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Volumn 11, Issue 6, 2015, Pages

Systems-wide analysis of BCR signalosomes and downstream phosphorylation and ubiquitylation

Author keywords

BCL10; BCR; phosphorylation; RAB7A; ubiquitylation

Indexed keywords

ANKRD13A PROTEIN, HUMAN; BCL10 PROTEIN, HUMAN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LYMPHOCYTE ANTIGEN RECEPTOR; MEMBRANE PROTEIN; RNF31 PROTEIN, HUMAN; SIGNAL TRANSDUCING ADAPTOR PROTEIN; UBIQUITIN PROTEIN LIGASE;

EID: 84934295586     PISSN: None     EISSN: 17444292     Source Type: Journal    
DOI: 10.15252/msb.20145880     Document Type: Article
Times cited : (96)

References (91)
  • 2
    • 84861897793 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics and network biology
    • Bensimon A, Heck AJ, Aebersold R, (2012) Mass spectrometry-based proteomics and network biology. Annu Rev Biochem 81: 379-405
    • (2012) Annu Rev Biochem , vol.81 , pp. 379-405
    • Bensimon, A.1    Heck, A.J.2    Aebersold, R.3
  • 6
    • 84902275313 scopus 로고    scopus 로고
    • Targeting the B-cell receptor signaling pathway in B lymphoid malignancies
    • Buchner M, Muschen M, (2014) Targeting the B-cell receptor signaling pathway in B lymphoid malignancies. Curr Opin Hematol 21: 341-349
    • (2014) Curr Opin Hematol , vol.21 , pp. 341-349
    • Buchner, M.1    Muschen, M.2
  • 7
    • 0035865135 scopus 로고    scopus 로고
    • Rab-interacting lysosomal protein (RILP): The Rab7 effector required for transport to lysosomes
    • Cantalupo G, Alifano P, Roberti V, Bruni CB, Bucci C, (2001) Rab-interacting lysosomal protein (RILP): the Rab7 effector required for transport to lysosomes. EMBO J 20: 683-693
    • (2001) EMBO J , vol.20 , pp. 683-693
    • Cantalupo, G.1    Alifano, P.2    Roberti, V.3    Bruni, C.B.4    Bucci, C.5
  • 9
    • 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
  • 10
    • 77952956167 scopus 로고    scopus 로고
    • Decoding signalling networks by mass spectrometry-based proteomics
    • Choudhary C, Mann M, (2010) Decoding signalling networks by mass spectrometry-based proteomics. Nat Rev Mol Cell Biol 11: 427-439
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 427-439
    • Choudhary, C.1    Mann, M.2
  • 12
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox J, Mann M, (2008) MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat Biotechnol 26: 1367-1372
    • (2008) Nat Biotechnol , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 15
  • 17
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • Elias JE, Gygi SP, (2007) Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat Methods 4: 207-214
    • (2007) Nat Methods , vol.4 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 23
    • 0034806291 scopus 로고    scopus 로고
    • B cell receptor signaling and autoimmunity
    • Hasler P, Zouali M, (2001) B cell receptor signaling and autoimmunity. FASEB J 15: 2085-2098
    • (2001) FASEB J , vol.15 , pp. 2085-2098
    • Hasler, P.1    Zouali, M.2
  • 25
    • 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 MS, (2009) Efficient protection and isolation of ubiquitylated proteins using tandem ubiquitin-binding entities. EMBO Rep 10: 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
  • 26
    • 79960944389 scopus 로고    scopus 로고
    • HOIL-1L interacting protein (HOIP) is essential for CD40 signaling
    • Hostager BS, Kashiwada M, Colgan JD, Rothman PB, (2011) HOIL-1L interacting protein (HOIP) is essential for CD40 signaling. PLoS ONE 6: e23061
    • (2011) PLoS ONE , vol.6 , pp. e23061
    • Hostager, B.S.1    Kashiwada, M.2    Colgan, J.D.3    Rothman, P.B.4
  • 27
    • 58549112996 scopus 로고    scopus 로고
    • Bioinformatics enrichment tools: Paths toward the comprehensive functional analysis of large gene lists
    • Huang DW, Sherman BT, Lempicki RA, (2009a) Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists. Nucleic Acids Res 37: 1-13
    • (2009) Nucleic Acids Res , vol.37 , pp. 1-13
    • Huang, D.W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 28
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • Huang DW, Sherman BT, Lempicki RA, (2009b) Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat Protoc 4: 44-57
    • (2009) Nat Protoc , vol.4 , pp. 44-57
    • Huang, D.W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 29
    • 84905264803 scopus 로고    scopus 로고
    • Convergence of ubiquitylation and phosphorylation signaling in rapamycin-treated yeast cells
    • Iesmantavicius V, Weinert BT, Choudhary C, (2014) Convergence of ubiquitylation and phosphorylation signaling in rapamycin-treated yeast cells. Mol Cell Proteomics 13: 1979-1992
    • (2014) Mol Cell Proteomics , vol.13 , pp. 1979-1992
    • Iesmantavicius, V.1    Weinert, B.T.2    Choudhary, C.3
  • 30
    • 84905036773 scopus 로고    scopus 로고
    • Linear ubiquitin chains. NF-kappaB signalling, cell death and beyond
