메뉴 건너뛰기




Volumn 30, Issue 1, 2010, Pages 160-171

Activation of the S-phase checkpoint inhibits degradation of the F-box protein dia

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME; F BOX PROTEIN; F BOX PROTEIN DIA2; HYDROXYUREA; MUTANT PROTEIN; S PHASE CHECKPOINT ENZYME; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 73549113777     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.00612-09     Document Type: Article
Times cited : (15)

References (48)
  • 2
    • 0027953230 scopus 로고
    • The SAD1/RAD53 protein kinase controls multiple checkpoints and DNA damage-induced transcription in yeast
    • Allen, J. B., Z. Zhou, W. Siede, E. C. Friedberg, and S. J. Elledge. 1994. The SAD1/RAD53 protein kinase controls multiple checkpoints and DNA damage-induced transcription in yeast. Genes Dev. 8:2401-2415.
    • (1994) Genes Dev , vol.8 , pp. 2401-2415
    • Allen, J.B.1    Zhou, Z.2    Siede, W.3    Friedberg, E.C.4    Elledge, S.J.5
  • 3
    • 1642378661 scopus 로고    scopus 로고
    • Control of the SCF(Skp2-Cks1) ubiquitin ligase by the APC/C(Cdh1) ubiquitin ligase
    • Bashir, T., N. V. Dorrello, V. Amador, D. Guardavaccaro, and M. Pagano. 2004. Control of the SCF(Skp2-Cks1) ubiquitin ligase by the APC/C(Cdh1) ubiquitin ligase. Nature 428:190-193.
    • (2004) Nature , vol.428 , pp. 190-193
    • Bashir, T.1    Dorrello, N.V.2    Amador, V.3    Guardavaccaro, D.4    Pagano, M.5
  • 5
    • 0034669189 scopus 로고    scopus 로고
    • Nuclear-specific degradation of Far1 is controlled by the localization of the F-box protein Cdc4
    • Blondel, M., J. M. Galan, Y. Chi, C. Lafourcade, C. Longaretti, R. J. Deshaies, and M. Peter. 2000. Nuclear-specific degradation of Far1 is controlled by the localization of the F-box protein Cdc4. EMBO J. 19:6085-6097.
    • (2000) EMBO J , vol.19 , pp. 6085-6097
    • Blondel, M.1    Galan, J.M.2    Chi, Y.3    Lafourcade, C.4    Longaretti, C.5    Deshaies, R.J.6    Peter, M.7
  • 6
    • 0000502113 scopus 로고    scopus 로고
    • DNA replication checkpoint
    • Boddy, M. N., and P. Russell. 2001. DNA replication checkpoint. Curr. Biol. 11:R953-R956.
    • (2001) Curr. Biol , vol.11
    • Boddy, M.N.1    Russell, P.2
  • 7
    • 27544445683 scopus 로고    scopus 로고
    • The DNA damage response during DNA replication
    • Branzei, D., and M. Foiani. 2005. The DNA damage response during DNA replication. Curr. Opin. Cell Biol. 17:568-575.
    • (2005) Curr. Opin. Cell Biol , vol.17 , pp. 568-575
    • Branzei, D.1    Foiani, M.2
  • 8
    • 41549152973 scopus 로고    scopus 로고
    • Orchestration of the S-phase and DNA damage checkpoint pathways by replication forks from early origins
    • Caldwell, J. M., Y. Chen, K. L. Schollaert, J. F. Theis, G. F. Babcock, C. S. Newlon, and Y. Sanchez. 2008. Orchestration of the S-phase and DNA damage checkpoint pathways by replication forks from early origins. J. Cell Biol. 180:1073-1086.
    • (2008) J. Cell Biol , vol.180 , pp. 1073-1086
    • Caldwell, J.M.1    Chen, Y.2    Schollaert, K.L.3    Theis, J.F.4    Babcock, G.F.5    Newlon, C.S.6    Sanchez, Y.7
  • 9
    • 0033176887 scopus 로고    scopus 로고
    • SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27
    • Carrano, A. C., E. Eytan, A. Hershko, and M. Pagano. 1999. SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27. Nat. Cell Biol. 1:193-199.
