메뉴 건너뛰기




Volumn 556, Issue 7701, 2018, Pages 381-385

Activity-based E3 ligase profiling uncovers an E3 ligase with esterification activity

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; MYC BINDING PROTEIN 2; THREONINE; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; LYSINE; MYCBP2 PROTEIN, HUMAN; SERINE; SIGNAL TRANSDUCING ADAPTOR PROTEIN; UBIQUITIN; UBIQUITIN PROTEIN LIGASE; THIOESTER;

EID: 85045950070     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/s41586-018-0026-1     Document Type: Article
Times cited : (185)

References (41)
  • 3
    • 0028907874 scopus 로고
    • A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase
    • Huibregtse, J. M., Scheffner, M., Beaudenon, S. & Howley, P. M. A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc. Natl Acad. Sci. USA 92, 2563-2567 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 2563-2567
    • Huibregtse, J.M.1    Scheffner, M.2    Beaudenon, S.3    Howley, P.M.4
  • 4
    • 0028898424 scopus 로고
    • Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade
    • Scheffner, M., Nuber, U. & Huibregtse, J. M. Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade. Nature 373, 81-83 (1995).
    • (1995) Nature , vol.373 , pp. 81-83
    • Scheffner, M.1    Nuber, U.2    Huibregtse, J.M.3
  • 5
    • 79957949190 scopus 로고    scopus 로고
    • UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids
    • Wenzel, D. M., Lissounov, A., Brzovic, P. S. & Klevit, R. E. UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. Nature 474, 105-108 (2011).
    • (2011) Nature , vol.474 , pp. 105-108
    • Wenzel, D.M.1    Lissounov, A.2    Brzovic, P.S.3    Klevit, R.E.4
  • 6
    • 85015042001 scopus 로고    scopus 로고
    • Activity-based probes for the ubiquitin conjugation-deconjugation machinery: New chemistries, new tools, and new insights
    • Hewings, D. S., Flygare, J. A., Bogyo, M. & Wertz, I. E. Activity-based probes for the ubiquitin conjugation-deconjugation machinery: new chemistries, new tools, and new insights. FEBS J. 284, 1555-1576 (2017).
    • (2017) FEBS J , vol.284 , pp. 1555-1576
    • Hewings, D.S.1    Flygare, J.A.2    Bogyo, M.3    Wertz, I.E.4
  • 7
    • 84959192267 scopus 로고    scopus 로고
    • Probes of ubiquitin E3 ligases enable systematic dissection of parkin activation
    • Pao, K. C. et al. Probes of ubiquitin E3 ligases enable systematic dissection of parkin activation. Nat. Chem. Biol. 12, 324-331 (2016).
    • (2016) Nat. Chem. Biol , vol.12 , pp. 324-331
    • Pao, K.C.1
  • 8
    • 84902142324 scopus 로고    scopus 로고
    • Enzyme inhibitor discovery by activity-based protein profiling
    • Niphakis, M. J. & Cravatt, B. F. Enzyme inhibitor discovery by activity-based protein profiling. Annu. Rev. Biochem. 83, 341-377 (2014).
    • (2014) Annu. Rev. Biochem , vol.83 , pp. 341-377
    • Niphakis, M.J.1    Cravatt, B.F.2
  • 9
    • 0036775490 scopus 로고    scopus 로고
    • Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family
    • Borodovsky, A. et al. Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family. Chem. Biol. 9, 1149-1159 (2002).
    • (2002) Chem. Biol , vol.9 , pp. 1149-1159
    • Borodovsky, A.1
  • 10
    • 0033710880 scopus 로고    scopus 로고
    • Regulation of presynaptic terminal organization by C. Elegans RPM-1, a putative guanine nucleotide exchanger with a RING-H2 finger domain
    • Zhen, M., Huang, X., Bamber, B. & Jin, Y. Regulation of presynaptic terminal organization by C. elegans RPM-1, a putative guanine nucleotide exchanger with a RING-H2 finger domain. Neuron 26, 331-343 (2000).
    • (2000) Neuron , vol.26 , pp. 331-343
    • Zhen, M.1    Huang, X.2    Bamber, B.3    Jin, Y.4
  • 11
    • 0033715810 scopus 로고    scopus 로고
    • Highwire regulates synaptic growth in Drosophila
    • Wan, H. I. et al. Highwire regulates synaptic growth in Drosophila. Neuron 26, 313-329 (2000).
