메뉴 건너뛰기




Volumn 34, Issue 3, 2015, Pages 307-325

Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain assembly and hydrolysis

Author keywords

deubiquitinase; Parkin; phosphorylation; PINK1; ubiquitin

Indexed keywords

DEUBIQUITINASE; LYSINE; PARKIN; PROTEIN KINASE; PROTEIN PINK1; PROTEIN USP15; PROTEIN USP30; PROTEIN USP8; SERINE; UBIQUITIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; CDC34 PROTEIN, HUMAN; ESCRT PROTEIN; MITOCHONDRIAL PROTEIN; PHOSPHOPROTEIN; POLYUBIQUITIN; PROTEINASE; RNF31 PROTEIN, HUMAN; SIGNAL TRANSDUCING ADAPTOR PROTEIN; TAB2 PROTEIN, HUMAN; THIOL ESTER HYDROLASE; TRANSCRIPTION FACTOR; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 6; UBE2N PROTEIN, HUMAN; UBE2V1 PROTEIN, HUMAN; UBIQUITIN CONJUGATING ENZYME; UBIQUITIN PROTEIN LIGASE; UBIQUITIN THIOLESTERASE; USP15 PROTEIN, HUMAN; USP30 PROTEIN, HUMAN; USP8 PROTEIN, HUMAN;

EID: 84922235969     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.15252/embj.201489847     Document Type: Article
Times cited : (255)

References (78)
  • 1
    • 79952301200 scopus 로고    scopus 로고
    • Molecular basis for ubiquitin and ISG15 cross-reactivity in viral ovarian tumor domains
    • Akutsu M, Ye Y, Virdee S, Chin JW, Komander D, (2011) Molecular basis for ubiquitin and ISG15 cross-reactivity in viral ovarian tumor domains. Proc Natl Acad Sci USA 108: 2228-2233
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 2228-2233
    • Akutsu, M.1    Ye, Y.2    Virdee, S.3    Chin, J.W.4    Komander, D.5
  • 2
    • 84898754901 scopus 로고    scopus 로고
    • New insights into ubiquitin E3 ligase mechanism
    • Berndsen CE, Wolberger C, (2014) New insights into ubiquitin E3 ligase mechanism. Nat Struct Mol Biol 21: 301-307
    • (2014) Nat Struct Mol Biol , vol.21 , pp. 301-307
    • Berndsen, C.E.1    Wolberger, C.2
  • 6
    • 59649086030 scopus 로고    scopus 로고
    • Nonproteolytic functions of ubiquitin in cell signaling
    • Chen ZJ, Sun LJ, (2009) Nonproteolytic functions of ubiquitin in cell signaling. Mol Cell 33: 275-286
    • (2009) Mol Cell , vol.33 , pp. 275-286
    • Chen, Z.J.1    Sun, L.J.2
  • 7
    • 84876531457 scopus 로고    scopus 로고
    • PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria
    • Chen Y, Dorn GW, (2013) PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria. Science 340: 471-475
    • (2013) Science , vol.340 , pp. 471-475
    • Chen, Y.1    Dorn, G.W.2
  • 9
    • 0026746290 scopus 로고
    • Structure of a diubiquitin conjugate and a model for interaction with ubiquitin conjugating enzyme (E2)
    • Cook WJ, Jeffrey LC, Carson M, Chen Z, Pickart CM, (1992) Structure of a diubiquitin conjugate and a model for interaction with ubiquitin conjugating enzyme (E2). J Biol Chem 267: 16467-16471
    • (1992) J Biol Chem , vol.267 , pp. 16467-16471
    • Cook, W.J.1    Jeffrey, L.C.2    Carson, M.3    Chen, Z.4    Pickart, C.M.5
  • 10
    • 39449087573 scopus 로고    scopus 로고
    • Direct detection of N-H[...]O=C hydrogen bonds in biomolecules by NMR spectroscopy
    • Cordier F, Nisius L, Dingley AJ, Grzesiek S, (2008) Direct detection of N-H[...]O=C hydrogen bonds in biomolecules by NMR spectroscopy. Nat Protoc 3: 235-241
