메뉴 건너뛰기




Volumn 15, Issue 12, 2004, Pages 5208-5218

Distinct in vivo dynamics of vertebrate SUMO paralogues

Author keywords

[No Author keywords available]

Indexed keywords

SUMO 1 PROTEIN; SUMO 2 PROTEIN; SUMO 3 PROTEIN; SUMO PROTEIN; UNCLASSIFIED DRUG; YELLOW FLUORESCENT PROTEIN;

EID: 9444260454     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E04-07-0589     Document Type: Article
Times cited : (166)

References (23)
  • 1
    • 0242509262 scopus 로고    scopus 로고
    • SUMO-2/3 regulates topoisomerase II in mitosis
    • Azuma, Y., Arnaoutov, A., and Dasso, M. (2003). SUMO-2/3 regulates topoisomerase II in mitosis. J. Cell Biol. 163, 477-487.
    • (2003) J. Cell Biol. , vol.163 , pp. 477-487
    • Azuma, Y.1    Arnaoutov, A.2    Dasso, M.3
  • 2
    • 0036291014 scopus 로고    scopus 로고
    • The SUMO-1 isopeptidase Smt4 is linked to centromeric cohesion through SUMO-1 modification of DNA topoisomerase II
    • Bachant, J., Alcasabas, A., Blat, Y., Kleckner, N., and Elledge, S.J. (2002). The SUMO-1 isopeptidase Smt4 is linked to centromeric cohesion through SUMO-1 modification of DNA topoisomerase II. Mol. Cell 9, 1169-1182.
    • (2002) Mol. Cell , vol.9 , pp. 1169-1182
    • Bachant, J.1    Alcasabas, A.2    Blat, Y.3    Kleckner, N.4    Elledge, S.J.5
  • 3
    • 1542407105 scopus 로고    scopus 로고
    • Smt3/SUMO and Ubc9 are required for efficient APC/C-mediated proteolysis in budding yeast
    • Dieckhoff, P., Bolte, M., Sancak, Y., Braus, G.H., and Imiger, S. (2004). Smt3/SUMO and Ubc9 are required for efficient APC/C-mediated proteolysis in budding yeast. Mol. Microbiol. 51, 1375-1387.
    • (2004) Mol. Microbiol. , vol.51 , pp. 1375-1387
    • Dieckhoff, P.1    Bolte, M.2    Sancak, Y.3    Braus, G.H.4    Imiger, S.5
  • 4
    • 0030794729 scopus 로고    scopus 로고
    • The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer
    • Johnson, E.S., Schwienhorst, I., Dohmen, R.J., and Blobel, G. (1997). The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer. EMBO J. 16, 5509-5519.
    • (1997) EMBO J. , vol.16 , pp. 5509-5519
    • Johnson, E.S.1    Schwienhorst, I.2    Dohmen, R.J.3    Blobel, G.4
  • 5
    • 1842715846 scopus 로고    scopus 로고
    • The RanGAP1-RanBP2 complex is essential for microtubule-kinetochore interactions in vivo
    • Joseph, J., Liu, S. T., Jablonski, S. A., Yen, T. J., Dosso, M. (2004). The RanGAP1-RanBP2 complex is essential for microtubule-kinetochore interactions in vivo. Curr. Biol. 14, 611-617.
    • (2004) Curr. Biol. , vol.14 , pp. 611-617
    • Joseph, J.1    Liu, S.T.2    Jablonski, S.A.3    Yen, T.J.4    Dosso, M.5
  • 6
    • 0037128207 scopus 로고    scopus 로고
    • SUMO-1 targets RanGAP1 to kinetochores and mitotic spindles
    • Joseph, J., Tan, S.H., Karpova, T.S., McNally, J.G., and Dasso, M. (2002). SUMO-1 targets RanGAP1 to kinetochores and mitotic spindles. J. Cell Biol. 156, 595-602.
    • (2002) J. Cell Biol. , vol.156 , pp. 595-602
    • Joseph, J.1    Tan, S.H.2    Karpova, T.S.3    McNally, J.G.4    Dasso, M.5
  • 7
    • 0032080337 scopus 로고    scopus 로고
    • Characterization of a second member of the sentrin family of ubiquitin-like proteins
