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Volumn 21, Issue 1, 2017, Pages 59-72

Erratum: The Ubiquitin Ligase Smurf1 Functions in Selective Autophagy of Mycobacterium tuberculosis and Anti-tuberculous Host Defense (Cell Host & Microbe (2017) 21(1) (59–72) (S1931312816304772) (10.1016/j.chom.2016.11.002));The Ubiquitin Ligase Smurf1 Functions in Selective Autophagy of Mycobacterium tuberculosis and Anti-tuberculous Host Defense

Author keywords

K48 ubiquitin; M. tuberculosis; selective autophagy; Smurf1

Indexed keywords

ADAPTOR PROTEIN; AUTOPHAGY RELATED PROTEIN; LC3 PROTEIN; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 1; NBR1 PROTEIN; POLYUBIQUITIN; PROTEASOME; UBIQUITIN PROTEIN LIGASE; UBIQUITIN PROTEIN LIGASE SMURF1; UNCLASSIFIED DRUG; LAMP1 PROTEIN, MOUSE; LYSOSOME ASSOCIATED MEMBRANE PROTEIN; MAP1LC3 PROTEIN, MOUSE; MICROTUBULE ASSOCIATED PROTEIN; NBR1 PROTEIN, MOUSE; PEPTIDE; PROTEIN; SMURF1 PROTEIN, MOUSE; TAT-BH4 PEPTIDE;

EID: 85009836949     PISSN: 19313128     EISSN: 19346069     Source Type: Journal    
DOI: 10.1016/j.chom.2017.08.005     Document Type: Erratum
Times cited : (167)