    • (2000) Neuron , vol.26 , pp. 313-329
    • Wan, H.I.1
  • 12
    • 84962788657 scopus 로고    scopus 로고
    • The PHR proteins: Intracellular signaling hubs in neuronal development and axon degeneration
    • Grill, B., Murphey, R. K. & Borgen, M. A. The PHR proteins: intracellular signaling hubs in neuronal development and axon degeneration. Neural Dev. 11, 8 (2016).
    • (2016) Neural Dev , vol.11 , pp. 8
    • Grill, B.1    Murphey, R.K.2    Borgen, M.A.3
  • 13
    • 85021397971 scopus 로고    scopus 로고
    • Activity-based probes for HECT E3 ubiquitin ligases
    • Byrne, R., Mund, T. & Licchesi, J. D. F. Activity-based probes for HECT E3 ubiquitin ligases. ChemBioChem 18, 1415-1427 (2017).
    • (2017) ChemBioChem , vol.18 , pp. 1415-1427
    • Byrne, R.1    Mund, T.2    Licchesi, J.D.F.3
  • 15
    • 0035827707 scopus 로고    scopus 로고
    • A HECT domain E3 enzyme assembles novel polyubiquitin chains
    • You, J. & Pickart, C. M. A HECT domain E3 enzyme assembles novel polyubiquitin chains. J. Biol. Chem. 276, 19871-19878 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 19871-19878
    • You, J.1    Pickart, C.M.2
  • 16
    • 84865781586 scopus 로고    scopus 로고
    • Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis
    • Plechanovová, A., Jaffray, E. G., Tatham, M. H., Naismith, J. H. & Hay, R. T. Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis. Nature 489, 115-120 (2012).
    • (2012) Nature , vol.489 , pp. 115-120
    • Plechanovová, A.1    Jaffray, E.G.2    Tatham, M.H.3    Naismith, J.H.4    Hay, R.T.5
  • 17
    • 84866124869 scopus 로고    scopus 로고
    • BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer
    • Dou, H., Buetow, L., Sibbet, G. J., Cameron, K. & Huang, D. T. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. Nat. Struct. Mol. Biol. 19, 876-883 (2012).
    • (2012) Nat. Struct. Mol. Biol , vol.19 , pp. 876-883
    • Dou, H.1    Buetow, L.2    Sibbet, G.J.3    Cameron, K.4    Huang, D.T.5
  • 18
    • 84956664551 scopus 로고    scopus 로고
    • Structure of a HOIP/E2-ubiquitin complex reveals RBR E3 ligase mechanism and regulation
    • Lechtenberg, B. C. et al. Structure of a HOIP/E2-ubiquitin complex reveals RBR E3 ligase mechanism and regulation. Nature 529, 546-550 (2016).
    • (2016) Nature , vol.529 , pp. 546-550
    • Lechtenberg, B.C.1
  • 19
    • 85019877864 scopus 로고    scopus 로고
    • Structural studies of HHARI/UbcH7-Ub reveal unique E2-Ub conformational restriction by RBR RING1
    • Dove, K. K. et al. Structural studies of HHARI/UbcH7-Ub reveal unique E2-Ub conformational restriction by RBR RING1. Structure 25, 890-900 (2017).
    • (2017) Structure , vol.25 , pp. 890-900
    • Dove, K.K.1
  • 20
    • 84871676178 scopus 로고    scopus 로고
    • The Highwire ubiquitin ligase promotes axonal degeneration by tuning levels of Nmnat protein
    • Xiong, X. et al. The Highwire ubiquitin ligase promotes axonal degeneration by tuning levels of Nmnat protein. PLoS Biol. 10, e1001440 (2012).
    • (2012) PLoS Biol , vol.10 , pp. e1001440
    • Xiong, X.1
  • 21
    • 84878586685 scopus 로고    scopus 로고
    • The Phr1 ubiquitin ligase promotes injury-induced axon self-destruction
    • Babetto, E., Beirowski, B., Russler, E. V., Milbrandt, J. & DiAntonio, A. The Phr1 ubiquitin ligase promotes injury-induced axon self-destruction. Cell Rep. 3, 1422-1429 (2013).