    • (2008) Nat Protoc , vol.3 , pp. 235-241
    • Cordier, F.1    Nisius, L.2    Dingley, A.J.3    Grzesiek, S.4
  • 12
    • 80054787664 scopus 로고    scopus 로고
    • What genetics tells us about the causes and mechanisms of Parkinson's disease
    • Corti O, Lesage S, Brice A, (2011) What genetics tells us about the causes and mechanisms of Parkinson's disease. Physiol Rev 91: 1161-1218
    • (2011) Physiol Rev , vol.91 , pp. 1161-1218
    • Corti, O.1    Lesage, S.2    Brice, A.3
  • 13
    • 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 GJ, Cameron K, Huang DT, (2012) BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. Nat Struct Mol Biol 19: 876-883
    • (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
  • 14
    • 84855287943 scopus 로고    scopus 로고
    • Ataxin-3 deubiquitination is coupled to parkin ubiquitination via E2 ubiquitin-conjugating enzyme
    • Durcan TM, Kontogiannea M, Bedard N, Wing SS, Fon EA, (2012) Ataxin-3 deubiquitination is coupled to parkin ubiquitination via E2 ubiquitin-conjugating enzyme. J Biol Chem 287: 531-541
    • (2012) J Biol Chem , vol.287 , pp. 531-541
    • Durcan, T.M.1    Kontogiannea, M.2    Bedard, N.3    Wing, S.S.4    Fon, E.A.5
  • 17
    • 33749506057 scopus 로고    scopus 로고
    • Mms2-Ubc13 covalently bound to ubiquitin reveals the structural basis of linkage-specific polyubiquitin chain formation
    • Eddins MJ, Carlile CM, Gomez KM, Pickart CM, Wolberger C, (2006) Mms2-Ubc13 covalently bound to ubiquitin reveals the structural basis of linkage-specific polyubiquitin chain formation. Nat Struct Mol Biol 13: 915-920
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 915-920
    • Eddins, M.J.1    Carlile, C.M.2    Gomez, K.M.3    Pickart, C.M.4    Wolberger, C.5
  • 19
    • 84877313192 scopus 로고    scopus 로고
    • Assembly, analysis and architecture of atypical ubiquitin chains
    • Hospenthal MK, Freund SMV, Komander D, (2013) Assembly, analysis and architecture of atypical ubiquitin chains. Nat Struct Mol Biol 20: 555-565
    • (2013) Nat Struct Mol Biol , vol.20 , pp. 555-565
    • Hospenthal, M.K.1    Freund, S.M.V.2    Komander, D.3
  • 20
    • 84861783400 scopus 로고    scopus 로고
    • Ubiquitin-binding proteins: Decoders of ubiquitin-mediated cellular functions
    • Husnjak K, Dikic I, (2012) Ubiquitin-binding proteins: decoders of ubiquitin-mediated cellular functions. Annu Rev Biochem 81: 291-322
    • (2012) Annu Rev Biochem , vol.81 , pp. 291-322
    • Husnjak, K.1    Dikic, I.2
  • 21
    • 0033594989 scopus 로고    scopus 로고
    • Thermal versus guanidine-induced unfolding of ubiquitin. An analysis in terms of the contributions from charge-charge interactions to protein stability
    • Ibarra-Molero B, Loladze VV, Makhatadze GI, Sanchez-Ruiz JM, (1999) Thermal versus guanidine-induced unfolding of ubiquitin. An analysis in terms of the contributions from charge-charge interactions to protein stability. Biochemistry 38: 8138-8149
    • (1999) Biochemistry , vol.38 , pp. 8138-8149
    • Ibarra-Molero, B.1    Loladze, V.V.2    Makhatadze, G.I.3    Sanchez-Ruiz, J.M.4
  • 27
    • 34547130325 scopus 로고    scopus 로고
