메뉴 건너뛰기




Volumn 36, Issue 5, 2008, Pages 843-847

Do F-box proteins with a C-terminal domain homologous with the tobacco lectin play a role in protein degradation in plants?

Author keywords

F box protein; Lectin; N glycan; Nictaba; Protein degradation; Ubiquitin

Indexed keywords

CULLIN; F BOX NICTABA PROTEIN; F BOX PROTEIN; LECTIN; MANNOSE; PROTEASOME; PROTEIN FBS; S PHASE KINASE ASSOCIATED PROTEIN; S PHASE KINASE ASSOCIATED PROTEIN 1; UBIQUITIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; VEGETABLE PROTEIN;

EID: 53849102959     PISSN: 03005127     EISSN: None     Source Type: Journal    
DOI: 10.1042/BST0360843     Document Type: Conference Paper
Times cited : (29)

References (31)
  • 1
    • 9744227183 scopus 로고    scopus 로고
    • Ubiquitin: Structures, functions, mechanisms
    • Pickart, C.M. and Eddins, M.J. (2004) Ubiquitin: structures, functions, mechanisms. Biochim. Biophys. Acta 1695, 55-72
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 55-72
    • Pickart, C.M.1    Eddins, M.J.2
  • 2
    • 3242665372 scopus 로고    scopus 로고
    • The ubiquitin 26S proteasome proteolytic pathway
    • Smalle, J. and Vierstra, R.D. (2004) The ubiquitin 26S proteasome proteolytic pathway. Annu. Rev. Plant Biol. 55, 555-590
    • (2004) Annu. Rev. Plant Biol , vol.55 , pp. 555-590
    • Smalle, J.1    Vierstra, R.D.2
  • 3
    • 17444420139 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway and plant development
    • Moon, J., Parry, G. and Estelle, M. (2004) The ubiquitin-proteasome pathway and plant development. Plant Cell 16, 3181-3195
    • (2004) Plant Cell , vol.16 , pp. 3181-3195
    • Moon, J.1    Parry, G.2    Estelle, M.3
  • 4
    • 18044364830 scopus 로고    scopus 로고
    • Post-translational regulation in plants employing a diverse set of polypeptide tags
    • Downes, B.P. and Vierstra, R.D. (2005) Post-translational regulation in plants employing a diverse set of polypeptide tags. Biochem. Soc. Trans. 33, 393-399
    • (2005) Biochem. Soc. Trans , vol.33 , pp. 393-399
    • Downes, B.P.1    Vierstra, R.D.2
  • 5
    • 34250897234 scopus 로고    scopus 로고
    • Ubiquitin, hormones and biotic stress in plants
    • Dreher, K. and Callis, J. (2007) Ubiquitin, hormones and biotic stress in plants. Ann. Bot. 99, 787-822
    • (2007) Ann. Bot , vol.99 , pp. 787-822
    • Dreher, K.1    Callis, J.2
  • 6
    • 0037712997 scopus 로고    scopus 로고
    • The ubiquitin/26S proteasome pathway, the complex last chapter in the life of many plant proteins
    • Vierstra, R.D. (2003) The ubiquitin/26S proteasome pathway, the complex last chapter in the life of many plant proteins. Trends Plant Sci. 8, 135-142
    • (2003) Trends Plant Sci , vol.8 , pp. 135-142
    • Vierstra, R.D.1
  • 8
    • 33746690468 scopus 로고    scopus 로고
    • The F-box protein family
    • Kipreos, E.T. and Pagano, M. (2000) The F-box protein family. Genome Biol. 1, 1-7
    • (2000) Genome Biol , vol.1 , pp. 1-7
    • Kipreos, E.T.1    Pagano, M.2
  • 9
    • 11244351579 scopus 로고    scopus 로고
    • Function and regulation of cullin-RING ubiquitin ligases
    • Petroski, M.D. and Deshaies, R.J. (2005) Function and regulation of cullin-RING ubiquitin ligases. Nat. Rev. Mol. Cell Biol. 6, 9-20