    • (1999) Nat. Cell Biol , vol.1 , pp. 193-199
    • Carrano, A.C.1    Eytan, E.2    Hershko, A.3    Pagano, M.4
  • 11
    • 0030695025 scopus 로고    scopus 로고
    • A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p
    • Feldman, R. M., C. C. Correll, K. B. Kaplan, and R. J. Deshaies. 1997. A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p. Cell 91:221-230.
    • (1997) Cell , vol.91 , pp. 221-230
    • Feldman, R.M.1    Correll, C.C.2    Kaplan, K.B.3    Deshaies, R.J.4
  • 12
    • 34249672693 scopus 로고    scopus 로고
    • Delayed accumulation of the yeast G(l) cyclins Clnl and Cln2 and the F-box protein Grrl in response to glucose
    • Fey, J. P., and S. Lanker. 2007. Delayed accumulation of the yeast G(l) cyclins Clnl and Cln2 and the F-box protein Grrl in response to glucose. Yeast 24:419-429.
    • (2007) Yeast , vol.24 , pp. 419-429
    • Fey, J.P.1    Lanker, S.2
  • 13
    • 0033529757 scopus 로고    scopus 로고
    • Ubiquitin-dependent degradation of multiple F-box proteins by an autocatalytic mechanism
    • Galan, J. M., and M. Peter. 1999. Ubiquitin-dependent degradation of multiple F-box proteins by an autocatalytic mechanism. Proc. Natl. Acad. Sci. U.S.A. 96:9124-9129.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 9124-9129
    • Galan, J.M.1    Peter, M.2
  • 14
    • 33751419716 scopus 로고    scopus 로고
    • Surviving the breakup: The DNA damage checkpoint
    • Harrison, J. C., and J. E. Haber. 2006. Surviving the breakup: the DNA damage checkpoint. Annu. Rev. Genet. 40:209-235.
    • (2006) Annu. Rev. Genet , vol.40 , pp. 209-235
    • Harrison, J.C.1    Haber, J.E.2
  • 15
    • 0037050004 scopus 로고    scopus 로고
    • Ho, Y., A. Gruhler, A. Heilbut, G. D. Bader, L. Moore, S. L. Adams, A. Millar, P. Taylor, K. Bennett, K. Boutilier, L. Yang, C. Wolting, I. Donaldson, S. Schandorff, J. Shewnarane, M. Vo, J. Taggart, M. Goudreault, B. Muskat, C. Alfarano, D. Dewar, Z. Lin, K. Michalickova, A. R. Willems, H. Sassi, P. A. Nielsen, K. J. Rasmussen, J. R. Andersen, L. E. Johansen, L. H. Hansen, H. Jespersen, A. Podtelejnikov, E. Nielsen, J. Crawford, V. Poulsen, B. D. Sorensen, J. Matthiesen, R. C. Hendrickson, F. Gleeson, T. Pawson, M. F. Moran, D. Durocher, M. Mann, C. W. Hogue, D. Figeys, and M. Tyers. 2002. Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 415:180-183.
    • Ho, Y., A. Gruhler, A. Heilbut, G. D. Bader, L. Moore, S. L. Adams, A. Millar, P. Taylor, K. Bennett, K. Boutilier, L. Yang, C. Wolting, I. Donaldson, S. Schandorff, J. Shewnarane, M. Vo, J. Taggart, M. Goudreault, B. Muskat, C. Alfarano, D. Dewar, Z. Lin, K. Michalickova, A. R. Willems, H. Sassi, P. A. Nielsen, K. J. Rasmussen, J. R. Andersen, L. E. Johansen, L. H. Hansen, H. Jespersen, A. Podtelejnikov, E. Nielsen, J. Crawford, V. Poulsen, B. D. Sorensen, J. Matthiesen, R. C. Hendrickson, F. Gleeson, T. Pawson, M. F. Moran, D. Durocher, M. Mann, C. W. Hogue, D. Figeys, and M. Tyers. 2002. Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 415:180-183.