    • Kamitani, T., Kito, K., Nguyen, H.P., Fukuda-Kamitani, T., and Yeh, E.T. (1998a). Characterization of a second member of the sentrin family of ubiquitin-like proteins. J. Biol. Chem. 273, 11349-11353.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11349-11353
    • Kamitani, T.1    Kito, K.2    Nguyen, H.P.3    Fukuda-Kamitani, T.4    Yeh, E.T.5
  • 8
    • 15644368249 scopus 로고    scopus 로고
    • Covalent modification of PML by the sentrin family of ubiquitin-like proteins
    • Kamitani, T., Nguyen, H.P., Kito, K., Fukuda-Kamitani, T., and Yeh, E.T. (1998b). Covalent modification of PML by the sentrin family of ubiquitin-like proteins. J. Biol. Chem. 273, 3117-3120.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3117-3120
    • Kamitani, T.1    Nguyen, H.P.2    Kito, K.3    Fukuda-Kamitani, T.4    Yeh, E.T.5
  • 9
    • 0032568321 scopus 로고    scopus 로고
    • Histone-GFP fusion protein enables sensitive analysis of chromosome dynamics in living mammalian cells
    • Kanda, T., Sullivan, K.F., and Wahl, G.M. (1998). Histone-GFP fusion protein enables sensitive analysis of chromosome dynamics in living mammalian cells. Curr. Biol. 8, 377-385.
    • (1998) Curr. Biol. , vol.8 , pp. 377-385
    • Kanda, T.1    Sullivan, K.F.2    Wahl, G.M.3
  • 10
  • 11
    • 0037169534 scopus 로고    scopus 로고
    • Nucleolar delocalization of human topoisomerase I in response to topotecan correlates with sumoylation of the protein
    • Mo, Y.Y., Yu, Y., Shen, Z., and Beck, W.T. (2002). Nucleolar delocalization of human topoisomerase I in response to topotecan correlates with sumoylation of the protein. J. Biol. Chem. 277, 2958-2964.
    • (2002) J. Biol. Chem. , vol.277 , pp. 2958-2964
    • Mo, Y.Y.1    Yu, Y.2    Shen, Z.3    Beck, W.T.4
  • 12
    • 0037498052 scopus 로고    scopus 로고
    • Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus
    • Muller, S., Matunis, M.J., and Dejean, A. (1998). Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus. EMBO J. 17, 61-70.
    • (1998) EMBO J. , vol.17 , pp. 61-70
    • Muller, S.1    Matunis, M.J.2    Dejean, A.3
  • 13
    • 0034611785 scopus 로고    scopus 로고
    • High mobility of proteins in the mammalian cell nucleus
    • Phair, R.D., and Misteli, T. (2000). High mobility of proteins in the mammalian cell nucleus. Nature 404, 604-609.
    • (2000) Nature , vol.404 , pp. 604-609
    • Phair, R.D.1    Misteli, T.2
  • 14
    • 0037131273 scopus 로고    scopus 로고
    • Sumoylation of topoisomerase I is involved in its partitioning between nucleoli and nucleoplasm and its clearing from nucleoli in response to camptothecin
    • Rallabhandi, P., Hashimoto, K., Mo, Y.Y., Beck, W.T., Moitra, P.K., and D'Arpa, P. (2002). Sumoylation of topoisomerase I is involved in its partitioning between nucleoli and nucleoplasm and its clearing from nucleoli in response to camptothecin. J. Biol. Chem. 277, 40020-40026.
    • (2002) J. Biol. Chem. , vol.277 , pp. 40020-40026
    • Rallabhandi, P.1    Hashimoto, K.2    Mo, Y.Y.3    Beck, W.T.4    Moitra, P.K.5    D'Arpa, P.6
  • 15
    • 0029786753 scopus 로고    scopus 로고
    • Direct and indirect association of the small GTPase ran with nuclear pore proteins and soluble transport factors: Studies in Xenopus laevis egg extracts