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 9-20
    • Petroski, M.D.1    Deshaies, R.J.2
  • 11
    • 0033279836 scopus 로고    scopus 로고
    • SCF and cullin/RING H2-based ubiquitin ligases
    • Deshaies, R.J. (1999) SCF and cullin/RING H2-based ubiquitin ligases. Annu. Rev. Cell Dev. Biol. 15, 435-467
    • (1999) Annu. Rev. Cell Dev. Biol , vol.15 , pp. 435-467
    • Deshaies, R.J.1
  • 13
    • 0030602813 scopus 로고    scopus 로고
    • SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box
    • Bai, C., Sen, P., Hofmann, K., Ma, L., Goebl, M., Harper, J.M. and Elledge, S.J. (1996) SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box. Cell 86, 263-274
    • (1996) Cell , vol.86 , pp. 263-274
    • Bai, C.1    Sen, P.2    Hofmann, K.3    Ma, L.4    Goebl, M.5    Harper, J.M.6    Elledge, S.J.7
  • 15
    • 4444318673 scopus 로고    scopus 로고
    • The SCF ubiquitin ligaser insights into a molecular machine
    • Cardozo, T. and Pagano, M. (2004) The SCF ubiquitin ligaser insights into a molecular machine. Nat. Rev. Mol. Cell Biol. 5, 739-751
    • (2004) Nat. Rev. Mol. Cell Biol , vol.5 , pp. 739-751
    • Cardozo, T.1    Pagano, M.2
  • 17
    • 0242321836 scopus 로고    scopus 로고
    • Fbs2 is a new member of the E3 ubiquitin ligase family that recognizes sugar chains
    • Yoshida, Y., Tokunaga, F., Chiba, T., Iwai, K., Tanaka, K. and Tai, T. (2003) Fbs2 is a new member of the E3 ubiquitin ligase family that recognizes sugar chains. J. Biol. Chem. 278, 43877-43884
    • (2003) J. Biol. Chem , vol.278 , pp. 43877-43884
    • Yoshida, Y.1    Tokunaga, F.2    Chiba, T.3    Iwai, K.4    Tanaka, K.5    Tai, T.6
  • 18
    • 45149112519 scopus 로고    scopus 로고
    • Diversity in tissue expression, substrate binding and SCF complex formation for a lectin family of ubiquitin ligases
    • Glenn, K.A., Nelson, R.F., Wen, H.M., Mallinger, A.J. and Paulson, H.L. (2008) Diversity in tissue expression, substrate binding and SCF complex formation for a lectin family of ubiquitin ligases. J. Biol. Chem. 283, 12717-12729
    • (2008) J. Biol. Chem , vol.283 , pp. 12717-12729
    • Glenn, K.A.1    Nelson, R.F.2    Wen, H.M.3    Mallinger, A.J.4    Paulson, H.L.5
  • 19
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked sugars in the endoplasmic reticulum
    • Helenius, A. and Aelbi, M. (2004) Roles of N-linked sugars in the endoplasmic reticulum. Annu. Rev. Biochem. 73, 1019-1049
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aelbi, M.2
  • 21
    • 18244371937 scopus 로고    scopus 로고
    • Thermodynamic analysis of interactions between Winked sugar chains and F-box protein Fbs1
    • Hagihara, S., Totan, K., Matsuo, I. and Ito, Y. (2005) Thermodynamic analysis of interactions between Winked sugar chains and F-box protein Fbs1. J. Med. Chem. 48, 3126-3129
    • (2005) J. Med. Chem , vol.48 , pp. 3126-3129
    • Hagihara, S.1    Totan, K.2    Matsuo, I.3    Ito, Y.4
  • 23
    • 16844369621 scopus 로고    scopus 로고
    • Glycoprotein-specific ubiquitin ligases recognize N-glycans in unfolded substrates
    • Yoshida, Y., Adachi, E., Fukiya, K., Iwai, K. and Tanaka, K. (2005) Glycoprotein-specific ubiquitin ligases recognize N-glycans in unfolded substrates. EMBO Rep. 6, 239-244
    • (2005) EMBO Rep , vol.6 , pp. 239-244