    • Certain pairs of ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s) synthesize nondegradable forked ubiquitin chains containing all possible isopeptide linkages
    • Kim HT, Kim KP, Lledias F, Kisselev AF, Scaglione KM, Skowyra D, Gygi SP, Goldberg AL, (2007) Certain pairs of ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s) synthesize nondegradable forked ubiquitin chains containing all possible isopeptide linkages. J Biol Chem 282: 17375-17386
    • (2007) J Biol Chem , vol.282 , pp. 17375-17386
    • Kim, H.T.1    Kim, K.P.2    Lledias, F.3    Kisselev, A.F.4    Scaglione, K.M.5    Skowyra, D.6    Gygi, S.P.7    Goldberg, A.L.8
  • 30
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: Structure and function of the deubiquitinases
    • Komander D, Clague MJ, Urbé S, (2009) Breaking the chains: structure and function of the deubiquitinases. Nat Rev Mol Cell Biol 10: 550-563
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbé, S.3
  • 34
    • 71449095149 scopus 로고    scopus 로고
    • Two-sided ubiquitin binding explains specificity of the TAB 2 NZF domain
    • Kulathu Y, Akutsu M, Bremm A, Hofmann K, Komander D, (2009) Two-sided ubiquitin binding explains specificity of the TAB 2 NZF domain. Nat Struct Mol Biol 16: 1328-1330
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 1328-1330
    • Kulathu, Y.1    Akutsu, M.2    Bremm, A.3    Hofmann, K.4    Komander, D.5
  • 35
    • 84864222562 scopus 로고    scopus 로고
    • Atypical ubiquitylation - The unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages
    • Kulathu Y, Komander D, (2012) Atypical ubiquitylation-the unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages. Nat Rev Mol Cell Biol 13: 508-523
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 508-523
    • Kulathu, Y.1    Komander, D.2
  • 37
    • 4143080425 scopus 로고    scopus 로고
    • AMSH is an endosome-associated ubiquitin isopeptidase
    • McCullough J, Clague MJ, Urbé S, (2004) AMSH is an endosome-associated ubiquitin isopeptidase. J Cell Biol 166: 487-492
    • (2004) J Cell Biol , vol.166 , pp. 487-492
    • McCullough, J.1    Clague, M.J.2    Urbé, S.3
  • 38
    • 67349128620 scopus 로고    scopus 로고
    • Control of the activity of WW-HECT domain E3 ubiquitin ligases by NDFIP proteins
    • Mund T, Pelham HRB, (2009) Control of the activity of WW-HECT domain E3 ubiquitin ligases by NDFIP proteins. EMBO Rep 10: 501-507
    • (2009) EMBO Rep , vol.10 , pp. 501-507
    • Mund, T.1    Pelham, H.R.B.2
  • 39
    • 84866847054 scopus 로고    scopus 로고
    • Key stabilizing elements of protein structure identified through pressure and temperature perturbation of its hydrogen bond network
    • Nisius L, Grzesiek S, (2012) Key stabilizing elements of protein structure identified through pressure and temperature perturbation of its hydrogen bond network. Nat Chem 4: 711-717
    • (2012) Nat Chem , vol.4 , pp. 711-717
    • Nisius, L.1    Grzesiek, S.2
  • 42
    • 0036866606 scopus 로고    scopus 로고
    • Arf, Arl, Arp and Sar proteins: A family of GTP-binding proteins with a structural device for "front-back" communication
    • Pasqualato S, Renault L, Cherfils J, (2002) Arf, Arl, Arp and Sar proteins: a family of GTP-binding proteins with a structural device for "front-back" communication. EMBO Rep 3: 1035-1041
