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Volumn 106, Issue 12, 2009, Pages 4864-4869

A family of Salmonella virulence factors functions as a distinct class of autoregulated E3 ubiquitin ligases

Author keywords

Crystallography; Microbial pathogenesis; SspH2; Type iii secretion

Indexed keywords

BACTERIAL PROTEIN; CYSTEINE; LEUCINE; SALMONELLA SSPH2 PROTEIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; UBIQUITIN PROTEIN LIGASE; VIRULENCE FACTOR;

EID: 63849280748     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0811058106     Document Type: Article
Times cited : (147)

References (36)
  • 1
    • 33745156511 scopus 로고    scopus 로고
    • Ubiquitin and SUMO systems in the regulation of mitotic checkpoints
    • Gutierrez GJ, Ronai Z (2006) Ubiquitin and SUMO systems in the regulation of mitotic checkpoints. Trends Biochem Sci 31:324-332.
    • (2006) Trends Biochem Sci , vol.31 , pp. 324-332
    • Gutierrez, G.J.1    Ronai, Z.2
  • 2
    • 33846471122 scopus 로고    scopus 로고
    • Proteasome-independent functions of ubiquitin in endocytosis and signaling
    • Mukhopadhyay D, Riezman H (2007) Proteasome-independent functions of ubiquitin in endocytosis and signaling. Science 315:201-205.
    • (2007) Science , vol.315 , pp. 201-205
    • Mukhopadhyay, D.1    Riezman, H.2
  • 3
    • 34548857955 scopus 로고    scopus 로고
    • Ubiquitin ligases in cancer: Ushers for degradation
    • Newton K, Vucic D (2007) Ubiquitin ligases in cancer: Ushers for degradation. Cancer Invest 25:502-513.
    • (2007) Cancer Invest , vol.25 , pp. 502-513
    • Newton, K.1    Vucic, D.2
  • 4
    • 33748336875 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway in cell cycle control
    • Reed SI (2006) The ubiquitin-proteasome pathway in cell cycle control. Results Probl Cell Differ 42:147-181.
    • (2006) Results Probl Cell Differ , vol.42 , pp. 147-181
    • Reed, S.I.1
  • 5
    • 19644384744 scopus 로고    scopus 로고
    • E3 ubiquitin ligases as regulators of membrane protein trafficking and degradation
    • d'Azzo A, Bongiovanni A, Nastasi T (2005) E3 ubiquitin ligases as regulators of membrane protein trafficking and degradation. Traffic 6:429-441.
    • (2005) Traffic , vol.6 , pp. 429-441
    • d'Azzo, A.1    Bongiovanni, A.2    Nastasi, T.3
  • 7
    • 34248379575 scopus 로고    scopus 로고
    • Ubiquitin and ubiquitin-like proteins in protein regulation
    • Herrmann J, Lerman LO, Lerman A (2007) Ubiquitin and ubiquitin-like proteins in protein regulation. CircRes100:1276-1291.
    • (2007) CircRes100 , pp. 1276-1291
    • Herrmann, J.1    Lerman, L.O.2    Lerman, A.3
  • 8
    • 23144449208 scopus 로고    scopus 로고
    • Ubiquitin and ubiquitin-like proteins as multifunctional signals
    • Welchman RL, Gordon C, Mayer RJ (2005) Ubiquitin and ubiquitin-like proteins as multifunctional signals. Nat Rev Mol Cell Biol 6:599-609.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 599-609
    • Welchman, R.L.1    Gordon, C.2    Mayer, R.J.3
  • 9
    • 33846574355 scopus 로고    scopus 로고
    • Exploitation of eukaryotic ubiquitin signaling pathways by effectors translocated by bacterial type III and type IV secretion systems
    • Angot A, Vergunst A, Genin S, Peeters N (2007) Exploitation of eukaryotic ubiquitin signaling pathways by effectors translocated by bacterial type III and type IV secretion systems. PLoS Pathog 3:e3.
    • (2007) PLoS Pathog , vol.3
    • Angot, A.1    Vergunst, A.2    Genin, S.3    Peeters, N.4
  • 10
    • 37849010910 scopus 로고    scopus 로고
    • Crystal structure of SopA, a Salmonella effector protein mimicking a eukaryotic ubiquitin ligase
    • Diao J, Zhang Y, Huibregtse JM, Zhou D, Chen J (2008) Crystal structure of SopA, a Salmonella effector protein mimicking a eukaryotic ubiquitin ligase. Nat Struct Mol Biol 15:65-70.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 65-70
    • Diao, J.1    Zhang, Y.2    Huibregtse, J.M.3    Zhou, D.4    Chen, J.5
  • 11
    • 30844458212 scopus 로고    scopus 로고
    • A bacterial inhibitor of host programmed cell death defenses is an E3 ubiquitin ligase
    • Janjusevic R, Abramovitch RB, Martin GB, Stebbins CE (2006) A bacterial inhibitor of host programmed cell death defenses is an E3 ubiquitin ligase. Science 311:222-226.
    • (2006) Science , vol.311 , pp. 222-226
