메뉴 건너뛰기




Volumn 291, Issue 40, 2016, Pages 20976-20992

Analyzing N-terminal arginylation through the use of peptide arrays and degradation assays

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; PEPTIDES;

EID: 84988962992     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M116.747956     Document Type: Article
Times cited : (25)

References (111)
  • 1
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair, A., Finley, D., and Varshavsky, A. (1986) In vivo half-life of a protein is a function of its amino-terminal residue. Science 234, 179-186
    • (1986) Science , vol.234 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 2
    • 0024562943 scopus 로고
    • The degradation signal in a short-lived protein
    • Bachmair, A., and Varshavsky, A. (1989) The degradation signal in a short-lived protein. Cell 56, 1019-1032
    • (1989) Cell , vol.56 , pp. 1019-1032
    • Bachmair, A.1    Varshavsky, A.2
  • 4
    • 27144557281 scopus 로고    scopus 로고
    • The N-end rule pathway as a nitric oxide sensor controlling the levels of multiple regulators
    • Hu, R.-G., Sheng, J., Qi, X., Xu, Z., Takahashi, T. T., and Varshavsky, A. (2005) The N-end rule pathway as a nitric oxide sensor controlling the levels of multiple regulators. Nature 437, 981-986
    • (2005) Nature , vol.437 , pp. 981-986
    • Hu, R.-G.1    Sheng, J.2    Qi, X.3    Xu, Z.4    Takahashi, T.T.5    Varshavsky, A.6
  • 5
    • 77149120798 scopus 로고    scopus 로고
    • N-terminal acetylation of cellular proteins creates specific degradation signals
    • Hwang, C. S., Shemorry, A., and Varshavsky, A. (2010) N-terminal acetylation of cellular proteins creates specific degradation signals. Science 327, 973-977
    • (2010) Science , vol.327 , pp. 973-977
    • Hwang, C.S.1    Shemorry, A.2    Varshavsky, A.3
  • 6
    • 84892802083 scopus 로고    scopus 로고
    • The N-terminal methionine of cellular proteins as a degradation signal
    • Kim, H. K., Kim, R. R., Oh, J. H., Cho, H., Varshavsky, A., and Hwang, C. S. (2014) The N-terminal methionine of cellular proteins as a degradation signal. Cell 156, 158-169
    • (2014) Cell , vol.156 , pp. 158-169
    • Kim, H.K.1    Kim, R.R.2    Oh, J.H.3    Cho, H.4    Varshavsky, A.5    Hwang, C.S.6
  • 7
    • 84908478523 scopus 로고    scopus 로고
    • The eukaryotic N-end rule pathway: Conserved mechanisms and diverse functions
    • Gibbs, D. J., Bacardit, J., Bachmair, A., and Holdsworth, M. J. (2014) The eukaryotic N-end rule pathway: conserved mechanisms and diverse functions. Trends Cell Biol. 24, 603-611
    • (2014) Trends Cell Biol. , vol.24 , pp. 603-611
    • Gibbs, D.J.1    Bacardit, J.2    Bachmair, A.3    Holdsworth, M.J.4
  • 9
    • 79960683356 scopus 로고    scopus 로고
    • The N-end rule pathway and regulation by proteolysis
    • Varshavsky, A. (2011) The N-end rule pathway and regulation by proteolysis. Protein Sci. 20, 1298-1345
    • (2011) Protein Sci. , vol.20 , pp. 1298-1345
    • Varshavsky, A.1
  • 10
    • 84961757512 scopus 로고    scopus 로고
    • The N-End rule: The beginning determines the end
    • Eldeeb, M., and Fahlman, R. (2016) The N-End rule: the beginning determines the end. Protein Pept. Lett. 23, 343-348
    • (2016) Protein Pept. Lett. , vol.23 , pp. 343-348
    • Eldeeb, M.1    Fahlman, R.2
  • 11
    • 84855198546 scopus 로고    scopus 로고
    • The N-end rule pathway: From recognition by N-recognins to destruction by AAA+ proteases
    • Dougan, D. A., Micevski, D., and Truscott, K. N. (2012) The N-end rule pathway: from recognition by N-recognins to destruction by AAA+ proteases. Biochim. Biophys. Acta 1823, 83-91
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 83-91
    • Dougan, D.A.1    Micevski, D.2    Truscott, K.N.3
  • 12
    • 57149115173 scopus 로고    scopus 로고
    • Discovery of cellular regulation by protein degradation
    • Varshavsky, A. (2008) Discovery of cellular regulation by protein degradation. J. Biol. Chem. 283, 34469-34489
    • (2008) J. Biol. Chem. , vol.283 , pp. 34469-34489
    • Varshavsky, A.1
  • 13
    • 84964929936 scopus 로고    scopus 로고
    • N-terminal acetylation-targeted N-end rule proteolytic system: The Ac/N-end rule pathway
    • Lee, K. E., Heo, J. E., Kim, J. M., and Hwang, C. S. (2016) N-terminal acetylation-targeted N-end rule proteolytic system: the Ac/N-end rule pathway. Mol. Cells 39, 169-178
    • (2016) Mol. Cells , vol.39 , pp. 169-178
    • Lee, K.E.1    Heo, J.E.2    Kim, J.M.3    Hwang, C.S.4
  • 14
    • 0034213352 scopus 로고    scopus 로고
    • Peptides accelerate their uptake by activating a ubiquitin-dependent proteolytic pathway