    • (2002) EMBO Rep , vol.3 , pp. 1035-1041
    • Pasqualato, S.1    Renault, L.2    Cherfils, J.3
  • 43
    • 84865781586 scopus 로고    scopus 로고
    • Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis
    • Plechanovova A, Jaffray EG, Tatham MH, Naismith JH, Hay RT, (2012) Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis. Nature 489: 115-120
    • (2012) Nature , vol.489 , pp. 115-120
    • Plechanovova, A.1    Jaffray, E.G.2    Tatham, M.H.3    Naismith, J.H.4    Hay, R.T.5
  • 44
    • 79952407243 scopus 로고    scopus 로고
    • Ubiquitin in motion: Structural studies of the ubiquitin-conjugating enzyme-ubiquitin conjugate
    • Pruneda JN, Stoll KE, Bolton LJ, Brzovic PS, Klevit RE, (2011) Ubiquitin in motion: structural studies of the ubiquitin-conjugating enzyme-ubiquitin conjugate. Biochemistry 50: 1624-1633
    • (2011) Biochemistry , vol.50 , pp. 1624-1633
    • Pruneda, J.N.1    Stoll, K.E.2    Bolton, L.J.3    Brzovic, P.S.4    Klevit, R.E.5
  • 46
    • 84898624312 scopus 로고    scopus 로고
    • Self and nonself: How autophagy targets mitochondria and bacteria
    • Randow F, Youle RJ, (2014) Self and nonself: how autophagy targets mitochondria and bacteria. Cell Host Microbe 15: 403-411
    • (2014) Cell Host Microbe , vol.15 , pp. 403-411
    • Randow, F.1    Youle, R.J.2
  • 52
    • 72449162040 scopus 로고    scopus 로고
    • Structural basis for specific recognition of Lys 63-linked polyubiquitin chains by NZF domains of TAB 2 and TAB 3
    • Sato Y, Yoshikawa A, Yamashita M, Yamagata A, Fukai S, (2009) Structural basis for specific recognition of Lys 63-linked polyubiquitin chains by NZF domains of TAB 2 and TAB 3. EMBO J 28: 3903-3909
    • (2009) EMBO J , vol.28 , pp. 3903-3909
    • Sato, Y.1    Yoshikawa, A.2    Yamashita, M.3    Yamagata, A.4    Fukai, S.5
  • 53
    • 84902716930 scopus 로고    scopus 로고
    • Phosphorylated ubiquitin: A new shade of PINK1 in Parkin activation
    • Sauvé V, Gehring K, (2014) Phosphorylated ubiquitin: a new shade of PINK1 in Parkin activation. Cell Res 24: 1025-1026
    • (2014) Cell Res , vol.24 , pp. 1025-1026
    • Sauvé, V.1    Gehring, K.2
  • 54
    • 67349256160 scopus 로고    scopus 로고
    • Ubiquitin-like protein activation by E1 enzymes: The apex for downstream signalling pathways
    • Schulman BA, Harper JW, (2009) Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways. Nat Rev Mol Cell Biol 10: 319-331
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 319-331
    • Schulman, B.A.1    Harper, J.W.2
  • 56
    • 84867096523 scopus 로고    scopus 로고
    • The E3 ligase HOIP specifies linear ubiquitin chain assembly through its RING-IBR-RING domain and the unique LDD extension
    • Smit JJ, Monteferrario D, Noordermeer SM, van Dijk WJ, van der Reijden BA, Sixma TK, (2012) The E3 ligase HOIP specifies linear ubiquitin chain assembly through its RING-IBR-RING domain and the unique LDD extension. EMBO J 31: 3833-3844
    • (2012) EMBO J , vol.31 , pp. 3833-3844
    • Smit, J.J.1    Monteferrario, D.2    Noordermeer, S.M.3    Van Dijk, W.J.4    Van Der Reijden, B.A.5    Sixma, T.K.6
  • 61
    • 0023644679 scopus 로고