References (42)
  • 1
    • 84899553358 scopus 로고    scopus 로고
    • Host and bacterial proteins that repress recruitment of LC3 to Shigella early during infection
    • Baxt, L.A., Goldberg, M.B., Host and bacterial proteins that repress recruitment of LC3 to Shigella early during infection. PLoS One, 9, 2014, e94653.
    • (2014) PLoS One , vol.9 , pp. e94653
    • Baxt, L.A.1    Goldberg, M.B.2
  • 2
    • 84879072668 scopus 로고    scopus 로고
    • A Smurf1 tale: function and regulation of an ubiquitin ligase in multiple cellular networks
    • Cao, Y., Zhang, L., A Smurf1 tale: function and regulation of an ubiquitin ligase in multiple cellular networks. Cell. Mol. Life Sci. 70 (2013), 2305–2317.
    • (2013) Cell. Mol. Life Sci. , vol.70 , pp. 2305-2317
    • Cao, Y.1    Zhang, L.2
  • 4
    • 78751697205 scopus 로고    scopus 로고
    • Phosphorylation of E3 ligase Smurf1 switches its substrate preference in support of axon development
    • Cheng, P.L., Lu, H., Shelly, M., Gao, H., Poo, M.M., Phosphorylation of E3 ligase Smurf1 switches its substrate preference in support of axon development. Neuron 69 (2011), 231–243.
    • (2011) Neuron , vol.69 , pp. 231-243
    • Cheng, P.L.1    Lu, H.2    Shelly, M.3    Gao, H.4    Poo, M.M.5
  • 5
    • 84866559918 scopus 로고    scopus 로고
    • Cytosolic clearance of replication-deficient mutants reveals Francisella tularensis interactions with the autophagic pathway
    • Chong, A., Wehrly, T.D., Child, R., Hansen, B., Hwang, S., Virgin, H.W., Celli, J., Cytosolic clearance of replication-deficient mutants reveals Francisella tularensis interactions with the autophagic pathway. Autophagy 8 (2012), 1342–1356.
    • (2012) Autophagy , vol.8 , pp. 1342-1356
    • Chong, A.1    Wehrly, T.D.2    Child, R.3    Hansen, B.4    Hwang, S.5    Virgin, H.W.6    Celli, J.7
  • 7
    • 84901024006 scopus 로고    scopus 로고
    • Smurf1-mediated axin ubiquitination requires Smurf1 C2 domain and is cell cycle-dependent
    • Fei, C., He, X., Xie, S., Miao, H., Zhou, Z., Li, L., Smurf1-mediated axin ubiquitination requires Smurf1 C2 domain and is cell cycle-dependent. J. Biol. Chem. 289 (2014), 14170–14177.
    • (2014) J. Biol. Chem. , vol.289 , pp. 14170-14177
    • Fei, C.1    He, X.2    Xie, S.3    Miao, H.4    Zhou, Z.5    Li, L.6
  • 8
    • 84924632659 scopus 로고    scopus 로고
    • Polyubiquitination of lysine-48 is an essential but indirect signal for MHC class I antigen processing
    • Fiebiger, B.M., Pfister, H., Behrends, U., Mautner, J., Polyubiquitination of lysine-48 is an essential but indirect signal for MHC class I antigen processing. Eur. J. Immunol. 45 (2015), 716–727.
    • (2015) Eur. J. Immunol. , vol.45 , pp. 716-727
    • Fiebiger, B.M.1    Pfister, H.2    Behrends, U.3    Mautner, J.4
  • 9
    • 84882896267 scopus 로고    scopus 로고
    • Cyclic GMP-AMP synthase is an innate immune sensor of HIV and other retroviruses
    • Gao, D., Wu, J., Wu, Y.T., Du, F., Aroh, C., Yan, N., Sun, L., Chen, Z.J., Cyclic GMP-AMP synthase is an innate immune sensor of HIV and other retroviruses. Science 341 (2013), 903–906.
    • (2013) Science , vol.341 , pp. 903-906
    • Gao, D.1    Wu, J.2    Wu, Y.T.3    Du, F.4    Aroh, C.5    Yan, N.6    Sun, L.7    Chen, Z.J.8
  • 10
    • 84899131967 scopus 로고    scopus 로고
    • Autophagy in antimicrobial immunity
    • Gomes, L.C., Dikic, I., Autophagy in antimicrobial immunity. Mol. Cell 54 (2014), 224–233.
    • (2014) Mol. Cell , vol.54 , pp. 224-233
    • Gomes, L.C.1    Dikic, I.2
  • 11
    • 84965013771 scopus 로고    scopus 로고
    • The recognition of ubiquitinated proteins by the proteasome
    • Grice, G.L., Nathan, J.A., The recognition of ubiquitinated proteins by the proteasome. Cell. Mol. Life Sci. 73 (2016), 3497–3506.
    • (2016) Cell. Mol. Life Sci. , vol.73 , pp. 3497-3506
    • Grice, G.L.1    Nathan, J.A.2
  • 12
    • 10944253145 scopus 로고    scopus 로고
    • Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages
    • Gutierrez, M.G., Master, S.S., Singh, S.B., Taylor, G.A., Colombo, M.I., Deretic, V., Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages. Cell 119 (2004), 753–766.
