메뉴 건너뛰기




Volumn 68, Issue 1, 2017, Pages 233-246.e5

Ubiquitin Linkage-Specific Affimers Reveal Insights into K6-Linked Ubiquitin Signaling

Author keywords

affimer; HUWE1; Lys6 linked ubiquitin chains; Mfn2; microscale thermophoresis; mitophagy; Parkin; X ray crystallography

Indexed keywords

BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; MITOFUSIN 2; SHORT HAIRPIN RNA; UBIQUITIN; CARRIER PROTEIN; GUANOSINE TRIPHOSPHATASE; HUWE1 PROTEIN, HUMAN; LYSINE; MFN2 PROTEIN, HUMAN; MITOCHONDRIAL PROTEIN; MOLECULAR PROBE; PROTEIN BINDING; RECOMBINANT PROTEIN; RNF144A PROTEIN, HUMAN; RNF144B PROTEIN, HUMAN; UBIQUITIN PROTEIN LIGASE;

EID: 85029693774     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2017.08.020     Document Type: Article
Times cited : (150)

References (64)
  • 2
    • 84964603365 scopus 로고    scopus 로고
    • Mechanisms of mitophagy: PINK1, Parkin, USP30 and beyond
    • Bingol, B., Sheng, M., Mechanisms of mitophagy: PINK1, Parkin, USP30 and beyond. Free Radic. Biol. Med. 100 (2016), 210–222.
    • (2016) Free Radic. Biol. Med. , vol.100 , pp. 210-222
    • Bingol, B.1    Sheng, M.2
  • 3
    • 73549090361 scopus 로고    scopus 로고
    • Efficient internalization of MHC I requires lysine-11 and lysine-63 mixed linkage polyubiquitin chains
    • Boname, J.M., Thomas, M., Stagg, H.R., Xu, P., Peng, J., Lehner, P.J., Efficient internalization of MHC I requires lysine-11 and lysine-63 mixed linkage polyubiquitin chains. Traffic 11 (2010), 210–220.
    • (2010) Traffic , vol.11 , pp. 210-220
    • Boname, J.M.1    Thomas, M.2    Stagg, H.R.3    Xu, P.4    Peng, J.5    Lehner, P.J.6
  • 4
    • 77955417276 scopus 로고    scopus 로고
    • Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne
    • Bremm, A., Freund, S.M.V., Komander, D., Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne. Nat. Struct. Mol. Biol. 17 (2010), 939–947.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 939-947
    • Bremm, A.1    Freund, S.M.V.2    Komander, D.3
  • 11
    • 85009815240 scopus 로고    scopus 로고
    • Molecular basis for specificity of the Met1-linked polyubiquitin signal
    • Elliott, P.R., Molecular basis for specificity of the Met1-linked polyubiquitin signal. Biochem. Soc. Trans. 44 (2016), 1581–1602.
    • (2016) Biochem. Soc. Trans. , vol.44 , pp. 1581-1602
    • Elliott, P.R.1
  • 16
    • 70449084692 scopus 로고    scopus 로고
    • Efficient protection and isolation of ubiquitylated proteins using tandem ubiquitin-binding entities
    • Hjerpe, R., Aillet, F., Lopitz-Otsoa, F., Lang, V., England, P., Rodriguez, M.S., Efficient protection and isolation of ubiquitylated proteins using tandem ubiquitin-binding entities. EMBO Rep. 10 (2009), 1250–1258.
    • (2009) EMBO Rep. , vol.10 , pp. 1250-1258
    • Hjerpe, R.1    Aillet, F.2    Lopitz-Otsoa, F.3    Lang, V.4    England, P.5    Rodriguez, M.S.6
  • 17
    • 84877313192 scopus 로고    scopus 로고
    • Assembly, analysis and architecture of atypical ubiquitin chains
    • Hospenthal, M.K., Freund, S.M.V., Komander, D., Assembly, analysis and architecture of atypical ubiquitin chains. Nat. Struct. Mol. Biol. 20 (2013), 555–565.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 555-565
    • Hospenthal, M.K.1    Freund, S.M.V.2    Komander, D.3
  • 18
    • 84861783400 scopus 로고    scopus 로고
    • Ubiquitin-binding proteins: decoders of ubiquitin-mediated cellular functions
    • Husnjak, K., Dikic, I., Ubiquitin-binding proteins: decoders of ubiquitin-mediated cellular functions. Annu. Rev. Biochem. 81 (2012), 291–322.
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 291-322
    • Husnjak, K.1    Dikic, I.2
  • 21
    • 79961000536 scopus 로고    scopus 로고
    • Protein standard absolute quantification (PSAQ) method for the measurement of cellular ubiquitin pools
    • Kaiser, S.E., Riley, B.E., Shaler, T.A., Trevino, R.S., Becker, C.H., Schulman, H., Kopito, R.R., Protein standard absolute quantification (PSAQ) method for the measurement of cellular ubiquitin pools. Nat. Methods 8 (2011), 691–696.
    • (2011) Nat. Methods , vol.8 , pp. 691-696