    • Turner, G. C., Du, F., and Varshavsky, A. (2000) Peptides accelerate their uptake by activating a ubiquitin-dependent proteolytic pathway. Nature 405, 579-583
    • (2000) Nature , vol.405 , pp. 579-583
    • Turner, G.C.1    Du, F.2    Varshavsky, A.3
  • 15
    • 0037195103 scopus 로고    scopus 로고
    • Pairs of dipeptides synergistically activate the binding of substrate by ubiquitin ligase through dissociation of its autoinhibitory domain
    • Du, F., Navarro-Garcia, F., Xia, Z., Tasaki, T., and Varshavsky, A. (2002) Pairs of dipeptides synergistically activate the binding of substrate by ubiquitin ligase through dissociation of its autoinhibitory domain. Proc. Natl. Acad. Sci. U.S.A. 99, 14110-14115
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 14110-14115
    • Du, F.1    Navarro-Garcia, F.2    Xia, Z.3    Tasaki, T.4    Varshavsky, A.5
  • 16
    • 60549096291 scopus 로고    scopus 로고
    • Two proteolytic pathways regulate DNA repair by cotargeting the Mgt1 alkylguanine transferase
    • Hwang, C. S., Shemorry, A., and Varshavsky, A. (2009) Two proteolytic pathways regulate DNA repair by cotargeting the Mgt1 alkylguanine transferase. Proc. Natl. Acad. Sci. U.S.A. 106, 2142-2147
    • (2009) Proc. Natl. Acad. Sci. U.S.A , vol.106 , pp. 2142-2147
    • Hwang, C.S.1    Shemorry, A.2    Varshavsky, A.3
  • 17
    • 75749101057 scopus 로고    scopus 로고
    • Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1
    • Heck, J. W., Cheung, S. K., and Hampton, R. Y. (2010) Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1. Proc. Natl. Acad. Sci. U.S.A. 107, 1106-1111
    • (2010) Proc. Natl. Acad. Sci. U.S.A , vol.107 , pp. 1106-1111
    • Heck, J.W.1    Cheung, S.K.2    Hampton, R.Y.3
  • 18
    • 57049182407 scopus 로고    scopus 로고
    • Degradation of misfolded proteins in the cytoplasm by the ubiquitin ligase Ubr1
    • Eisele, F., and Wolf, D. H. (2008) Degradation of misfolded proteins in the cytoplasm by the ubiquitin ligase Ubr1. FEBS Lett. 582, 4143-4146
    • (2008) FEBS Lett. , vol.582 , pp. 4143-4146
    • Eisele, F.1    Wolf, D.H.2
  • 19
    • 0033231281 scopus 로고    scopus 로고
    • Degradation signals in the lysine-asparagine sequence space
    • Suzuki, T., and Varshavsky, A. (1999) Degradation signals in the lysine-asparagine sequence space. EMBO J. 18, 6017-6026
    • (1999) EMBO J , vol.18 , pp. 6017-6026
    • Suzuki, T.1    Varshavsky, A.2
  • 20
    • 84896032345 scopus 로고    scopus 로고
    • Paradigms of protein degradation by the proteasome
    • Inobe, T., and Matouschek, A. (2014) Paradigms of protein degradation by the proteasome. Curr. Opin. Struct. Biol. 24, 156-164
    • (2014) Curr. Opin. Struct. Biol. , vol.24 , pp. 156-164
    • Inobe, T.1    Matouschek, A.2
  • 22
    • 33947713897 scopus 로고    scopus 로고
    • The N-end rule pathway of regulated proteolysis: Prokaryotic and eukaryotic strategies
    • Mogk, A., Schmidt, R., and Bukau, B. (2007) The N-end rule pathway of regulated proteolysis: prokaryotic and eukaryotic strategies. Trends Cell Biol. 17, 165-172
    • (2007) Trends Cell Biol. , vol.17 , pp. 165-172
    • Mogk, A.1    Schmidt, R.2    Bukau, B.3
  • 23
    • 84907220044 scopus 로고    scopus 로고
    • Remodeling of a delivery complex allows ClpS-mediated degradation of N-degron substrates
    • Rivera-Rivera, I., Román-Hernández, G., Sauer, R. T., and Baker, T. A. (2014) Remodeling of a delivery complex allows ClpS-mediated degradation of N-degron substrates. Proc. Natl. Acad. Sci. U.S.A. 111, E3853-E3859
    • (2014) Proc. Natl. Acad. Sci. U.S.A , vol.111 , pp. E3853-E3859
    • Rivera-Rivera, I.1    Román-Hernández, G.2    Sauer, R.T.3    Baker, T.A.4
  • 24
    • 84964938224 scopus 로고    scopus 로고
    • Formylmethionine as a degradation signal at the N-termini of bacterial proteins
    • Piatkov, K. I., Vu, T. T., Hwang, C.-S., and Varshavsky, A. (2015) Formylmethionine as a degradation signal at the N-termini of bacterial proteins. Microbial Cell 2, 376-393
    • (2015) Microbial Cell , vol.2 , pp. 376-393
    • Piatkov, K.I.1    Vu, T.T.2    Hwang, C.-S.3    Varshavsky, A.4
  • 25
    • 84885123033 scopus 로고    scopus 로고
    • The N-degradome of Escherichia coli: Limited proteolysis in vivo generates a large pool of proteins bearing N-degrons
    • Humbard, M. A., Surkov, S., De Donatis, G. M., Jenkins, L. M., and Maurizi, M. R. (2013) The N-degradome of Escherichia coli: limited proteolysis in vivo generates a large pool of proteins bearing N-degrons. J. Biol. Chem. 288, 28913-28924
    • (2013) J. Biol. Chem. , vol.288 , pp. 28913-28924