  • 18
    • 0035812709 scopus 로고    scopus 로고
    • Phosphorylation-dependent ubiquitination of cyclin E by the SCFFbw7 ubiquitin ligase
    • Koepp, D. M., L. K. Schaefer, X. Ye, K. Keyomarsi, C. Chu, J. W. Harper, and S. J. Elledge. 2001. Phosphorylation-dependent ubiquitination of cyclin E by the SCFFbw7 ubiquitin ligase. Science 294:173-177.
    • (2001) Science , vol.294 , pp. 173-177
    • Koepp, D.M.1    Schaefer, L.K.2    Ye, X.3    Keyomarsi, K.4    Chu, C.5    Harper, J.W.6    Elledge, S.J.7
  • 19
    • 1042268088 scopus 로고    scopus 로고
    • Functional interaction of 13 yeast SCF complexes with a set of yeast E2 enzymes in vitro
    • Kus, B. M., C. E. Caldon, R. Andorn-Broza, and A. M. Edwards. 2004. Functional interaction of 13 yeast SCF complexes with a set of yeast E2 enzymes in vitro. Proteins 54:455-467.
    • (2004) Proteins , vol.54 , pp. 455-467
    • Kus, B.M.1    Caldon, C.E.2    Andorn-Broza, R.3    Edwards, A.M.4
  • 20
    • 34247135913 scopus 로고    scopus 로고
    • Classical nuclear localization signals: Definition, function, and interaction with importin alpha
    • Lange, A., R. E. Mills, C. J. Lange, M. Stewart, S. E. Devine, and A. H. Corbett. 2007. Classical nuclear localization signals: definition, function, and interaction with importin alpha. J. Biol. Chem. 282:5101-5105.
    • (2007) J. Biol. Chem , vol.282 , pp. 5101-5105
    • Lange, A.1    Mills, R.E.2    Lange, C.J.3    Stewart, M.4    Devine, S.E.5    Corbett, A.H.6
  • 21
    • 0032481104 scopus 로고    scopus 로고
    • The univector plasmid-fusion system, a method for rapid construction of recombinant DNA without restriction enzymes
    • Liu, Q., M. Z. Li, D. Leibham, D. Cortez, and S. J. Elledge. 1998. The univector plasmid-fusion system, a method for rapid construction of recombinant DNA without restriction enzymes. Curr. Biol. 8:1300-1309.
    • (1998) Curr. Biol , vol.8 , pp. 1300-1309
    • Liu, Q.1    Li, M.Z.2    Leibham, D.3    Cortez, D.4    Elledge, S.J.5
  • 23
    • 0037418195 scopus 로고    scopus 로고
    • Yeast Rad17/Mec3/Ddc1: A sliding clamp for the DNA damage checkpoint
    • Majka, J., and P. M. Burgers. 2003. Yeast Rad17/Mec3/Ddc1: a sliding clamp for the DNA damage checkpoint. Proc. Natl. Acad. Sci. U.S.A. 100: 2249-2254.
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 2249-2254
    • Majka, J.1    Burgers, P.M.2
  • 24
    • 0033055912 scopus 로고    scopus 로고
    • The abundance of cell cycle regulatory protein Cdc4p is controlled by interactions between its F box and Skp1p
    • Mathias, N., S. Johnson, B. Byers, and M. Goebl. 1999. The abundance of cell cycle regulatory protein Cdc4p is controlled by interactions between its F box and Skp1p. Mol. Cell. Biol. 19:1759-1767.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 1759-1767
    • Mathias, N.1    Johnson, S.2    Byers, B.3    Goebl, M.4
  • 25
    • 0029860817 scopus 로고    scopus 로고
    • Cdc53p acts in concert with Cdc4p and Cdc34p to control the G1-to-S-phase transition and identifies a conserved family of proteins
    • Mathias, N., S. L. Johnson, M. Winey, A. E. Adams, L. Goetsch, J. R. Pringle, B. Byers, and M. G. Goebl. 1996. Cdc53p acts in concert with Cdc4p and Cdc34p to control the G1-to-S-phase transition and identifies a conserved family of proteins. Mol. Cell. Biol. 16:6634-6643.