    • Kaiser, S.E.1    Riley, B.E.2    Shaler, T.A.3    Trevino, R.S.4    Becker, C.H.5    Schulman, H.6    Kopito, R.R.7
  • 24
    • 84865395988 scopus 로고    scopus 로고
    • Stress-induced phosphorylation and proteasomal degradation of mitofusin 2 facilitates mitochondrial fragmentation and apoptosis
    • Leboucher, G.P., Tsai, Y.C., Yang, M., Shaw, K.C., Zhou, M., Veenstra, T.D., Glickman, M.H., Weissman, A.M., Stress-induced phosphorylation and proteasomal degradation of mitofusin 2 facilitates mitochondrial fragmentation and apoptosis. Mol. Cell 47 (2012), 547–557.
    • (2012) Mol. Cell , vol.47 , pp. 547-557
    • Leboucher, G.P.1    Tsai, Y.C.2    Yang, M.3    Shaw, K.C.4    Zhou, M.5    Veenstra, T.D.6    Glickman, M.H.7    Weissman, A.M.8
  • 30
    • 85021674924 scopus 로고    scopus 로고
    • Mechanisms of deubiquitinase specificity and regulation
    • Mevissen, T.E.T., Komander, D., Mechanisms of deubiquitinase specificity and regulation. Annu. Rev. Biochem. 86 (2017), 159–192.
    • (2017) Annu. Rev. Biochem. , vol.86 , pp. 159-192
    • Mevissen, T.E.T.1    Komander, D.2
  • 31
    • 84900337781 scopus 로고    scopus 로고
    • Enhanced protein degradation by branched ubiquitin chains
    • Meyer, H.-J., Rape, M., Enhanced protein degradation by branched ubiquitin chains. Cell 157 (2014), 910–921.
    • (2014) Cell , vol.157 , pp. 910-921
    • Meyer, H.-J.1    Rape, M.2
  • 33
    • 1942517849 scopus 로고    scopus 로고
    • BRCA1: BARD1 induces the formation of conjugated ubiquitin structures, dependent on K6 of ubiquitin, in cells during DNA replication and repair
    • Morris, J.R., Solomon, E., BRCA1: BARD1 induces the formation of conjugated ubiquitin structures, dependent on K6 of ubiquitin, in cells during DNA replication and repair. Hum. Mol. Genet. 13 (2004), 807–817.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 807-817
    • Morris, J.R.1    Solomon, E.2
  • 35
    • 78649300971 scopus 로고    scopus 로고
    • p62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both
    • Narendra, D., Kane, L.A., Hauser, D.N., Fearnley, I.M., Youle, R.J., p62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both. Autophagy 6 (2010), 1090–1106.
    • (2010) Autophagy , vol.6 , pp. 1090-1106
    • Narendra, D.1    Kane, L.A.2    Hauser, D.N.3    Fearnley, I.M.4    Youle, R.J.5
  • 39
    • 77949323346 scopus 로고    scopus 로고
    • A structural element within the HUWE1 HECT domain modulates self-ubiquitination and substrate ubiquitination activities
    • Pandya, R.K., Partridge, J.R., Love, K.R., Schwartz, T.U., Ploegh, H.L., A structural element within the HUWE1 HECT domain modulates self-ubiquitination and substrate ubiquitination activities. J. Biol. Chem. 285 (2010), 5664–5673.
    • (2010) J. Biol. Chem. , vol.285 , pp. 5664-5673
    • Pandya, R.K.1    Partridge, J.R.2    Love, K.R.3    Schwartz, T.U.4    Ploegh, H.L.5
  • 43
  • 44
    • 84890136771 scopus 로고    scopus 로고
    • Mammalian HECT ubiquitin-protein ligases: biological and pathophysiological aspects
    • Scheffner, M., Kumar, S., Mammalian HECT ubiquitin-protein ligases: biological and pathophysiological aspects. Biochim. Biophys. Acta 1843 (2014), 61–74.
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 61-74
    • Scheffner, M.1    Kumar, S.2
  • 48
    • 84961743030 scopus 로고    scopus 로고
    • Ubiquitin modifications
    • Swatek, K.N., Komander, D., Ubiquitin modifications. Cell Res. 26 (2016), 399–422.
    • (2016) Cell Res. , vol.26 , pp. 399-422
    • Swatek, K.N.1    Komander, D.2
  • 50
    • 84908072100 scopus 로고    scopus 로고
    • Quantitative Lys-ϵ-Gly-Gly (diGly) proteomics coupled with inducible RNAi reveals ubiquitin-mediated proteolysis of DNA damage-inducible transcript 4 (DDIT4) by the E3 ligase HUWE1
    • Thompson, J.W., Nagel, J., Hoving, S., Gerrits, B., Bauer, A., Thomas, J.R., Kirschner, M.W., Schirle, M., Luchansky, S.J., Quantitative Lys-ϵ-Gly-Gly (diGly) proteomics coupled with inducible RNAi reveals ubiquitin-mediated proteolysis of DNA damage-inducible transcript 4 (DDIT4) by the E3 ligase HUWE1. J. Biol. Chem. 289 (2014), 28942–28955.