    • (2013) Cell Rep , vol.3 , pp. 1422-1429
    • Babetto, E.1    Beirowski, B.2    Russler, E.V.3    Milbrandt, J.4    DiAntonio, A.5
  • 22
    • 84876987935 scopus 로고    scopus 로고
    • Subcellular localization determines the stability and axon protective capacity of axon survival factor Nmnat2
    • Milde, S., Gilley, J. & Coleman, M. P. Subcellular localization determines the stability and axon protective capacity of axon survival factor Nmnat2. PLoS Biol. 11, e1001539 (2013).
    • (2013) PLoS Biol , vol.11 , pp. e1001539
    • Milde, S.1    Gilley, J.2    Coleman, M.P.3
  • 23
    • 0034682718 scopus 로고    scopus 로고
    • Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases
    • Zheng, N., Wang, P., Jeffrey, P. D. & Pavletich, N. P. Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases. Cell 102, (533-539 (2000).
    • (2000) Cell , vol.102 , pp. 533-539
    • Zheng, N.1    Wang, P.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 24
    • 84876864015 scopus 로고    scopus 로고
    • Structure of a ubiquitin E1-E2 complex: Insights to E1-E2 thioester transfer
    • Olsen, S. K. & Lima, C. D. Structure of a ubiquitin E1-E2 complex: insights to E1-E2 thioester transfer. Mol. Cell 49, 884-896 (2013).
    • (2013) Mol. Cell , vol.49 , pp. 884-896
    • Olsen, S.K.1    Lima, C.D.2
  • 25
    • 21744433861 scopus 로고    scopus 로고
    • Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase
    • Cadwell, K. & Coscoy, L. Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase. Science 309, 127-130 (2005).
    • (2005) Science , vol.309 , pp. 127-130
    • Cadwell, K.1    Coscoy, L.2
  • 26
    • 78650253267 scopus 로고    scopus 로고
    • Ubiquitylation of an ERAD substrate occurs on multiple types of amino acids
    • Shimizu, Y., Okuda-Shimizu, Y. & Hendershot, L. M. Ubiquitylation of an ERAD substrate occurs on multiple types of amino acids. Mol. Cell 40, 917-926 (2010).
    • (2010) Mol. Cell , vol.40 , pp. 917-926
    • Shimizu, Y.1    Okuda-Shimizu, Y.2    Hendershot, L.M.3
  • 27
    • 83255185097 scopus 로고    scopus 로고
    • Ubiquitination of substrates by esterification
    • Wang, X., Herr, R. A. & Hansen, T. H. Ubiquitination of substrates by esterification. Traffic 13, 19-24 (2012).
    • (2012) Traffic , vol.13 , pp. 19-24
    • Wang, X.1    Herr, R.A.2    Hansen, T.H.3
  • 28
    • 84994589276 scopus 로고    scopus 로고
    • Mechanism and disease association of E2-conjugating enzymes: Lessons from UBE2T and UBE2L3
    • Alpi, A. F., Chaugule, V. & Walden, H. Mechanism and disease association of E2-conjugating enzymes: lessons from UBE2T and UBE2L3. Biochem. J. 473, 3401-3419 (2016).
    • (2016) Biochem. J , vol.473 , pp. 3401-3419
    • Alpi, A.F.1    Chaugule, V.2    Walden, H.3
  • 29
    • 84901007122 scopus 로고    scopus 로고
    • Wallerian degeneration: An emerging axon death pathway linking injury and disease
    • Conforti, L., Gilley, J. & Coleman, M. P. Wallerian degeneration: an emerging axon death pathway linking injury and disease. Nat. Rev. Neurosci. 15, 394-409 (2014).
    • (2014) Nat. Rev. Neurosci , vol.15 , pp. 394-409
    • Conforti, L.1    Gilley, J.2    Coleman, M.P.3
  • 30
    • 85014751405 scopus 로고    scopus 로고
    • Screening with an NMNAT2-MSD platform identifies small molecules that modulate NMNAT2 levels in cortical neurons
    • Ali, Y. O., Bradley, G. & Lu, H. C. Screening with an NMNAT2-MSD platform identifies small molecules that modulate NMNAT2 levels in cortical neurons. Sci. Rep. 7, 43846 (2017).
