • (2008) Genes Dev. , vol.22 , pp. 2496-2506
    • Abbas, T.1    Sivaprasad, U.2    Terai, K.3    Amador, V.4    Pagano, M.5    Dutta, A.6
  • 30
    • 67649641658 scopus 로고    scopus 로고
    • Docking of a specialized PIP Box onto chromatin-bound PCNA creates a degron for the ubiquitin ligase CRL4Cdt2
    • Havens, C. G., and Walter, J. C. (2009) Docking of a specialized PIP Box onto chromatin-bound PCNA creates a degron for the ubiquitin ligase CRL4Cdt2. Mol. Cell 35, 93-104
    • (2009) Mol. Cell , vol.35 , pp. 93-104
    • Havens, C.G.1    Walter, J.C.2
  • 31
    • 73649125005 scopus 로고    scopus 로고
    • CRL4(Cdt2) E3 ubiquitin ligase monoubiquitinates PCNA to promote translesion DNA synthesis
    • Terai, K., Abbas, T., Jazaeri, A. A., and Dutta, A. (2010) CRL4(Cdt2) E3 ubiquitin ligase monoubiquitinates PCNA to promote translesion DNA synthesis. Mol. Cell 37, 143-149
    • (2010) Mol. Cell , vol.37 , pp. 143-149
    • Terai, K.1    Abbas, T.2    Jazaeri, A.A.3    Dutta, A.4
  • 32
    • 41649117158 scopus 로고    scopus 로고
    • WD40 protein FBW5 promotes ubiquitination of tumor suppressor TSC2 by DDB1-CUL4-ROC1 ligase
    • Hu, J., Zacharek, S., He, Y. J., Lee, H., Shumway, S., Duronio, R. J., and Xiong, Y. (2008) WD40 protein FBW5 promotes ubiquitination of tumor suppressor TSC2 by DDB1-CUL4-ROC1 ligase. Genes Dev. 22, 866-871
    • (2008) Genes Dev. , vol.22 , pp. 866-871
    • Hu, J.1    Zacharek, S.2    He, Y.J.3    Lee, H.4    Shumway, S.5    Duronio, R.J.6    Xiong, Y.7
  • 34
    • 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., and Sabatini, D. M. (2005) Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex. Science 307, 1098-1101
    • (2005) Science , vol.307 , pp. 1098-1101
    • Sarbassov, D.D.1    Guertin, D.A.2    Ali, S.M.3    Sabatini, D.M.4
  • 35
    • 51349145743 scopus 로고    scopus 로고
    • Confocal imaging and tracking of the exocytotic routes for D-serine-mediated gliotransmission
    • Martineau, M., Galli, T., Baux, G., and Mothet, J. P. (2008) Confocal imaging and tracking of the exocytotic routes for D-serine-mediated gliotransmission. Glia 56, 1271-1284
    • (2008) Glia , vol.56 , pp. 1271-1284
    • Martineau, M.1    Galli, T.2    Baux, G.3    Mothet, J.P.4
  • 37
    • 77955904679 scopus 로고    scopus 로고
    • A chromatin-bound kinase, ERK8, protects genomic integrity by inhibiting HDM2-mediated degradation of the DNA clamp PCNA
    • Groehler, A. L., and Lannigan, D. A. (2010) A chromatin-bound kinase, ERK8, protects genomic integrity by inhibiting HDM2-mediated degradation of the DNA clamp PCNA. J. Cell Biol. 190, 575-586
    • (2010) J. Cell Biol. , vol.190 , pp. 575-586
    • Groehler, A.L.1    Lannigan, D.A.2
  • 39
    • 34047161279 scopus 로고    scopus 로고
    • Cullin 4 makes its mark on chromatin
    • Dai, Q., and Wang, H. (2006) Cullin 4 makes its mark on chromatin. Cell Div. 1, 14
    • (2006) Cell Div. , vol.1 , pp. 14
    • Dai, Q.1    Wang, H.2
  • 41
  • 42
    • 65649084086 scopus 로고    scopus 로고
    • The CUL4 enigma: Culling DNA repair factors
    • Sugasawa, K. (2009) The CUL4 enigma: culling DNA repair factors. Mol. Cell 34, 403-404
    • (2009) Mol. Cell , vol.34 , pp. 403-404
    • Sugasawa, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.