    • (2004) Cell , vol.119 , pp. 753-766
    • Gutierrez, M.G.1    Master, S.S.2    Singh, S.B.3    Taylor, G.A.4    Colombo, M.I.5    Deretic, V.6
  • 14
    • 58349085112 scopus 로고    scopus 로고
    • Modulation of ubiquitin dynamics and suppression of DALIS formation by the Legionella pneumophila Dot/Icm system
    • Ivanov, S.S., Roy, C.R., Modulation of ubiquitin dynamics and suppression of DALIS formation by the Legionella pneumophila Dot/Icm system. Cell. Microbiol. 11 (2009), 261–278.
    • (2009) Cell. Microbiol. , vol.11 , pp. 261-278
    • Ivanov, S.S.1    Roy, C.R.2
  • 15
    • 62049084947 scopus 로고    scopus 로고
    • Autophagy enhances the efficacy of BCG vaccine by increasing peptide presentation in mouse dendritic cells
    • Jagannath, C., Lindsey, D.R., Dhandayuthapani, S., Xu, Y., Hunter, R.L. Jr., Eissa, N.T., Autophagy enhances the efficacy of BCG vaccine by increasing peptide presentation in mouse dendritic cells. Nat. Med. 15 (2009), 267–276.
    • (2009) Nat. Med. , vol.15 , pp. 267-276
    • Jagannath, C.1    Lindsey, D.R.2    Dhandayuthapani, S.3    Xu, Y.4    Hunter, R.L.5    Eissa, N.T.6
  • 17
    • 84880896860 scopus 로고    scopus 로고
    • Host and bacterial factors that regulate LC3 recruitment to Listeria monocytogenes during the early stages of macrophage infection
    • Lam, G.Y., Cemma, M., Muise, A.M., Higgins, D.E., Brumell, J.H., Host and bacterial factors that regulate LC3 recruitment to Listeria monocytogenes during the early stages of macrophage infection. Autophagy 9 (2013), 985–995.
    • (2013) Autophagy , vol.9 , pp. 985-995
    • Lam, G.Y.1    Cemma, M.2    Muise, A.M.3    Higgins, D.E.4    Brumell, J.H.5
  • 18
    • 33947134377 scopus 로고    scopus 로고
    • Autophagy-dependent viral recognition by plasmacytoid dendritic cells
    • Lee, H.K., Lund, J.M., Ramanathan, B., Mizushima, N., Iwasaki, A., Autophagy-dependent viral recognition by plasmacytoid dendritic cells. Science 315 (2007), 1398–1401.
    • (2007) Science , vol.315 , pp. 1398-1401
    • Lee, H.K.1    Lund, J.M.2    Ramanathan, B.3    Mizushima, N.4    Iwasaki, A.5
  • 19
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • Levine, B., Kroemer, G., Autophagy in the pathogenesis of disease. Cell 132 (2008), 27–42.
    • (2008) Cell , vol.132 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 20
    • 78751672975 scopus 로고    scopus 로고
    • Autophagy in immunity and inflammation
    • Levine, B., Mizushima, N., Virgin, H.W., Autophagy in immunity and inflammation. Nature 469 (2011), 323–335.
    • (2011) Nature , vol.469 , pp. 323-335
    • Levine, B.1    Mizushima, N.2    Virgin, H.W.3
  • 22
    • 79955775161 scopus 로고    scopus 로고
    • Pivotal role of the C2 domain of the Smurf1 ubiquitin ligase in substrate selection
    • Lu, K., Li, P., Zhang, M., Xing, G., Li, X., Zhou, W., Bartlam, M., Zhang, L., Rao, Z., He, F., Pivotal role of the C2 domain of the Smurf1 ubiquitin ligase in substrate selection. J. Biol. Chem. 286 (2011), 16861–16870.
    • (2011) J. Biol. Chem. , vol.286 , pp. 16861-16870
    • Lu, K.1    Li, P.2    Zhang, M.3    Xing, G.4    Li, X.5    Zhou, W.6    Bartlam, M.7    Zhang, L.8    Rao, Z.9    He, F.10
  • 25
    • 0031935546 scopus 로고    scopus 로고
    • Resistance ranking of some common inbred mouse strains to Mycobacterium tuberculosis and relationship to major histocompatibility complex haplotype and Nramp1 genotype
    • Medina, E., North, R.J., Resistance ranking of some common inbred mouse strains to Mycobacterium tuberculosis and relationship to major histocompatibility complex haplotype and Nramp1 genotype. Immunology 93 (1998), 270–274.
    • (1998) Immunology , vol.93 , pp. 270-274
    • Medina, E.1    North, R.J.2
  • 26
    • 84864060156 scopus 로고    scopus 로고
    • The Salmonella deubiquitinase SseL inhibits selective autophagy of cytosolic aggregates
    • Mesquita, F.S., Thomas, M., Sachse, M., Santos, A.J.M., Figueira, R., Holden, D.W., The Salmonella deubiquitinase SseL inhibits selective autophagy of cytosolic aggregates. PLoS Pathog., 8, 2012, e1002743.