    • (2017) Sci. Rep , vol.7 , pp. 43846
    • Ali, Y.O.1    Bradley, G.2    Lu, H.C.3
  • 31
    • 84888034624 scopus 로고    scopus 로고
    • Structural basis for ligase-specific conjugation of linear ubiquitin chains by HOIP
    • Stieglitz, B. et al. Structural basis for ligase-specific conjugation of linear ubiquitin chains by HOIP. Nature 503, 422-426 (2013).
    • (2013) Nature , vol.503 , pp. 422-426
    • Stieglitz, B.1
  • 32
    • 84934990030 scopus 로고    scopus 로고
    • Orthogonal thiol functionalization at a single atomic center for profiling transthiolation activity of E1 activating enzymes
    • Stanley, M. et al. Orthogonal thiol functionalization at a single atomic center for profiling transthiolation activity of E1 activating enzymes. ACS Chem. Biol. 10, 1542-1554 (2015).
    • (2015) ACS Chem. Biol , vol.10 , pp. 1542-1554
    • Stanley, M.1
  • 33
    • 84866117936 scopus 로고    scopus 로고
    • Identification of cross-linked peptides from complex samples
    • Yang, B. et al. Identification of cross-linked peptides from complex samples. Nat. Methods 9, 904-906 (2012).
    • (2012) Nat. Methods , vol.9 , pp. 904-906
    • Yang, B.1
  • 34
    • 84866858702 scopus 로고    scopus 로고
    • Structure of an E3:E2-Ub complex reveals an allosteric mechanism shared among RING/U-box ligases
    • Pruneda, J. N. et al. Structure of an E3:E2-Ub complex reveals an allosteric mechanism shared among RING/U-box ligases. Mol. Cell 47, 933-942 (2012).
    • (2012) Mol. Cell , vol.47 , pp. 933-942
    • Pruneda, J.N.1
  • 35
    • 0141753130 scopus 로고    scopus 로고
    • A conserved catalytic residue in the ubiquitin-conjugating enzyme family
    • Wu, P. Y. et al. A conserved catalytic residue in the ubiquitin-conjugating enzyme family. EMBO J. 22, 5241-5250 (2003).
    • (2003) EMBO J , vol.22 , pp. 5241-5250
    • Wu, P.Y.1
  • 36
    • 33744911377 scopus 로고    scopus 로고
    • Lysine activation and functional analysis of E2-mediated conjugation in the SUMO pathway
    • Yunus, A. A. & Lima, C. D. Lysine activation and functional analysis of E2-mediated conjugation in the SUMO pathway. Nat. Struct. Mol. Biol. 13, 491-499 (2006).
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 491-499
    • Yunus, A.A.1    Lima, C.D.2
  • 37
    • 73649110303 scopus 로고    scopus 로고
    • Substrate-assisted inhibition of ubiquitin-like proteinactivating enzymes: The NEDD8 E1 inhibitor MLN4924 forms a NEDD8-AMP mimetic in situ
    • Brownell, J. E. et al. Substrate-assisted inhibition of ubiquitin-like proteinactivating enzymes: the NEDD8 E1 inhibitor MLN4924 forms a NEDD8-AMP mimetic in situ. Mol. Cell 37, 102-111 (2010).
    • (2010) Mol. Cell , vol.37 , pp. 102-111
    • Brownell, J.E.1
  • 38
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • Langer, G., Cohen, S. X., Lamzin, V. S. & Perrakis, A. Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7. Nat. Protoc. 3, 1171-1179 (2008).
    • (2008) Nat. Protoc , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 40
    • 79953763877 scopus 로고    scopus 로고
    • REFMAC5 for the refinement of macromolecular crystal structures
    • Murshudov, G. N. et al. REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr. D 67, 355-367 (2011).
    • (2011) Acta Crystallogr. D , vol.67 , pp. 355-367
    • Murshudov, G.N.1
  • 41
    • 0037441653 scopus 로고    scopus 로고
    • Structure validation by Cα geometry: φ, ψ and Cβ deviation
    • Lovell, S. C. et al. Structure validation by Cα geometry: φ, ψ and Cβ deviation. Proteins 50, 437-450 (2003).
    • (2003) Proteins , vol.50 , pp. 437-450
    • Lovell, S.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.