    • Humbard, M.A.1    Surkov, S.2    De Donatis, G.M.3    Jenkins, L.M.4    Maurizi, M.R.5
  • 26
    • 33644786997 scopus 로고    scopus 로고
    • Aminoacyl-transferases and the N-end rule pathway of prokaryotic/eukaryotic specificity in a human pathogen
    • Graciet, E., Hu, R. G., Piatkov, K., Rhee, J. H., Schwarz, E. M., and Varshavsky, A. (2006) Aminoacyl-transferases and the N-end rule pathway of prokaryotic/eukaryotic specificity in a human pathogen. Proc. Natl. Acad. Sci. U.S.A. 103, 3078-3083
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 3078-3083
    • Graciet, E.1    Hu, R.G.2    Piatkov, K.3    Rhee, J.H.4    Schwarz, E.M.5    Varshavsky, A.6
  • 30
    • 0028964284 scopus 로고
    • A recognition component of the ubiquitin system is required for peptide transport in Saccharomyces cerevisiae
    • Alagramam, K., Naider, F., and Becker, J. M. (1995) A recognition component of the ubiquitin system is required for peptide transport in Saccharomyces cerevisiae. Mol. Microbiol. 15, 225-234
    • (1995) Mol. Microbiol. , vol.15 , pp. 225-234
    • Alagramam, K.1    Naider, F.2    Becker, J.M.3
  • 31
    • 0032472322 scopus 로고    scopus 로고
    • The N-end rule pathway controls the import of peptides through degradation of a transcriptional repressor
    • Byrd, C., Turner, G. C., and Varshavsky, A. (1998) The N-end rule pathway controls the import of peptides through degradation of a transcriptional repressor. EMBO J. 17, 269-277
    • (1998) EMBO J , vol.17 , pp. 269-277
    • Byrd, C.1    Turner, G.C.2    Varshavsky, A.3
  • 32
    • 58049196794 scopus 로고    scopus 로고
    • Regulation of peptide import through phosphorylation of Ubr1, the ubiquitin ligase of the N-end rule pathway
    • Hwang, C. S., and Varshavsky, A. (2008) Regulation of peptide import through phosphorylation of Ubr1, the ubiquitin ligase of the N-end rule pathway. Proc. Natl. Acad. Sci. U.S.A. 105, 19188-19193
    • (2008) Proc. Natl. Acad. Sci. U.S.A , vol.105 , pp. 19188-19193
    • Hwang, C.S.1    Varshavsky, A.2
  • 33
    • 84872105177 scopus 로고    scopus 로고
    • The type-2 N-end rule peptide recognition activity of Ubr11 ubiquitin ligase is required for the expression of peptide transporters
    • Kitamura, K., and Fujiwara, H. (2013) The type-2 N-end rule peptide recognition activity of Ubr11 ubiquitin ligase is required for the expression of peptide transporters. FEBS Lett. 587, 214-219
    • (2013) FEBS Lett. , vol.587 , pp. 214-219
    • Kitamura, K.1    Fujiwara, H.2
  • 34
    • 53049096418 scopus 로고    scopus 로고
    • Substrate-binding sites of UBR1, the ubiquitin ligase of the N-end rule pathway
    • Xia, Z., Webster, A., Du, F., Piatkov, K., Ghislain, M., and Varshavsky, A. (2008) Substrate-binding sites of UBR1, the ubiquitin ligase of the N-end rule pathway. J. Biol. Chem. 283, 24011-24028
    • (2008) J. Biol. Chem. , vol.283 , pp. 24011-24028
    • Xia, Z.1    Webster, A.2    Du, F.3    Piatkov, K.4    Ghislain, M.5    Varshavsky, A.6
  • 35
    • 57649223684 scopus 로고    scopus 로고
    • Amino acids induce peptide uptake via accelerated degradation of CUP9, the transcriptional repressor of the PTR2 peptide transporter
    • Xia, Z., Turner, G. C., Hwang, C.-S., Byrd, C., and Varshavsky, A. (2008) Amino acids induce peptide uptake via accelerated degradation of CUP9, the transcriptional repressor of the PTR2 peptide transporter. J. Biol. Chem. 283, 28958-28968
    • (2008) J. Biol. Chem. , vol.283 , pp. 28958-28968
    • Xia, Z.1    Turner, G.C.2    Hwang, C.-S.3    Byrd, C.4    Varshavsky, A.5
  • 36
    • 84878195272 scopus 로고    scopus 로고
    • Control of protein quality and stoichiometries by N-terminal acetylation and the N-end rule pathway
    • Shemorry, A., Hwang, C. S., and Varshavsky, A. (2013) Control of protein quality and stoichiometries by N-terminal acetylation and the N-end rule pathway. Mol. Cell 50, 540-551
    • (2013) Mol. Cell , vol.50 , pp. 540-551
    • Shemorry, A.1    Hwang, C.S.2    Varshavsky, A.3
  • 37
    • 84863615329 scopus 로고    scopus 로고
    • A network of ubiquitin ligases is important for the dynamics of misfolded protein aggregates in yeast
    • Theodoraki, M. A., Nillegoda, N. B., Saini, J., and Caplan, A. J. (2012) A network of ubiquitin ligases is important for the dynamics of misfolded protein aggregates in yeast. J. Biol. Chem. 287, 23911-23922
    • (2012) J. Biol. Chem. , vol.287 , pp. 23911-23922
    • Theodoraki, M.A.1    Nillegoda, N.B.2    Saini, J.3    Caplan, A.J.4
  • 38
    • 84871313656 scopus 로고    scopus 로고
    • The yeast Ubr1 ubiquitin ligase participates in a prominent pathway that targets cytosolic thermosensitive mutants for degradation