    • (2014) J. Biol. Chem. , vol.289 , pp. 28942-28955
    • Thompson, J.W.1    Nagel, J.2    Hoving, S.3    Gerrits, B.4    Bauer, A.5    Thomas, J.R.6    Kirschner, M.W.7    Schirle, M.8    Luchansky, S.J.9
  • 53
    • 77956903406 scopus 로고    scopus 로고
    • Engineered diubiquitin synthesis reveals Lys29-isopeptide specificity of an OTU deubiquitinase
    • Virdee, S., Ye, Y., Nguyen, D.P., Komander, D., Chin, J.W., Engineered diubiquitin synthesis reveals Lys29-isopeptide specificity of an OTU deubiquitinase. Nat. Chem. Biol. 6 (2010), 750–757.
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 750-757
    • Virdee, S.1    Ye, Y.2    Nguyen, D.P.3    Komander, D.4    Chin, J.W.5
  • 55
    • 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 (2011), 105–108.
    • (2011) Nature , vol.474 , pp. 105-108
    • Wenzel, D.M.1    Lissounov, A.2    Brzovic, P.S.3    Klevit, R.E.4
  • 56
    • 0042317328 scopus 로고    scopus 로고
    • The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an unconventional linkage involving lysine residue K6 of ubiquitin
    • Wu-Baer, F., Lagrazon, K., Yuan, W., Baer, R., The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an unconventional linkage involving lysine residue K6 of ubiquitin. J. Biol. Chem. 278 (2003), 34743–34746.
    • (2003) J. Biol. Chem. , vol.278 , pp. 34743-34746
    • Wu-Baer, F.1    Lagrazon, K.2    Yuan, W.3    Baer, R.4
  • 57
    • 70350015537 scopus 로고    scopus 로고
    • A ubiquitin replacement strategy in human cells reveals distinct mechanisms of IKK activation by TNFalpha and IL-1beta
    • Xu, M., Skaug, B., Zeng, W., Chen, Z.J., A ubiquitin replacement strategy in human cells reveals distinct mechanisms of IKK activation by TNFalpha and IL-1beta. Mol. Cell 36 (2009), 302–314.
    • (2009) Mol. Cell , vol.36 , pp. 302-314
    • Xu, M.1    Skaug, B.2    Zeng, W.3    Chen, Z.J.4
  • 58
    • 85013777029 scopus 로고    scopus 로고
    • The HECT domain ubiquitin ligase HUWE1 targets unassembled soluble proteins for degradation
    • Xu, Y., Anderson, D.E., Ye, Y., The HECT domain ubiquitin ligase HUWE1 targets unassembled soluble proteins for degradation. Cell Discov., 2, 2016, 16040.
    • (2016) Cell Discov. , vol.2 , pp. 16040
    • Xu, Y.1    Anderson, D.E.2    Ye, Y.3
  • 59
    • 84971236561 scopus 로고    scopus 로고
    • The increasing complexity of the ubiquitin code
    • Yau, R., Rape, M., The increasing complexity of the ubiquitin code. Nat. Cell Biol. 18 (2016), 579–586.
    • (2016) Nat. Cell Biol. , vol.18 , pp. 579-586
    • Yau, R.1    Rape, M.2
  • 60
    • 70350461507 scopus 로고    scopus 로고
    • Building ubiquitin chains: E2 enzymes at work
    • Ye, Y., Rape, M., Building ubiquitin chains: E2 enzymes at work. Nat. Rev. Mol. Cell Biol. 10 (2009), 755–764.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 755-764
    • Ye, Y.1    Rape, M.2
  • 61
    • 79953314427 scopus 로고    scopus 로고
    • Polyubiquitin binding and cross-reactivity in the USP domain deubiquitinase USP21
    • Ye, Y., Akutsu, M., Reyes-Turcu, F., Enchev, R.I., Wilkinson, K.D., Komander, D., Polyubiquitin binding and cross-reactivity in the USP domain deubiquitinase USP21. EMBO Rep. 12 (2011), 350–357.
    • (2011) EMBO Rep. , vol.12 , pp. 350-357
    • Ye, Y.1    Akutsu, M.2    Reyes-Turcu, F.3    Enchev, R.I.4    Wilkinson, K.D.5    Komander, D.6
  • 63
    • 85021691475 scopus 로고    scopus 로고
    • Ubiquitin ligases: structure, function, and regulation
    • Zheng, N., Shabek, N., Ubiquitin ligases: structure, function, and regulation. Annu. Rev. Biochem. 86 (2017), 129–157.
    • (2017) Annu. Rev. Biochem. , vol.86 , pp. 129-157
    • Zheng, N.1    Shabek, N.2
  • 64
    • 21244472965 scopus 로고    scopus 로고
    • Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis
    • Zhong, Q., Gao, W., Du, F., Wang, X., Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis. Cell 121 (2005), 1085–1095.
    • (2005) Cell , vol.121 , pp. 1085-1095
    • Zhong, Q.1    Gao, W.2    Du, F.3    Wang, X.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.