    • (1996) Mol. Cell. Biol , vol.16 , pp. 6634-6643
    • Mathias, N.1    Johnson, S.L.2    Winey, M.3    Adams, A.E.4    Goetsch, L.5    Pringle, J.R.6    Byers, B.7    Goebl, M.G.8
  • 26
    • 0036948433 scopus 로고    scopus 로고
    • Toward maintaining the genome: DNA damage and replication checkpoints
    • Nyberg, K. A., R. J. Michelson, C. W. Putnam, and T. A. Weinert. 2002. Toward maintaining the genome: DNA damage and replication checkpoints. Annu. Rev. Genet. 36:617-656.
    • (2002) Annu. Rev. Genet , vol.36 , pp. 617-656
    • Nyberg, K.A.1    Michelson, R.J.2    Putnam, C.W.3    Weinert, T.A.4
  • 27
    • 0038506000 scopus 로고    scopus 로고
    • Mrc1 is a replication fork component whose phosphorylation in response to DNA replication stress activates Rad53
    • Osborn, A. J., and S. J. Elledge. 2003. Mrc1 is a replication fork component whose phosphorylation in response to DNA replication stress activates Rad53. Genes Dev. 17:1755-1767.
    • (2003) Genes Dev , vol.17 , pp. 1755-1767
    • Osborn, A.J.1    Elledge, S.J.2
  • 28
    • 33644778778 scopus 로고    scopus 로고
    • A DNA integrity network in the yeast Saccharomyces cerevisiae
    • Pan, X., P. Ye, D. S. Yuan, X. Wang, J. S. Bader, and J. D. Boeke. 2006. A DNA integrity network in the yeast Saccharomyces cerevisiae. Cell 124: 1069-1081.
    • (2006) Cell , vol.124 , pp. 1069-1081
    • Pan, X.1    Ye, P.2    Yuan, D.S.3    Wang, X.4    Bader, J.S.5    Boeke, J.D.6
  • 29
    • 0032191402 scopus 로고    scopus 로고
    • Cdc53 is a scaffold protein for multiple Cdc34/Skp1/F box protein complexes that regulate cell division and methionine biosynthesis in yeast (vol 12, pg 914, 1998)
    • Patton, E. E., A. R. Willems, D. Sa, L. Kuras, D. Thomas, K. L. Craig, and M. Tyers. 1998. Cdc53 is a scaffold protein for multiple Cdc34/Skp1/F box protein complexes that regulate cell division and methionine biosynthesis in yeast (vol 12, pg 914, 1998). Genes Dev. 12:3144.
    • (1998) Genes Dev , vol.12 , pp. 3144
    • Patton, E.E.1    Willems, A.R.2    Sa, D.3    Kuras, L.4    Thomas, D.5    Craig, K.L.6    Tyers, M.7
  • 30
    • 0029085781 scopus 로고
    • A checkpoint regulates the rate of progression through S phase in S. cerevisiae in response to DNA damage
    • Paulovich, A. G., and L. H. Hartwell. 1995. A checkpoint regulates the rate of progression through S phase in S. cerevisiae in response to DNA damage. Cell 82:841-847.
    • (1995) Cell , vol.82 , pp. 841-847
    • Paulovich, A.G.1    Hartwell, L.H.2
  • 31
    • 6344284782 scopus 로고    scopus 로고
    • Mcm10 regulates the stability and chromatin association of DNA polymerase-alpha
    • Ricke, R. M., and A. K. Bielinsky. 2004. Mcm10 regulates the stability and chromatin association of DNA polymerase-alpha. Mol. Cell 16:173-185.