    • Khosrow-Khavar, F., Fang, N. N., Ng, A. H. M., Winget, J. M., Comyn, S. A., and Mayor, T. (2012) The yeast Ubr1 ubiquitin ligase participates in a prominent pathway that targets cytosolic thermosensitive mutants for degradation. G3 Genes 2, 619-628
    • (2012) G3 Genes , vol.2 , pp. 619-628
    • Khosrow-Khavar, F.1    Fang, N.N.2    Ng, A.H.M.3    Winget, J.M.4    Comyn, S.A.5    Mayor, T.6
  • 39
    • 84865549121 scopus 로고    scopus 로고
    • Biosynthetic mode can determine the mechanism of protein quality control
    • Prasad, R., Kawaguchi, S., and Ng, D. T. (2012) Biosynthetic mode can determine the mechanism of protein quality control. Biochem. Biophys. Res. Commun. 425, 689-695
    • (2012) Biochem. Biophys. Res. Commun. , vol.425 , pp. 689-695
    • Prasad, R.1    Kawaguchi, S.2    Ng, D.T.3
  • 40
    • 81355127301 scopus 로고    scopus 로고
    • UBR1 promotes protein kinase quality control and sensitizes cells to Hsp90 inhibition
    • Sultana, R., Theodoraki, M. A., and Caplan, A. J. (2012) UBR1 promotes protein kinase quality control and sensitizes cells to Hsp90 inhibition. Exp. Cell Res. 18, 53-60
    • (2012) Exp. Cell Res. , vol.18 , pp. 53-60
    • Sultana, R.1    Theodoraki, M.A.2    Caplan, A.J.3
  • 42
    • 84887453820 scopus 로고    scopus 로고
    • PINK1 is degraded through the N-end rule pathway
    • Yamano, K., and Youle, R. J. (2013) PINK1 is degraded through the N-end rule pathway. Autophagy 9, 1758-1769
    • (2013) Autophagy , vol.9 , pp. 1758-1769
    • Yamano, K.1    Youle, R.J.2
  • 43
    • 84863571174 scopus 로고    scopus 로고
    • The N-end rule pathway counteracts cell death by destroying proapoptotic protein fragments
    • Piatkov, K. I., Brower, C. S., and Varshavsky, A. (2012) The N-end rule pathway counteracts cell death by destroying proapoptotic protein fragments. Proc. Natl. Acad. Sci. U.S.A. 109, E1839-E1847
    • (2012) Proc. Natl. Acad. Sci. U.S.A , vol.109 , pp. E1839-E1847
    • Piatkov, K.I.1    Brower, C.S.2    Varshavsky, A.3
  • 44
    • 84876832401 scopus 로고    scopus 로고
    • Neurodegeneration-associated protein fragments as short-lived substrates of the N-end rule pathway
    • Brower, C. S., Piatkov, K. I., and Varshavsky, A. (2013) Neurodegeneration-associated protein fragments as short-lived substrates of the N-end rule pathway. Mol. Cell 50, 161-171
    • (2013) Mol. Cell , vol.50 , pp. 161-171
    • Brower, C.S.1    Piatkov, K.I.2    Varshavsky, A.3
  • 45
    • 84863249152 scopus 로고    scopus 로고
    • The C-terminal proteolytic fragment of the breast cancer susceptibility type 1 protein (BRCA1) is degraded by the N-end rule pathway
    • Xu, Z., Payoe, R., and Fahlman, R. P. (2012) The C-terminal proteolytic fragment of the breast cancer susceptibility type 1 protein (BRCA1) is degraded by the N-end rule pathway. J. Biol. Chem. 287, 7495-7502
    • (2012) J. Biol. Chem. , vol.287 , pp. 7495-7502
    • Xu, Z.1    Payoe, R.2    Fahlman, R.P.3
  • 46
    • 84901218392 scopus 로고    scopus 로고
    • The anti-apoptotic form of tyrosine kinase Lyn that is generated by proteolysis is degraded by the N-end rule pathway
    • Eldeeb, M. A., and Fahlman, R. P. (2014) The anti-apoptotic form of tyrosine kinase Lyn that is generated by proteolysis is degraded by the N-end rule pathway. Oncotarget 5, 2714-2722
    • (2014) Oncotarget , vol.5 , pp. 2714-2722
    • Eldeeb, M.A.1    Fahlman, R.P.2
  • 47
    • 0023236126 scopus 로고
    • The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme
    • Jentsch, S., McGrath, J. P., and Varshavsky, A. (1987) The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme. Nature 329, 131-134
    • (1987) Nature , vol.329 , pp. 131-134
    • Jentsch, S.1    McGrath, J.P.2    Varshavsky, A.3
  • 48
    • 0035912183 scopus 로고    scopus 로고
    • Degradation of a cohesin subunit by the N-end rule pathway is essential for chromosome stability
    • Rao, H., Uhlmann, F., Nasmyth, K., and Varshavsky, A. (2001) Degradation of a cohesin subunit by the N-end rule pathway is essential for chromosome stability. Nature 410, 955-959
    • (2001) Nature , vol.410 , pp. 955-959
    • Rao, H.1    Uhlmann, F.2    Nasmyth, K.3    Varshavsky, A.4
  • 49
    • 84871675699 scopus 로고    scopus 로고
    • The auto-generated fragment of the Usp1 deubiquitylase is a physiological substrate of the N-end rule pathway
    • Piatkov, K. I., Colnaghi, L., Békés, M., Varshavsky, A., and Huang, T. T. (2012) The auto-generated fragment of the Usp1 deubiquitylase is a physiological substrate of the N-end rule pathway. Mol. Cell 48, 926-933
    • (2012) Mol. Cell , vol.48 , pp. 926-933