    • Structure of ubiquitin refined at 1.8 A resolution
    • Vijay-Kumar S, Bugg CE, Cook WJ, (1987) Structure of ubiquitin refined at 1.8 A resolution. J Mol Biol 194: 531-544
    • (1987) J Mol Biol , vol.194 , pp. 531-544
    • Vijay-Kumar, S.1    Bugg, C.E.2    Cook, W.J.3
  • 65
    • 84881477223 scopus 로고    scopus 로고
    • Structure of the human Parkin ligase domain in an autoinhibited state
    • Wauer T, Komander D, (2013) Structure of the human Parkin ligase domain in an autoinhibited state. EMBO J 32: 2099-2112
    • (2013) EMBO J , vol.32 , pp. 2099-2112
    • Wauer, T.1    Komander, D.2
  • 66
    • 79953009529 scopus 로고    scopus 로고
    • Crystal structure of a Josephin-ubiquitin complex: Evolutionary restraints on ataxin-3 deubiquitinating activity
    • Weeks SD, Grasty KC, Hernandez-Cuebas L, Loll PJ, (2011) Crystal structure of a Josephin-ubiquitin complex: evolutionary restraints on ataxin-3 deubiquitinating activity. J Biol Chem 286: 4555-4565
    • (2011) J Biol Chem , vol.286 , pp. 4555-4565
    • Weeks, S.D.1    Grasty, K.C.2    Hernandez-Cuebas, L.3    Loll, P.J.4
  • 67
    • 79957949190 scopus 로고    scopus 로고
    • UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids
    • Wenzel DM, Lissounov A, Brzovic PS, Klevit RE, (2011) UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. Nature 474: 105-108
    • (2011) Nature , vol.474 , pp. 105-108
    • Wenzel, D.M.1    Lissounov, A.2    Brzovic, P.S.3    Klevit, R.E.4
  • 68
    • 84858135252 scopus 로고    scopus 로고
    • Following Ariadne's thread: A new perspective on RBR ubiquitin ligases
    • Wenzel DM, Klevit RE, (2012) Following Ariadne's thread: a new perspective on RBR ubiquitin ligases. BMC Biol 10: 24
    • (2012) BMC Biol , vol.10 , pp. 24
    • Wenzel, D.M.1    Klevit, R.E.2
  • 69
    • 84862806447 scopus 로고    scopus 로고
    • The mechanism of OTUB1-mediated inhibition of ubiquitination
    • Wiener R, Zhang X, Wang T, Wolberger C, (2012) The mechanism of OTUB1-mediated inhibition of ubiquitination. Nature 483: 618-622
    • (2012) Nature , vol.483 , pp. 618-622
    • Wiener, R.1    Zhang, X.2    Wang, T.3    Wolberger, C.4
  • 72
    • 72949102636 scopus 로고    scopus 로고
    • Dissection of USP catalytic domains reveals five common insertion points
    • Ye Y, Scheel H, Hofmann K, Komander D, (2009) Dissection of USP catalytic domains reveals five common insertion points. Mol BioSyst 5: 1797-1808
    • (2009) Mol BioSyst , vol.5 , pp. 1797-1808
    • Ye, Y.1    Scheel, H.2    Hofmann, K.3    Komander, D.4
  • 77
    • 84879885169 scopus 로고    scopus 로고
    • Parkin mitochondrial translocation is achieved through a novel catalytic activity coupled mechanism
    • Zheng X, Hunter T, (2013) Parkin mitochondrial translocation is achieved through a novel catalytic activity coupled mechanism. Cell Res 23: 886-897
    • (2013) Cell Res , vol.23 , pp. 886-897
    • Zheng, X.1    Hunter, T.2
  • 78
    • 84905384868 scopus 로고    scopus 로고
    • Pink1, the first ubiquitin kinase
    • Zheng X, Hunter T, (2014) Pink1, the first ubiquitin kinase. EMBO J 33: 1621-1623
    • (2014) EMBO J , vol.33 , pp. 1621-1623
    • Zheng, X.1    Hunter, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.