    • Janjusevic, R.1    Abramovitch, R.B.2    Martin, G.B.3    Stebbins, C.E.4
  • 13
    • 33750034105 scopus 로고    scopus 로고
    • The inflammation- associated Salmonella SopA is a HECT-like E3 ubiquitin ligase
    • Zhang Y, Higashide WM, McCormick BA, Chen J, Zhou D (2006) The inflammation- associated Salmonella SopA is a HECT-like E3 ubiquitin ligase. Mol Micro biol 62:786-793.
    • (2006) Mol Micro biol , vol.62 , pp. 786-793
    • Zhang, Y.1    Higashide, W.M.2    McCormick, B.A.3    Chen, J.4    Zhou, D.5
  • 14
    • 0344413859 scopus 로고    scopus 로고
    • Temporal regulation of salmonella virulence effector function by proteasome-dependent protein degradation
    • Kubori T, Galan JE (2003) Temporal regulation of salmonella virulence effector function by proteasome-dependent protein degradation. Cell 115:333-342.
    • (2003) Cell , vol.115 , pp. 333-342
    • Kubori, T.1    Galan, J.E.2
  • 15
    • 64249106114 scopus 로고    scopus 로고
    • Diversification of a Salmonella effector protein function by ubiquitin-dependent differential localization
    • Patel J, Hueffer K, Lam T, Galán J (2009) Diversification of a Salmonella effector protein function by ubiquitin-dependent differential localization. Cell, inpress.
    • (2009) Cell, inpress
    • Patel, J.1    Hueffer, K.2    Lam, T.3    Galán, J.4
  • 16
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman MH, Ciechanover A (2002) The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction. Physiol Rev 82:373-428.
    • (2002) Physiol Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 17
    • 23844540675 scopus 로고    scopus 로고
    • Structural biology of ubiquitin-protein ligases
    • Pavletich NP (2002) Structural biology of ubiquitin-protein ligases. Harvey Lect 98:65- 102.
    • (2002) Harvey Lect , vol.98 , pp. 65-102
    • Pavletich, N.P.1
  • 18
    • 0032701087 scopus 로고    scopus 로고
    • Salmonella typhimurium leucine-rich repeat proteins are targeted to the SPI1 and SPI2 type III secretion systems
    • Miao EA, et al. (1999) Salmonella typhimurium leucine-rich repeat proteins are targeted to the SPI1 and SPI2 type III secretion systems. Mol Microbiol 34:850-864.
    • (1999) Mol Microbiol , vol.34 , pp. 850-864
    • Miao, E.A.1
  • 19
    • 33645551769 scopus 로고    scopus 로고
    • A Salmonella type III secretion effector interacts with the mammalian serine/threonine protein kinase PKN1
    • Haraga A, Miller SI (2006) A Salmonella type III secretion effector interacts with the mammalian serine/threonine protein kinase PKN1. Cell Microbiol 8:837-846.
    • (2006) Cell Microbiol , vol.8 , pp. 837-846
    • Haraga, A.1    Miller, S.I.2
  • 20
    • 0037772375 scopus 로고    scopus 로고
    • Salmonella effectors translocated across the vacuolar membrane interact with the actin cytoskeleton
    • Miao E, et al. (2003) Salmonella effectors translocated across the vacuolar membrane interact with the actin cytoskeleton. Mol Microbiol 48:401-415.
    • (2003) Mol Microbiol , vol.48 , pp. 401-415
    • Miao, E.1
  • 21
    • 13444254300 scopus 로고    scopus 로고
    • PDBsum more: New summaries and analyses of the known 3D structures of proteins and nucleic acids
    • Laskowski RA, Chistyakov VV, Thornton JM (2005) PDBsum more: New summaries and analyses of the known 3D structures of proteins and nucleic acids. Nucleic Acids Res 33:D266-268.
    • (2005) Nucleic Acids Res , vol.33
    • Laskowski, R.A.1    Chistyakov, V.V.2    Thornton, J.M.3
  • 22
    • 0035965144 scopus 로고    scopus 로고
    • Unusual molecular architecture of the Yersinia pestis cytotoxin YopM: A leucine-rich repeat protein with the shortest repeating unit
    • Evdokimov AG, Anderson DE, Routzahn KM, Waugh DS (2001) Unusual molecular architecture of the Yersinia pestis cytotoxin YopM: A leucine-rich repeat protein with the shortest repeating unit. J Mol Biol 312:807-821.
    • (2001) J Mol Biol , vol.312 , pp. 807-821
    • Evdokimov, A.G.1    Anderson, D.E.2    Routzahn, K.M.3    Waugh, D.S.4
  • 23
    • 0028871926 scopus 로고
    • Dali: A network tool for protein structure comparison
    • Holm L, Sander C (1995) Dali: A network tool for protein structure comparison. Trends Biochem Sci 20:478-480.
    • (1995) Trends Biochem Sci , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 24
    • 0035692811 scopus 로고    scopus 로고
