메뉴 건너뛰기




Volumn 579, Issue 18, 2005, Pages 3885-3890

Arabidopsis ubiquitin-specific protease 6 (AtUBP6) interacts with calmodulin

Author keywords

Calmodulin; Calmodulin binding protein; Deubiquitination; Ubiquitin proteasome pathway; Ubiquitin specific protease

Indexed keywords

ARABIDOPSIS CALMODULIN2; ARABIDOPSIS UBIQUITIN SPECIFIC PROTEASE 6; CALCIUM ION; CALMODULIN DERIVATIVE; CANAVANINE; HORSERADISH PEROXIDASE; ISOENZYME; PHOSPHODIESTERASE; PROTEINASE; UBIQUITIN SPECIFIC PROTEASE 6; UNCLASSIFIED DRUG;

EID: 21844436532     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.05.080     Document Type: Article
Times cited : (28)

References (31)
  • 3
    • 0035809014 scopus 로고    scopus 로고
    • Calcium: Silver bullet in signaling
    • A.S.N. Reddy Calcium: silver bullet in signaling Plant Sci. 160 2000 381 404
    • (2000) Plant Sci. , vol.160 , pp. 381-404
    • Reddy, A.S.N.1
  • 4
    • 0034945001 scopus 로고    scopus 로고
    • Calmodulin as a versatile calcium signal transducer in plants
    • W.A. Snedden, and H. Fromm Calmodulin as a versatile calcium signal transducer in plants New Phytol. 151 2001 35 66
    • (2001) New Phytol. , vol.151 , pp. 35-66
    • Snedden, W.A.1    Fromm, H.2
  • 5
    • 0037155689 scopus 로고    scopus 로고
    • Calmodulin in action: Diversity in target recognition and activation mechanisms
    • K.P. Hoeflich, and M. Ikura Calmodulin in action: diversity in target recognition and activation mechanisms Cell 108 2002 739 742
    • (2002) Cell , vol.108 , pp. 739-742
    • Hoeflich, K.P.1    Ikura, M.2
  • 6
    • 0036269779 scopus 로고    scopus 로고
    • Ubiquitination and auxin signaling: A degrading story
    • O. Leyser, and S. Kepinski Ubiquitination and auxin signaling: a degrading story Plant Cell. supplement 2002 S81 S95
    • (2002) Plant Cell.
    • Leyser, O.1    Kepinski, S.2
  • 7
    • 0042572096 scopus 로고    scopus 로고
    • Role of ubiquitination in the regulation of plant defense against pathogens
    • A. Devoto, P.R. Muskett, and K. Shirasu Role of ubiquitination in the regulation of plant defense against pathogens Curr. Opin. Cell. Biol. 6 2003 307 311
    • (2003) Curr. Opin. Cell. Biol. , vol.6 , pp. 307-311
    • Devoto, A.1    Muskett, P.R.2    Shirasu, K.3
  • 8
    • 0141725444 scopus 로고    scopus 로고
    • Modulation of sensitivity and selectivity in plant signaling by proteasomal destabilization
    • P.D. Hare, H.S. Seo, J.-H. Yang, and N.-H. Chua Modulation of sensitivity and selectivity in plant signaling by proteasomal destabilization Curr. Opin. Cell. Biol. 6 2003 453 462
    • (2003) Curr. Opin. Cell. Biol. , vol.6 , pp. 453-462
    • Hare, P.D.1    Seo, H.S.2    Yang, J.-H.3    Chua, N.-H.4
  • 10
    • 0037008512 scopus 로고    scopus 로고
    • Plant development: Regulation by protein degradation
    • H. Hellmann, and M. Estelle Plant development: regulation by protein degradation Science 297 2002 793 797
    • (2002) Science , vol.297 , pp. 793-797
    • Hellmann, H.1    Estelle, M.2
  • 11
    • 0037712997 scopus 로고    scopus 로고
    • The ubiquitin/26S proteasome pathway, the complex last chapter in the life of many plant proteins
    • R.D. Vierstra The ubiquitin/26S proteasome pathway, the complex last chapter in the life of many plant proteins Trend Plant Sci. 8 2003 135 142
    • (2003) Trend Plant Sci. , vol.8 , pp. 135-142
    • Vierstra, R.D.1
  • 12