    • Saitoh, H., Cooke, C.A., Burgess, W.H., Earnshaw, W.C., and Dasso, M. (1996). Direct and indirect association of the small GTPase ran with nuclear pore proteins and soluble transport factors: studies in Xenopus laevis egg extracts. Mol. Biol. Cell 7, 1319-1334.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1319-1334
    • Saitoh, H.1    Cooke, C.A.2    Burgess, W.H.3    Earnshaw, W.C.4    Dasso, M.5
  • 16
    • 0034054669 scopus 로고    scopus 로고
    • Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3
    • Saitoh, H., and Hinchey, J. (2000). Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3. J. Biol. Chem. 275, 6252-6258.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6252-6258
    • Saitoh, H.1    Hinchey, J.2
  • 17
  • 19
    • 0344736804 scopus 로고    scopus 로고
    • Pds5p regulates the maintenance of sister chromatid cohesion and is sumoylated to promote the dissolution of cohesion
    • Stead, K., Aguilar, C., Hartman, T., Drexel, M., Meluh, P., and Guacci, V. (2003). Pds5p regulates the maintenance of sister chromatid cohesion and is sumoylated to promote the dissolution of cohesion. J. Cell Biol. 163, 729-741.
    • (2003) J. Cell Biol. , vol.163 , pp. 729-741
    • Stead, K.1    Aguilar, C.2    Hartman, T.3    Drexel, M.4    Meluh, P.5    Guacci, V.6
  • 20
    • 0033037274 scopus 로고    scopus 로고
    • PIC-1/SUMO-1-modified PML-retinoic acid receptor alpha mediates arsenic trioxide-induced apoptosis in acute promyelocytic leukemia
    • Sternsdorf, T., Puccetti, E., Jensen, K., Hoelzer, D., Will, H., Ottmann, O.G., and Ruthardt, M. (1999). PIC-1/SUMO-1-modified PML-retinoic acid receptor alpha mediates arsenic trioxide-induced apoptosis in acute promyelocytic leukemia. Mol. Cell. Biol. 19, 5170-5178.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5170-5178
    • Sternsdorf, T.1    Puccetti, E.2    Jensen, K.3    Hoelzer, D.4    Will, H.5    Ottmann, O.G.6    Ruthardt, M.7
  • 21
    • 0035004370 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae SMT4 encodes an evolutionarily conserved protease with a role in chromosome condensation regulation
    • Strunnikov, A.V., Aravind, L., and Koonin, E.V. (2001). Saccharomyces cerevisiae SMT4 encodes an evolutionarily conserved protease with a role in chromosome condensation regulation. Genetics 158, 95-107.
    • (2001) Genetics , vol.158 , pp. 95-107
    • Strunnikov, A.V.1    Aravind, L.2    Koonin, E.V.3
  • 23
    • 0033508431 scopus 로고    scopus 로고
    • Characterization of a fission yeast SUMO-1 homologue, pmt3p, required for multiple nuclear events, including the control of telomere length and chromosome segregation
    • Tanaka, K., Nishide, J., Okazaki, K., Kato, H., Niwa, O., Nakagawa, T., Matsuda, H., Kawamukai, M., and Murakami, Y. (1999). Characterization of a fission yeast SUMO-1 homologue, pmt3p, required for multiple nuclear events, including the control of telomere length and chromosome segregation. Mol. Cell. Biol. 19, 8660-8672.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8660-8672
    • Tanaka, K.1    Nishide, J.2    Okazaki, K.3    Kato, H.4    Niwa, O.5    Nakagawa, T.6    Matsuda, H.7    Kawamukai, M.8    Murakami, Y.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.