    • Piatkov, K.I.1    Colnaghi, L.2    Békés, M.3    Varshavsky, A.4    Huang, T.T.5
  • 51
  • 56
    • 84924769665 scopus 로고    scopus 로고
    • Control of mammalian G protein signaling by N-terminal acetylation and the N-end rule pathway
    • Park, S. E., Kim, J. M., Seok, O. H., Cho, H., Wadas, B., Kim, S. Y., Varshavsky, A., and Hwang, C. S. (2015) Control of mammalian G protein signaling by N-terminal acetylation and the N-end rule pathway. Science 347, 1249-1252
    • (2015) Science , vol.347 , pp. 1249-1252
    • Park, S.E.1    Kim, J.M.2    Seok, O.H.3    Cho, H.4    Wadas, B.5    Kim, S.Y.6    Varshavsky, A.7    Hwang, C.S.8
  • 59
    • 84981350332 scopus 로고    scopus 로고
    • Degradation of serotonin N-acetyltransferase, a circadian regulator, by the N-end rule pathway
    • Wadas, B., Borjigin, J., Huang, Z., Oh, J.-H., Hwang, C.-S., and Varshavsky, A. (2016) Degradation of serotonin N-acetyltransferase, a circadian regulator, by the N-end rule pathway. J. Biol. Chem. 291, 17178-17196
    • (2016) J. Biol. Chem. , vol.291 , pp. 17178-17196
    • Wadas, B.1    Borjigin, J.2    Huang, Z.3    Oh, J.-H.4    Hwang, C.-S.5    Varshavsky, A.6
  • 62
    • 78649496203 scopus 로고    scopus 로고
    • The ubiquitin ligase Ubr2, a recognition E3 component of the N-end rule pathway, stabilizes Tex.19.1 during spermatogenesis
    • Yang, F., Cheng, Y., An, J. Y., Kwon, Y. T., Eckardt, S., Leu, N. A., McLaughlin, K. J., and Wang, P. J. (2010) The ubiquitin ligase Ubr2, a recognition E3 component of the N-end rule pathway, stabilizes Tex.19.1 during spermatogenesis. PLoS One 5, e14017
    • (2010) PLoS One , vol.5
    • Yang, F.1    Cheng, Y.2    An, J.Y.3    Kwon, Y.T.4    Eckardt, S.5    Leu, N.A.6    McLaughlin, K.J.7    Wang, P.J.8
  • 63
    • 0242664014 scopus 로고    scopus 로고
    • Female lethality and apoptosis of spermatocytes in mice lacking the UBR2 ubiquitin ligase of the N-end rule pathway
    • Kwon, Y. T., Xia, Z., An, J. Y., Tasaki, T., Davydov, I. V., Seo, J. W., Sheng, J., Xie, Y., and Varshavsky, A. (2003) Female lethality and apoptosis of spermatocytes in mice lacking the UBR2 ubiquitin ligase of the N-end rule pathway. Mol. Cell. Biol. 23, 8255-8271
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8255-8271
    • Kwon, Y.T.1    Xia, Z.2    An, J.Y.3    Tasaki, T.4    Davydov, I.V.5    Seo, J.W.6    Sheng, J.7    Xie, Y.8    Varshavsky, A.9
  • 64
    • 33646573377 scopus 로고    scopus 로고
    • Impaired neurogenesis and cardiovascular development in mice lacking the E3 ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway
    • An, J. Y., Seo, J. W., Tasaki, T., Lee, M. J., Varshavsky, A., and Kwon, Y. T. (2006) Impaired neurogenesis and cardiovascular development in mice lacking the E3 ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway. Proc. Natl. Acad. Sci. U.S.A. 103, 6212-6217
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 6212-6217
    • An, J.Y.1    Seo, J.W.2    Tasaki, T.3    Lee, M.J.4    Varshavsky, A.5    Kwon, Y.T.6
  • 65
    • 77955268037 scopus 로고    scopus 로고
    • The plant N-end rule pathway: Structure and functions
    • Graciet, E., and Wellmer, F. (2010) The plant N-end rule pathway: structure and functions. Trends Plant Sci. 15, 447-453
    • (2010) Trends Plant Sci. , vol.15 , pp. 447-453
    • Graciet, E.1    Wellmer, F.2
  • 68
    • 84856452223 scopus 로고    scopus 로고
    • Plant oxygen sensing is mediated by the N-end rule pathway: A milestone in plant anaerobiosis
    • Sasidharan, R., and Mustroph, A. (2011) Plant oxygen sensing is mediated by the N-end rule pathway: a milestone in plant anaerobiosis. Plant Cell 23, 4173-4183
    • (2011) Plant Cell , vol.23 , pp. 4173-4183
    • Sasidharan, R.1    Mustroph, A.2
  • 69
    • 84879637332 scopus 로고    scopus 로고
    • Signaling mechanism of tumor cell-induced up-regulation of E3 ubiquitin ligase UBR2
    • Zhang, G., Lin, R. K., Kwon, Y. T., and Li, Y. P. (2013) Signaling mechanism of tumor cell-induced up-regulation of E3 ubiquitin ligase UBR2. FASEB J. 27, 2893-2901
    • (2013) FASEB J , vol.27 , pp. 2893-2901
    • Zhang, G.1    Lin, R.K.2    Kwon, Y.T.3    Li, Y.P.4
  • 70
    • 84925251881 scopus 로고    scopus 로고
    • Molecular, cellular, and physiological significance of N-terminal acetylation
    • Aksnes, H., Hole, K., and Arnesen, T. (2015) Molecular, cellular, and physiological significance of N-terminal acetylation. Int. Rev. Cell. Mol. Biol. 316, 267-305
    • (2015) Int. Rev. Cell. Mol. Biol. , vol.316 , pp. 267-305
    • Aksnes, H.1    Hole, K.2    Arnesen, T.3
  • 71
    • 84937635572 scopus 로고    scopus 로고