    • (2004) Mol. Cell , vol.16 , pp. 173-185
    • Ricke, R.M.1    Bielinsky, A.K.2
  • 33
    • 0033527787 scopus 로고    scopus 로고
    • Control of the DNA damage checkpoint by chk1 and rad53 protein kinases through distinct mechanisms
    • Sanchez, Y., J. Bachant, H. Wang, F. Hu, D. Liu, M. Tetzlaff, and S. J. Elledge. 1999. Control of the DNA damage checkpoint by chk1 and rad53 protein kinases through distinct mechanisms. Science 286:1166-1171.
    • (1999) Science , vol.286 , pp. 1166-1171
    • Sanchez, Y.1    Bachant, J.2    Wang, H.3    Hu, F.4    Liu, D.5    Tetzlaff, M.6    Elledge, S.J.7
  • 34
    • 0032497529 scopus 로고    scopus 로고
    • A Mec1- and Rad53-dependent checkpoint controls late-firing origins of DNA replication
    • Santocanale, C., and J. F. Diffley. 1998. A Mec1- and Rad53-dependent checkpoint controls late-firing origins of DNA replication. Nature 395:615-618.
    • (1998) Nature , vol.395 , pp. 615-618
    • Santocanale, C.1    Diffley, J.F.2
  • 37
    • 0030662523 scopus 로고    scopus 로고
    • F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex
    • Skowyra, D., K. L. Craig, M. Tyers, S. J. Elledge, and J. W. Harper. 1997. F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex. Cell 91:209-219.
    • (1997) Cell , vol.91 , pp. 209-219
    • Skowyra, D.1    Craig, K.L.2    Tyers, M.3    Elledge, S.J.4    Harper, J.W.5
  • 39
    • 0033776759 scopus 로고    scopus 로고
    • The abundance of Met30p limits SCFMet30p complex activity and is regulated by methionine availability
    • Smothers, D. B., L. Kozubowski, C. Dixon, M. G. Goebl, and N. Mathias. 2000. The abundance of Met30p limits SCFMet30p complex activity and is regulated by methionine availability. Mol. Cell. Biol. 20:7845-7852.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 7845-7852
    • Smothers, D.B.1    Kozubowski, L.2    Dixon, C.3    Goebl, M.G.4    Mathias, N.5
  • 41
    • 0035921849 scopus 로고    scopus 로고
    • Human F-box protein hCdc4 targets cyclin E for proteolysis and is mutated in a breast cancer cell line
    • Strohmaier, H., C. H. Spruck, P. Kaiser, K. A. Won, O. Sangfelt, and S. I. Reed. 2001. Human F-box protein hCdc4 targets cyclin E for proteolysis and is mutated in a breast cancer cell line. Nature 413:316-322.
    • (2001) Nature , vol.413 , pp. 316-322
    • Strohmaier, H.1    Spruck, C.H.2    Kaiser, P.3    Won, K.A.4    Sangfelt, O.5    Reed, S.I.6
  • 42
    • 34347360773 scopus 로고    scopus 로고
    • Yra1 is required for S phase entry and affects Dia2 binding to replication origins
    • Swaminathan, S., A. C. Kile, E. M. MacDonald, and D. M. Koepp. 2007. Yra1 is required for S phase entry and affects Dia2 binding to replication origins. Mol. Cell. Biol. 27:4674-4684.
    • (2007) Mol. Cell. Biol , vol.27 , pp. 4674-4684
    • Swaminathan, S.1    Kile, A.C.2    MacDonald, E.M.3    Koepp, D.M.4
  • 43
    • 0035797444 scopus 로고    scopus 로고
    • Regulation of DNA replication fork progression through damaged DNA by the Mec1/Rad53 checkpoint
    • Tercero, J. A., and J. F. Diffley. 2001. Regulation of DNA replication fork progression through damaged DNA by the Mec1/Rad53 checkpoint. Nature 412:553-557.