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • M. Hochstrasser Ubiquitin-dependent protein degradation Annu. Rev. Genet. 30 1996 405 439
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 13
    • 0030660073 scopus 로고    scopus 로고
    • Regulation of ubiquitin-dependent processes by deubiquitinating enzymes
    • K.D. Wilkinson Regulation of ubiquitin-dependent processes by deubiquitinating enzymes FASEB J. 11 1997 1245 1256
    • (1997) FASEB J. , vol.11 , pp. 1245-1256
    • Wilkinson, K.D.1
  • 14
    • 0035209519 scopus 로고    scopus 로고
    • Ubiquitylation in plants: A post-genomic look at a post-translational modification
    • A. Bachmair, M. Novatchkova, T. Potuschak, and F. Eisenhaber Ubiquitylation in plants: a post-genomic look at a post-translational modification Trand Plant Sci. 6 2001 463 470
    • (2001) Trand Plant Sci. , vol.6 , pp. 463-470
    • Bachmair, A.1    Novatchkova, M.2    Potuschak, T.3    Eisenhaber, F.4
  • 15
    • 0034512691 scopus 로고    scopus 로고
    • The ubiquitin-specific protease family from Arabidopsis. AtUBP1 and 2 are required for the resistance to the amino acid analog canavanine
    • N. Yan, J.H. Doelling, T.G. Falbel, A.M. Durski, and R.D. Vierstra The ubiquitin-specific protease family from Arabidopsis. AtUBP1 and 2 are required for the resistance to the amino acid analog canavanine Plant Physiol. 124 2000 1828 1843
    • (2000) Plant Physiol. , vol.124 , pp. 1828-1843
    • Yan, N.1    Doelling, J.H.2    Falbel, T.G.3    Durski, A.M.4    Vierstra, R.D.5
  • 16
    • 0034795089 scopus 로고    scopus 로고
    • The ubiquitin-specific protease UBP14 is essential for early embryo development in Arabidopsis thaliana
    • J.H. Delling, N. Yan, J. Kurepa, J. Walker, and R.D. Vierstra The ubiquitin-specific protease UBP14 is essential for early embryo development in Arabidopsis thaliana Plant J. 27 2001 393 405
    • (2001) Plant J. , vol.27 , pp. 393-405
    • Delling, J.H.1    Yan, N.2    Kurepa, J.3    Walker, J.4    Vierstra, R.D.5
  • 17
    • 0034661392 scopus 로고    scopus 로고
    • Ubiquitin-specific proteases from Arabidopsis thaliana: Cloning of AtUBP5 and analysis of substrate specificity of AtUBP3, AtUBP4, and AtUBP5 using Escherichia coli in vivo and in vitro assays
    • C. Rao-Naik, J.S. Chandler, B. McArdle, and J. Callis Ubiquitin-specific proteases from Arabidopsis thaliana: cloning of AtUBP5 and analysis of substrate specificity of AtUBP3, AtUBP4, and AtUBP5 using Escherichia coli in vivo and in vitro assays Arch. Biochem. Biophys. 379 2000 198 208
    • (2000) Arch. Biochem. Biophys. , vol.379 , pp. 198-208
    • Rao-Naik, C.1    Chandler, J.S.2    McArdle, B.3    Callis, J.4
  • 18
    • 0030751724 scopus 로고    scopus 로고
    • AtUBP3 and AtUBP4 are two closely related Arabidopsis thaliana ubiquitin-specific protease present in the nucleus
    • J. Chandler, B. McArdle, and J. Callis AtUBP3 and AtUBP4 are two closely related Arabidopsis thaliana ubiquitin-specific protease present in the nucleus Mol. Gen. Genet. 255 1997 302 310
    • (1997) Mol. Gen. Genet. , vol.255 , pp. 302-310
    • Chandler, J.1    McArdle, B.2    Callis, J.3
  • 21
    • 0023061735 scopus 로고
    • Recognition and characterization of calmodulin-binding sequences in peptides and proteins
    • S. Erickson-Viitanen, and W.F. DeGrado Recognition and characterization of calmodulin-binding sequences in peptides and proteins Meth. Enzymol. 139 1987 455 478