    • Yoshida, Y.1    Adachi, E.2    Fukiya, K.3    Iwai, K.4    Tanaka, K.5
  • 24
    • 0037143725 scopus 로고    scopus 로고
    • The F-box subunit of the SCF E3 complex is encoded by a diverse superfamily of genes in Arabidopsis
    • Gagne, J.M., Downes, B.P., Shiu, S.-H., Durski, A.M. and Vierstra, R.D. (2002) The F-box subunit of the SCF E3 complex is encoded by a diverse superfamily of genes in Arabidopsis. Proc. Natl. Acad. Sci. U.S.A. 99, 11519-11524
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 11519-11524
    • Gagne, J.M.1    Downes, B.P.2    Shiu, S.-H.3    Durski, A.M.4    Vierstra, R.D.5
  • 25
    • 0036809968 scopus 로고    scopus 로고
    • Classification and expression analysis of Arabidopsis F-box-containing protein genes
    • Kuroda, H., Takahashi, N., Shinnada, H., Seki, M., Shinozaki, K. and Matsui, M. (2002) Classification and expression analysis of Arabidopsis F-box-containing protein genes. Plant Cell Physiol. 43, 1073-1085
    • (2002) Plant Cell Physiol , vol.43 , pp. 1073-1085
    • Kuroda, H.1    Takahashi, N.2    Shinnada, H.3    Seki, M.4    Shinozaki, K.5    Matsui, M.6
  • 27
    • 34249819663 scopus 로고    scopus 로고
    • F-box proteins in rice: Genome-wide analysis, classification, temporal and spatial gene expression during panicle and seed development, and regulation by light and abiotic stress
    • Jain, M., Nijhawan, A., Arora, R., Agarwal, P., Ray, S., Sharma, P., Kapoor, S., Tyagi, A.K. and Khurana, J. (2007) F-box proteins in rice: genome-wide analysis, classification, temporal and spatial gene expression during panicle and seed development, and regulation by light and abiotic stress. Plant Physiol. 143, 1467-1483
    • (2007) Plant Physiol , vol.143 , pp. 1467-1483
    • Jain, M.1    Nijhawan, A.2    Arora, R.3    Agarwal, P.4    Ray, S.5    Sharma, P.6    Kapoor, S.7    Tyagi, A.K.8    Khurana, J.9
  • 28
    • 0036616781 scopus 로고    scopus 로고
    • Jasmonic acid methyl ester induces the synthesis of a cytoplasmic/nuclear chitooligosaccharide-binding lectin in tobacco leaves
    • Chen, Y., Peumans, W.J., Hause, B., Bras, J., Kumar, M., Proost, P., Barre, A., Rougé, P. and Van Damme, E.J.M. (2002) Jasmonic acid methyl ester induces the synthesis of a cytoplasmic/nuclear chitooligosaccharide-binding lectin in tobacco leaves. FASEB J. 16, 905-907
    • (2002) FASEB J , vol.16 , pp. 905-907
    • Chen, Y.1    Peumans, W.J.2    Hause, B.3    Bras, J.4    Kumar, M.5    Proost, P.6    Barre, A.7    Rougé, P.8    Van Damme, E.J.M.9
  • 29
    • 33751083838 scopus 로고    scopus 로고
    • Localization and in vitro binding studies suggest that the cytoplasmic/nuclear tobacco lectin can interact in situ with high-mannose and complex N-glycans
    • Lannoo, N., Peumans, W.J., Van Pamel, E., Alvarez, R., Xiong, T.-C., Hause, G., Mazars, C. and Van Damme, E.J.M. (2006) Localization and in vitro binding studies suggest that the cytoplasmic/nuclear tobacco lectin can interact in situ with high-mannose and complex N-glycans. FEBS Lett. 580, 6329-6337
    • (2006) FEBS Lett , vol.580 , pp. 6329-6337
    • Lannoo, N.1    Peumans, W.J.2    Van Pamel, E.3    Alvarez, R.4    Xiong, T.-C.5    Hause, G.6    Mazars, C.7    Van Damme, E.J.M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.