    • The biological functions of Naa10: From amino-terminal acetylation to human disease
    • Dörfel, M. J., and Lyon, G. J. (2015) The biological functions of Naa10: from amino-terminal acetylation to human disease. Gene 567, 103-131
    • (2015) Gene , vol.567 , pp. 103-131
    • Dörfel, M.J.1    Lyon, G.J.2
  • 72
    • 84859490749 scopus 로고    scopus 로고
    • Protein N-terminal acettyltransferases: When the start matters
    • Starheim, K. K., Gevaert, K., and Arnesen, T. (2012) Protein N-terminal acettyltransferases: when the start matters. Trends Biochem. Sci. 37, 152-161
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 152-161
    • Starheim, K.K.1    Gevaert, K.2    Arnesen, T.3
  • 73
    • 84895826235 scopus 로고    scopus 로고
    • Calpain-generated natural protein pragments as short-lived substrates of the N-end rule pathway
    • Piatkov, K. I., Oh, J.-H., Liu, Y., and Varshavsky, A. (2014) Calpain-generated natural protein pragments as short-lived substrates of the N-end rule pathway. Proc. Natl. Acad. Sci. U.S.A. 111, E817-E826
    • (2014) Proc. Natl. Acad. Sci. U.S.A , vol.111 , pp. E817-E826
    • Piatkov, K.I.1    Oh, J.-H.2    Liu, Y.3    Varshavsky, A.4
  • 74
    • 77957805791 scopus 로고    scopus 로고
    • Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases
    • Choi, W. S., Jeong, B.-C., Joo, Y. J., Lee, M.-R., Kim, J., Eck, M. J., and Song, H. K. (2010) Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Nat. Struct. Mol. Biol. 17, 1175-1181
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 1175-1181
    • Choi, W.S.1    Jeong, B.-C.2    Joo, Y.J.3    Lee, M.-R.4    Kim, J.5    Eck, M.J.6    Song, H.K.7
  • 75
    • 77957790301 scopus 로고    scopus 로고
    • Structural basis of substrate recognition and specificity in the N-end rule pathway
    • Matta-Camacho, E., Kozlov, G., Li, F. F., and Gehring, K. (2010) Structural basis of substrate recognition and specificity in the N-end rule pathway. Nat. Struct. Mol. Biol. 17, 1182-1187
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 1182-1187
    • Matta-Camacho, E.1    Kozlov, G.2    Li, F.F.3    Gehring, K.4
  • 76
    • 67449146916 scopus 로고    scopus 로고
    • Glutamine-specific N-terminal amidase, a component of the N-end rule pathway
    • Wang, H., Piatkov, K. I., Brower, C. S., and Varshavsky, A. (2009) Glutamine-specific N-terminal amidase, a component of the N-end rule pathway. Mol. Cell 34, 686-695
    • (2009) Mol. Cell , vol.34 , pp. 686-695
    • Wang, H.1    Piatkov, K.I.2    Brower, C.S.3    Varshavsky, A.4
  • 77
    • 78649894111 scopus 로고    scopus 로고
    • The N-end rule pathway is mediated by a complex of the RING-type Ubr1 and HECT-type Ufd4 ubiquitin ligases
    • Hwang, C. S., Shemorry, A., Auerbach, D., and Varshavsky, A. (2010) The N-end rule pathway is mediated by a complex of the RING-type Ubr1 and HECT-type Ufd4 ubiquitin ligases. Nat. Cell Biol. 12, 1177-1185
    • (2010) Nat. Cell Biol. , vol.12 , pp. 1177-1185
    • Hwang, C.S.1    Shemorry, A.2    Auerbach, D.3    Varshavsky, A.4
  • 78
    • 0001602527 scopus 로고    scopus 로고
    • Alternative splicing results in differential expression, activity, and localization of the two forms of arginyl-tRNA-protein transferase, a component of the N-end rule pathway
    • Kwon, Y. T., Kashina, A. S., and Varshavsky, A. (1999) Alternative splicing results in differential expression, activity, and localization of the two forms of arginyl-tRNA-protein transferase, a component of the N-end rule pathway. Mol. Cell. Biol. 19, 182-193
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 182-193
    • Kwon, Y.T.1    Kashina, A.S.2    Varshavsky, A.3
  • 79
    • 33845953070 scopus 로고    scopus 로고
    • Arginyl-transferase, its specificity, putative substrates, bidirectional promoter, and splicing-derived isoforms
    • Hu, R.-G., Brower, C. S., Wang, H., Davydov, I. V., Sheng, J., Zhou, J., Kwon, Y. T., and Varshavsky, A. (2006) Arginyl-transferase, its specificity, putative substrates, bidirectional promoter, and splicing-derived isoforms. J. Biol. Chem. 281, 32559-32573
    • (2006) J. Biol. Chem. , vol.281 , pp. 32559-32573
    • Hu, R.-G.1    Brower, C.S.2    Wang, H.3    Davydov, I.V.4    Sheng, J.5    Zhou, J.6    Kwon, Y.T.7    Varshavsky, A.8
  • 80
    • 70649088959 scopus 로고    scopus 로고
    • Ablation of arginylation in the mouse N-end rule pathway: Loss of fat, higher metabolic rate, damaged spermatogenesis, and neurological perturbations
    • Brower, C. S., and Varshavsky, A. (2009) Ablation of arginylation in the mouse N-end rule pathway: loss of fat, higher metabolic rate, damaged spermatogenesis, and neurological perturbations. PLoS One 4, e7757