    • The leucine-rich repeat as a protein recognition motif
    • Kobe B, Kajava AV (2001) The leucine-rich repeat as a protein recognition motif. Curr Opin Struct Biol 11:725-732.
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 725-732
    • Kobe, B.1    Kajava, A.V.2
  • 25
    • 23944453840 scopus 로고    scopus 로고
    • The HERC proteins: Functional and evolutionary insights
    • Garcia-Gonzalo FR, Rosa JL (2005) The HERC proteins: Functional and evolutionary insights. Cell Mol Life Sci 62:1826-1838.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 1826-1838
    • Garcia-Gonzalo, F.R.1    Rosa, J.L.2
  • 26
    • 1842591240 scopus 로고    scopus 로고
    • The Nedd4 family of E3 ubiquitin ligases: Functional diversity within a common modular architecture
    • Ingham RJ, Gish G, Pawson T (2004) The Nedd4 family of E3 ubiquitin ligases: Functional diversity within a common modular architecture. Oncogene 23:1972-1984.
    • (2004) Oncogene , vol.23 , pp. 1972-1984
    • Ingham, R.J.1    Gish, G.2    Pawson, T.3
  • 27
    • 33745089231 scopus 로고    scopus 로고
    • Regulation of functional diversity within the Nedd4 family by accessory and adaptor proteins
    • Shearwin-Whyatt L, Dalton HE, Foot N, Kumar S (2006) Regulation of functional diversity within the Nedd4 family by accessory and adaptor proteins. Bioessays 28:617-628.
    • (2006) Bioessays , vol.28 , pp. 617-628
    • Shearwin-Whyatt, L.1    Dalton, H.E.2    Foot, N.3    Kumar, S.4
  • 28
    • 34547958577 scopus 로고    scopus 로고
    • Autoinhibition of the HECT-type ubiquitin ligase Smurf2 through its C2 domain
    • Wiesner S, et al. (2007) Autoinhibition of the HECT-type ubiquitin ligase Smurf2 through its C2 domain. Cell 130:651-662.
    • (2007) Cell , vol.130 , pp. 651-662
    • Wiesner, S.1
  • 29
    • 57149098210 scopus 로고    scopus 로고
    • Structure of a Shigella effector reveals a new class of ubiquitin ligases
    • Zhu Y, et al. (2008) Structure of a Shigella effector reveals a new class of ubiquitin ligases. Nat Struct Mol Biol 15:1302-1308.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 1302-1308
    • Zhu, Y.1
  • 30
    • 57149105701 scopus 로고    scopus 로고
    • Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases
    • Singer AU, et al. (2008) Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases. Nat Struct Mol Biol 15:1293-1301.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 1293-1301
    • Singer, A.U.1
  • 31
    • 2342423344 scopus 로고    scopus 로고
    • Illuminating the evolutionary history of chlamydiae
    • Horn M, et al. (2004) Illuminating the evolutionary history of chlamydiae. Science 304:728-730.
    • (2004) Science , vol.304 , pp. 728-730
    • Horn, M.1
  • 32
    • 0025977037 scopus 로고
    • Eukaryotic proteins expressed in Escherichia coli:An improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase
    • Guan KL, Dixon JE (1991) Eukaryotic proteins expressed in Escherichia coli:An improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase. Ann Biochem 192:262-267.
    • (1991) Ann Biochem , vol.192 , pp. 262-267
    • Guan, K.L.1    Dixon, J.E.2
  • 33
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy AJ, et al. (2007) Phaser crystallographic software. J Appl Cryst 40:658-674.
    • (2007) J Appl Cryst , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 34
    • 50249136103 scopus 로고    scopus 로고
    • Langer G, Cohen SX, Lamzin VS, Perrakis A (2008) Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7. Nat Protoc 3:1171-1179
    • Langer G, Cohen SX, Lamzin VS, Perrakis A (2008) Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7. Nat Protoc 3:1171-1179.
  • 35
    • 16644364842 scopus 로고    scopus 로고
    • Vagin AA, et al. (2004) REFMAC5 dictionary: Organization of prior chemical knowledge and guidelines for its use. Acta Crystallogr D Biol Crystallogr 60 (Pt 12 Pt 1):2184-2195.
    • Vagin AA, et al. (2004) REFMAC5 dictionary: Organization of prior chemical knowledge and guidelines for its use. Acta Crystallogr D Biol Crystallogr 60 (Pt 12 Pt 1):2184-2195.
  • 36
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Pt 1
    • Emsley P, Cowtan K (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60(Pt 12 Pt 1):2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , Issue.PART 12 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.