    • (2012) PLoS Pathog. , vol.8 , pp. e1002743
    • Mesquita, F.S.1    Thomas, M.2    Sachse, M.3    Santos, A.J.M.4    Figueira, R.5    Holden, D.W.6
  • 27
    • 1542283812 scopus 로고    scopus 로고
    • In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker
    • Mizushima, N., Yamamoto, A., Matsui, M., Yoshimori, T., Ohsumi, Y., In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker. Mol. Biol. Cell 15 (2004), 1101–1111.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1101-1111
    • Mizushima, N.1    Yamamoto, A.2    Matsui, M.3    Yoshimori, T.4    Ohsumi, Y.5
  • 30
    • 2342464290 scopus 로고    scopus 로고
    • Recognition of bacteria in the cytosol of mammalian cells by the ubiquitin system
    • Perrin, A.J., Jiang, X., Birmingham, C.L., So, N.S., Brumell, J.H., Recognition of bacteria in the cytosol of mammalian cells by the ubiquitin system. Curr. Biol. 14 (2004), 806–811.
    • (2004) Curr. Biol. , vol.14 , pp. 806-811
    • Perrin, A.J.1    Jiang, X.2    Birmingham, C.L.3    So, N.S.4    Brumell, J.H.5
  • 34
    • 0242268398 scopus 로고    scopus 로고
    • Acute infection and macrophage subversion by Mycobacterium tuberculosis require a specialized secretion system
    • Stanley, S.A., Raghavan, S., Hwang, W.W., Cox, J.S., Acute infection and macrophage subversion by Mycobacterium tuberculosis require a specialized secretion system. Proc. Natl. Acad. Sci. USA 100 (2003), 13001–13006.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13001-13006
    • Stanley, S.A.1    Raghavan, S.2    Hwang, W.W.3    Cox, J.S.4
  • 36
    • 79960359069 scopus 로고    scopus 로고
    • Binding of RhoA by the C2 domain of E3 ligase Smurf1 is essential for Smurf1-regulated RhoA ubiquitination and cell protrusive activity
    • Tian, M., Bai, C., Lin, Q., Lin, H., Liu, M., Ding, F., Wang, H.R., Binding of RhoA by the C2 domain of E3 ligase Smurf1 is essential for Smurf1-regulated RhoA ubiquitination and cell protrusive activity. FEBS Lett. 585 (2011), 2199–2204.
    • (2011) FEBS Lett. , vol.585 , pp. 2199-2204
    • Tian, M.1    Bai, C.2    Lin, Q.3    Lin, H.4    Liu, M.5    Ding, F.6    Wang, H.R.7
  • 39
    • 84865220380 scopus 로고    scopus 로고
    • Extracellular M. tuberculosis DNA targets bacteria for autophagy by activating the host DNA-sensing pathway
    • Watson, R.O., Manzanillo, P.S., Cox, J.S., Extracellular M. tuberculosis DNA targets bacteria for autophagy by activating the host DNA-sensing pathway. Cell 150 (2012), 803–815.
    • (2012) Cell , vol.150 , pp. 803-815
    • Watson, R.O.1    Manzanillo, P.S.2    Cox, J.S.3
  • 40
    • 84901471156 scopus 로고    scopus 로고
    • Parkin and mitochondrial quality control: toward assembling the puzzle
    • Winklhofer, K.F., Parkin and mitochondrial quality control: toward assembling the puzzle. Trends Cell Biol. 24 (2014), 332–341.
    • (2014) Trends Cell Biol. , vol.24 , pp. 332-341
    • Winklhofer, K.F.1
  • 41
    • 17044414102 scopus 로고    scopus 로고
    • Ubiquitin ligase Smurf1 controls osteoblast activity and bone homeostasis by targeting MEKK2 for degradation
    • Yamashita, M., Ying, S.X., Zhang, G.M., Li, C., Cheng, S.Y., Deng, C.X., Zhang, Y.E., Ubiquitin ligase Smurf1 controls osteoblast activity and bone homeostasis by targeting MEKK2 for degradation. Cell 121 (2005), 101–113.
    • (2005) Cell , vol.121 , pp. 101-113
    • Yamashita, M.1    Ying, S.X.2    Zhang, G.M.3    Li, C.4    Cheng, S.Y.5    Deng, C.X.6    Zhang, Y.E.7
  • 42
    • 84861210911 scopus 로고    scopus 로고
    • Smurf1 protein negatively regulates interferon-γ signaling through promoting STAT1 protein ubiquitination and degradation
    • Yuan, C., Qi, J., Zhao, X., Gao, C., Smurf1 protein negatively regulates interferon-γ signaling through promoting STAT1 protein ubiquitination and degradation. J. Biol. Chem. 287 (2012), 17006–17015.
    • (2012) J. Biol. Chem. , vol.287 , pp. 17006-17015
    • Yuan, C.1    Qi, J.2    Zhao, X.3    Gao, C.4


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