    • (2009) PLoS One , vol.4
    • Brower, C.S.1    Varshavsky, A.2
  • 81
    • 84911922733 scopus 로고    scopus 로고
    • Liat1, an arginyltransferase-binding protein whose evolution among primates involved changes in the numbers of its 10-residue repeats
    • Brower, C. S., Rosen, C. E., Jones, R. H., Wadas, B. C., Piatkov, K. I., and Varshavsky, A. (2014) Liat1, an arginyltransferase-binding protein whose evolution among primates involved changes in the numbers of its 10-residue repeats. Proc. Natl. Acad. Sci. U.S.A. 111, E4936-E4945
    • (2014) Proc. Natl. Acad. Sci. U.S.A , vol.111 , pp. E4936-E4945
    • Brower, C.S.1    Rosen, C.E.2    Jones, R.H.3    Wadas, B.C.4    Piatkov, K.I.5    Varshavsky, A.6
  • 84
    • 77956663124 scopus 로고    scopus 로고
    • Differential arginylation of actin isoforms is regulated by coding sequence-dependent degradation
    • Zhang, F., Saha, S., Shabalina, S. A., and Kashina, A. (2010) Differential arginylation of actin isoforms is regulated by coding sequence-dependent degradation. Science 329, 1534-1537
    • (2010) Science , vol.329 , pp. 1534-1537
    • Zhang, F.1    Saha, S.2    Shabalina, S.A.3    Kashina, A.4
  • 86
    • 84867665006 scopus 로고    scopus 로고
    • Augmented generation of protein fragments during wakefulness as the molecular cause of sleep: A hypothesis
    • Varshavsky, A. (2012) Augmented generation of protein fragments during wakefulness as the molecular cause of sleep: a hypothesis. Protein Sci. 21, 1634-1661
    • (2012) Protein Sci. , vol.21 , pp. 1634-1661
    • Varshavsky, A.1
  • 88
    • 59749087384 scopus 로고    scopus 로고
    • Arginyltransferase regulates α cardiac actin function, myofibril formation and contractility during heart development
    • Rai, R., Wong, C. C., Xu, T., Leu, N. A., Dong, D. W., Guo, C., McLaughlin, K. J., Yates, J. R., 3rd, and Kashina, A. (2008) Arginyltransferase regulates α cardiac actin function, myofibril formation and contractility during heart development. Development 135, 3881-3889
    • (2008) Development , vol.135 , pp. 3881-3889
    • Rai, R.1    Wong, C.C.2    Xu, T.3    Leu, N.A.4    Dong, D.W.5    Guo, C.6    McLaughlin, K.J.7    Yates, J.R.8    Kashina, A.9
  • 89
    • 63349110971 scopus 로고    scopus 로고
    • Identification of N-terminally arginylated proteins and peptides by mass spectrometry
    • Xu, T., Wong, C. C., Kashina, A., and Yates, J. R., 3rd (2009) Identification of N-terminally arginylated proteins and peptides by mass spectrometry. Nat. Protoc. 4, 325-332
    • (2009) Nat. Protoc , vol.4 , pp. 325-332
    • Xu, T.1    Wong, C.C.2    Kashina, A.3    Yates, J.R.4
  • 90
    • 82255181179 scopus 로고    scopus 로고
    • Arginylation and methylation double up to regulate nuclear proteins and nuclear architecture in vivo
    • Saha, S., Wong, C. C., Xu, T., Namgoong, S., Zebroski, H., Yates, J. R., 3rd, and Kashina, A. (2011) Arginylation and methylation double up to regulate nuclear proteins and nuclear architecture in vivo. Chem. Biol. 18, 1369-1378
    • (2011) Chem. Biol. , vol.18 , pp. 1369-1378
    • Saha, S.1    Wong, C.C.2    Xu, T.3    Namgoong, S.4    Zebroski, H.5    Yates, J.R.6    Kashina, A.7
  • 91
    • 79251568327 scopus 로고    scopus 로고
    • Arginyltransferase is an ATP-independent self-regulating enzyme that forms distinct functional complexes in vivo
    • Wang, J., Han, X., Saha, S., Xu, T., Rai, R., Zhang, F., Wolf, Y. I., Wolfson, A., Yates, J. R., 3rd, and Kashina, A. (2011) Arginyltransferase is an ATP-independent self-regulating enzyme that forms distinct functional complexes in vivo. Chem. Biol. 18, 121-130
    • (2011) Chem. Biol. , vol.18 , pp. 121-130
    • Wang, J.1    Han, X.2    Saha, S.3    Xu, T.4    Rai, R.5    Zhang, F.6    Wolf, Y.I.7    Wolfson, A.8    Yates, J.R.9    Kashina, A.10
  • 93
    • 22544484457 scopus 로고    scopus 로고
    • Identification of mammalian arginyltransferases that modify a specific subset of protein substrates
    • Rai, R., and Kashina, A. (2005) Identification of mammalian arginyltransferases that modify a specific subset of protein substrates. Proc. Natl. Acad. Sci. U.S.A. 102, 10123-10128
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 10123-10128
    • Rai, R.1    Kashina, A.2
  • 97
    • 84973505602 scopus 로고    scopus 로고
    • Quantitative proteomics analysis of the Arg/N-end rule pathway of targeted degradation in Arabidopsis roots
    • Zhang, H., Deery, M. J., Gannon, L., Powers, S. J., Lilley, K. S., and Theodoulou, F. L. (2015) Quantitative proteomics analysis of the Arg/N-end rule pathway of targeted degradation in Arabidopsis roots. Proteomics 15, 2447-2457