    • (1987) Meth. Enzymol. , vol.139 , pp. 455-478
    • Erickson-Viitanen, S.1    Degrado, W.F.2
  • 23
    • 0037155853 scopus 로고    scopus 로고
    • Genes encoding calmodulin-binding proteins in the Arabidopsis genome
    • V.S. Reddy, G.S. Ali, and A.S. Reddy Genes encoding calmodulin-binding proteins in the Arabidopsis genome J. Biol. Chem. 277 2002 9840 9852
    • (2002) J. Biol. Chem. , vol.277 , pp. 9840-9852
    • Reddy, V.S.1    Ali, G.S.2    Reddy, A.S.3
  • 25
    • 0035903538 scopus 로고    scopus 로고
    • A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14
    • A. Borodovsky, B.M. Kessler, R. Casagrande, H.S. Overkleeft, K.D. Wilkinson, and H.L. Ploegh A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14 EMBO J. 20 2001 5187 5196
    • (2001) EMBO J. , vol.20 , pp. 5187-5196
    • Borodovsky, A.1    Kessler, B.M.2    Casagrande, R.3    Overkleeft, H.S.4    Wilkinson, K.D.5    Ploegh, H.L.6
  • 26
    • 0033032409 scopus 로고    scopus 로고
    • The Ubp6 family of deubiquitinating enzymes contains a ubiquitin-like domain: Sub
    • A.M. Wyndham, R.T. Baker, and G. Chelvanyagam The Ubp6 family of deubiquitinating enzymes contains a ubiquitin-like domain: Sub Protein Sci. 8 1999 1268 1275
    • (1999) Protein Sci. , vol.8 , pp. 1268-1275
    • Wyndham, A.M.1    Baker, R.T.2    Chelvanyagam, G.3
  • 27
    • 0030945196 scopus 로고    scopus 로고
    • Sequence motifs for calmodulin recognition
    • A.R. Rhoads, and F. Friedberg Sequence motifs for calmodulin recognition FASEB J. 11 1997 331 340
    • (1997) FASEB J. , vol.11 , pp. 331-340
    • Rhoads, A.R.1    Friedberg, F.2
  • 28
    • 0025159272 scopus 로고
    • How calmodulin binds its targets: Sequence independent recognition of amphiphilic alpha-helices
    • K.T. O' Neil, and W.F. DeGrado How calmodulin binds its targets: sequence independent recognition of amphiphilic alpha-helices Trend Biol. Sci. 15 1990 59 64
    • (1990) Trend Biol. Sci. , vol.15 , pp. 59-64
    • Neil, K.T.O.'.1    Degrado, W.F.2
  • 29
    • 0029149085 scopus 로고
    • Molecular and structural basis of target recognition by calmodulin
    • A. Crivici, and M. Ikura Molecular and structural basis of target recognition by calmodulin Annu. Rev. Biophys. Biomol. Struct. 24 1995 85 116
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 85-116
    • Crivici, A.1    Ikura, M.2
  • 30
    • 0034616885 scopus 로고    scopus 로고
    • 2+-free calmodulin and calmodulin damaged by in vitro aging are selectively degraded by 26S proteasomes without ubiquitination
    • 2+-free calmodulin and calmodulin damaged by in vitro aging are selectively degraded by 26S proteasomes without ubiquitination J. Biol. Chem. 275 2000 20295 20301
    • (2000) J. Biol. Chem. , vol.275 , pp. 20295-20301
    • Tarcsa, E.1    Szymanska, G.2    Lecker, S.3    O'Connor, C.M.4    Goldberg, A.L.5
  • 31
    • 8544273285 scopus 로고    scopus 로고
    • Hsp90 enhances degradation of oxidized calmodulin by the 20S proteasome
    • J.F. Whittier, Y. Xiong, M.C. Rechsteiner, and T.C. Squier Hsp90 enhances degradation of oxidized calmodulin by the 20S proteasome J. Biol. Chem. 279 2004 46135 46142
    • (2004) J. Biol. Chem. , vol.279 , pp. 46135-46142
    • Whittier, J.F.1    Xiong, Y.2    Rechsteiner, M.C.3    Squier, T.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.