    • (2001) Nature , vol.412 , pp. 553-557
    • Tercero, J.A.1    Diffley, J.F.2
  • 44
    • 10744230485 scopus 로고    scopus 로고
    • Tong, A. H., G. Lesage, G. D. Bader, H. Ding, H. Xu, X. Xin, J. Young, G. F. Berriz, R. L. Brost, M. Chang, Y. Chen, X. Cheng, G. Chua, H. Friesen, D. S. Goldberg, J. Haynes, C. Humphries, G. He, S. Hussein, L. Ke, N. Krogan, Z. Li, J. N. Levinson, H. Lu, P. Menard, C. Munyana, A. B. Parsons, O. Ryan, R. Tonikian, T. Roberts, A. M. Sdicu, J. Shapiro, B. Sheikh, B. Suter, S. L. Wong, L. V. Zhang, H. Zhu, C. G. Burd, S. Munro, C. Sander, J. Rine, J. Greenblatt, M. Peter, A. Bretscher, G. Bell, F. P. Roth, G. W. Brown, B. Andrews, H. Bussey, and C. Boone. 2004. Global mapping of the yeast genetic interaction network. Science 303:808-813.
    • Tong, A. H., G. Lesage, G. D. Bader, H. Ding, H. Xu, X. Xin, J. Young, G. F. Berriz, R. L. Brost, M. Chang, Y. Chen, X. Cheng, G. Chua, H. Friesen, D. S. Goldberg, J. Haynes, C. Humphries, G. He, S. Hussein, L. Ke, N. Krogan, Z. Li, J. N. Levinson, H. Lu, P. Menard, C. Munyana, A. B. Parsons, O. Ryan, R. Tonikian, T. Roberts, A. M. Sdicu, J. Shapiro, B. Sheikh, B. Suter, S. L. Wong, L. V. Zhang, H. Zhu, C. G. Burd, S. Munro, C. Sander, J. Rine, J. Greenblatt, M. Peter, A. Bretscher, G. Bell, F. P. Roth, G. W. Brown, B. Andrews, H. Bussey, and C. Boone. 2004. Global mapping of the yeast genetic interaction network. Science 303:808-813.
  • 45
    • 0033578073 scopus 로고    scopus 로고
    • p27(Kip1) ubiquitination and degradation is regulated by the SCF(Skp2) complex through phosphorylated Thr187 in p27
    • Tsvetkov, L. M., K. H. Yeh, S. J. Lee, H. Sun, and H. Zhang. 1999. p27(Kip1) ubiquitination and degradation is regulated by the SCF(Skp2) complex through phosphorylated Thr187 in p27. Curr. Biol. 9:661-664.
    • (1999) Curr. Biol , vol.9 , pp. 661-664
    • Tsvetkov, L.M.1    Yeh, K.H.2    Lee, S.J.3    Sun, H.4    Zhang, H.5
  • 46
    • 0034235463 scopus 로고    scopus 로고
    • Structure-based predictions of Rad1, Rad9, Hus1 and Rad17 participation in sliding clamp and clamp-loading complexes
    • Venclovas, C., and M. P. Thelen. 2000. Structure-based predictions of Rad1, Rad9, Hus1 and Rad17 participation in sliding clamp and clamp-loading complexes. Nucleic Acids Res. 28:2481-2493.
    • (2000) Nucleic Acids Res , vol.28 , pp. 2481-2493
    • Venclovas, C.1    Thelen, M.P.2
  • 48
    • 0032215237 scopus 로고    scopus 로고
    • Ubiquitination and degradation of the substrate recognition subunits of SCF ubiquitin-protein ligases
    • Zhou, P., and P. M. Howley. 1998. Ubiquitination and degradation of the substrate recognition subunits of SCF ubiquitin-protein ligases. Mol. Cell 2:571-580.
    • (1998) Mol. Cell , vol.2 , pp. 571-580
    • Zhou, P.1    Howley, P.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.