    • (2015) Proteomics , vol.15 , pp. 2447-2457
    • Zhang, H.1    Deery, M.J.2    Gannon, L.3    Powers, S.J.4    Lilley, K.S.5    Theodoulou, F.L.6
  • 99
    • 84954445952 scopus 로고    scopus 로고
    • Enzymatic generation of peptides flanked by basic amino acids to obtain MS/MS spectra with 2X sequence coverage
    • Ebhardt, H. A., Nan, J., Chaulk, S. G., Fahlman, R. P., and Aebersold, R. (2014) Enzymatic generation of peptides flanked by basic amino acids to obtain MS/MS spectra with 2X sequence coverage. Rapid Commun. Mass Spectrom. 28, 2735-2743
    • (2014) Rapid Commun. Mass Spectrom. , vol.28 , pp. 2735-2743
    • Ebhardt, H.A.1    Nan, J.2    Chaulk, S.G.3    Fahlman, R.P.4    Aebersold, R.5
  • 100
    • 84863992173 scopus 로고    scopus 로고
    • Arginylation-dependent regulation of a proteolytic product of talin is essential for cell-cell adhesion
    • Zhang, F., Saha, S., and Kashina, A. (2012) Arginylation-dependent regulation of a proteolytic product of talin is essential for cell-cell adhesion. J. Cell Biol. 197, 819-836
    • (2012) J. Cell Biol. , vol.197 , pp. 819-836
    • Zhang, F.1    Saha, S.2    Kashina, A.3
  • 102
    • 73949155950 scopus 로고    scopus 로고
    • CelluSpots: A reproducible means of making peptide arrays for the determination of SH2 domain binding specificity
    • Wu, C., and Li, S. S. (2009) CelluSpots: a reproducible means of making peptide arrays for the determination of SH2 domain binding specificity. Methods Mol. Biol. 570, 197-202
    • (2009) Methods Mol. Biol. , vol.570 , pp. 197-202
    • Wu, C.1    Li, S.S.2
  • 103
    • 80052140473 scopus 로고    scopus 로고
    • Application of CelluSpots peptide arrays for the analysis of the binding specificity of epigenetic reading domains to modified histone tails
    • Bock, I., Kudithipudi, S., Tamas, R., Kungulovski, G., Dhayalan, A., and Jeltsch, A. (2011) Application of CelluSpots peptide arrays for the analysis of the binding specificity of epigenetic reading domains to modified histone tails. BMC Biochem. 12, 48
    • (2011) BMC Biochem. , vol.12 , pp. 48
    • Bock, I.1    Kudithipudi, S.2    Tamas, R.3    Kungulovski, G.4    Dhayalan, A.5    Jeltsch, A.6
  • 104
    • 79151476637 scopus 로고    scopus 로고
    • Detailed specificity analysis of antibodies binding to modified histone tails with peptide arrays
    • Bock, I., Dhayalan, A., Kudithipudi, S., Brandt, O., Rathert, P., and Jeltsch, A. (2011) Detailed specificity analysis of antibodies binding to modified histone tails with peptide arrays. Epigenetics 6, 256-263
    • (2011) Epigenetics , vol.6 , pp. 256-263
    • Bock, I.1    Dhayalan, A.2    Kudithipudi, S.3    Brandt, O.4    Rathert, P.5    Jeltsch, A.6
  • 106
    • 1842485068 scopus 로고    scopus 로고
    • Spalog and sequelog: Neutral terms for spatial and sequence similarity
    • Varshavsky, A. (2004) Spalog and sequelog: neutral terms for spatial and sequence similarity. Curr. Biol. 14, R181-R183
    • (2004) Curr. Biol. , vol.14 , pp. R181-R183
    • Varshavsky, A.1
  • 107
    • 0034725661 scopus 로고    scopus 로고
    • RGS4 is arginylated and degraded by the N-end rule pathway in vitro
    • Davydov, I. V., and Varshavsky, A. (2000) RGS4 is arginylated and degraded by the N-end rule pathway in vitro. J. Biol. Chem. 275, 22931-22941
    • (2000) J. Biol. Chem. , vol.275 , pp. 22931-22941
    • Davydov, I.V.1    Varshavsky, A.2
  • 108
    • 28944437762 scopus 로고    scopus 로고
    • Ubiquitin fusion technique and related methods
    • Varshavsky, A. (2005) Ubiquitin fusion technique and related methods. Methods Enzymol. 399, 777-799
    • (2005) Methods Enzymol. , vol.399 , pp. 777-799
    • Varshavsky, A.1
  • 109
    • 0034581529 scopus 로고    scopus 로고
    • Ubiquitin fusion technique and its descendants
    • Varshavsky, A. (2000) Ubiquitin fusion technique and its descendants. Methods Enzymol. 327, 578-593
    • (2000) Methods Enzymol. , vol.327 , pp. 578-593
    • Varshavsky, A.1
  • 111
    • 1942537173 scopus 로고    scopus 로고
    • An efficient system for high-level expression and easy purification of authentic recombinant proteins
    • Catanzariti, A.-M., Soboleva, T. A., Jans, D. A., Board, P. G., and Baker, R. T. (2004) An efficient system for high-level expression and easy purification of authentic recombinant proteins. Protein Sci. 13, 1331-1339
    • (2004) Protein Sci. , vol.13 , pp. 1331-1339
    • Catanzariti, A.-M.1    Soboleva, T.A.2    Jans, D.A.3    Board, P.G.4    Baker, R.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.