    • Iwai K, Fujita H, Sasaki Y, (2014) Linear ubiquitin chains. NF-kappaB signalling, cell death and beyond. Nat Rev Mol Cell Biol 15: 503-508
    • (2014) Nat Rev Mol Cell Biol , vol.15 , pp. 503-508
    • Iwai, K.1    Fujita, H.2    Sasaki, Y.3
  • 31
    • 33344475413 scopus 로고    scopus 로고
    • Differential modification of Ras proteins by ubiquitination
    • Jura N, Scotto-Lavino E, Sobczyk A, Bar-Sagi D, (2006) Differential modification of Ras proteins by ubiquitination. Mol Cell 21: 679-687
    • (2006) Mol Cell , vol.21 , pp. 679-687
    • Jura, N.1    Scotto-Lavino, E.2    Sobczyk, A.3    Bar-Sagi, D.4
  • 32
    • 0030695339 scopus 로고    scopus 로고
    • Characterization of NEDD8, a developmentally down-regulated ubiquitin-like protein
    • Kamitani T, Kito K, Nguyen HP, Yeh ET, (1997) Characterization of NEDD8, a developmentally down-regulated ubiquitin-like protein. J Biol Chem 272: 28557-28562
    • (1997) J Biol Chem , vol.272 , pp. 28557-28562
    • Kamitani, T.1    Kito, K.2    Nguyen, H.P.3    Yeh, E.T.4
  • 34
    • 84861800006 scopus 로고    scopus 로고
    • Optimized fast and sensitive acquisition methods for shotgun proteomics on a quadrupole orbitrap mass spectrometer
    • Kelstrup CD, Young C, Lavallee R, Nielsen ML, Olsen JV, (2012) Optimized fast and sensitive acquisition methods for shotgun proteomics on a quadrupole orbitrap mass spectrometer. J Proteome Res 11: 3487-3497
    • (2012) J Proteome Res , vol.11 , pp. 3487-3497
    • Kelstrup, C.D.1    Young, C.2    Lavallee, R.3    Nielsen, M.L.4    Olsen, J.V.5
  • 35
    • 84863621364 scopus 로고    scopus 로고
    • Analysis of nuclear factor-kappaB (NF-kappaB) essential modulator (NEMO) binding to linear and lysine-linked ubiquitin chains and its role in the activation of NF-kappaB
    • Kensche T, Tokunaga F, Ikeda F, Goto E, Iwai K, Dikic I, (2012) Analysis of nuclear factor-kappaB (NF-kappaB) essential modulator (NEMO) binding to linear and lysine-linked ubiquitin chains and its role in the activation of NF-kappaB. J Biol Chem 287: 23626-23634
    • (2012) J Biol Chem , vol.287 , pp. 23626-23634
    • Kensche, T.1    Tokunaga, F.2    Ikeda, F.3    Goto, E.4    Iwai, K.5    Dikic, I.6
  • 42
    • 0036171910 scopus 로고    scopus 로고
    • Burst-enhancing role of the IgG membrane tail as a molecular determinant of memory
    • Martin SW, Goodnow CC, (2002) Burst-enhancing role of the IgG membrane tail as a molecular determinant of memory. Nat Immunol 3: 182-188
    • (2002) Nat Immunol , vol.3 , pp. 182-188
    • Martin, S.W.1    Goodnow, C.C.2
  • 43
    • 77950686629 scopus 로고    scopus 로고
    • Disease mutations in Rab7 result in unregulated nucleotide exchange and inappropriate activation
    • McCray BA, Skordalakes E, Taylor JP, (2010) Disease mutations in Rab7 result in unregulated nucleotide exchange and inappropriate activation. Hum Mol Genet 19: 1033-1047
    • (2010) Hum Mol Genet , vol.19 , pp. 1033-1047
    • McCray, B.A.1    Skordalakes, E.2    Taylor, J.P.3
  • 44
    • 0019837928 scopus 로고
    • Major histocompatibility complex-restricted antigen presentation to antigen-reactive T cells by B lymphocyte tumor cells
    • McKean DJ, Infante AJ, Nilson A, Kimoto M, Fathman CG, Walker E, Warner N, (1981) Major histocompatibility complex-restricted antigen presentation to antigen-reactive T cells by B lymphocyte tumor cells. J Exp Med 154: 1419-1431
    • (1981) J Exp Med , vol.154 , pp. 1419-1431
    • McKean, D.J.1    Infante, A.J.2    Nilson, A.3    Kimoto, M.4    Fathman, C.G.5    Walker, E.6    Warner, N.7
  • 49
    • 84901070124 scopus 로고    scopus 로고
    • Unconventional post-translational modifications in immunological signaling
    • Mowen KA, David M, (2014) Unconventional post-translational modifications in immunological signaling. Nat Immunol 15: 512-520
    • (2014) Nat Immunol , vol.15 , pp. 512-520
    • Mowen, K.A.1    David, M.2
  • 51
    • 0029955714 scopus 로고    scopus 로고
    • The pCL vector system: Rapid production of helper-free, high-titer, recombinant retroviruses
    • Naviaux RK, Costanzi E, Haas M, Verma IM, (1996) The pCL vector system: rapid production of helper-free, high-titer, recombinant retroviruses. J Virol 70: 5701-5705
    • (1996) J Virol , vol.70 , pp. 5701-5705
    • Naviaux, R.K.1    Costanzi, E.2    Haas, M.3    Verma, I.M.4
  • 53
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M, (2006) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127: 635-648
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 55
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong SE, Blagoev B, Kratchmarova I, Kristensen DB, Steen H, Pandey A, Mann M, (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol Cell Proteomics 1: 376-386
    • (2002) Mol Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 56
    • 84858129678 scopus 로고    scopus 로고
    • Signaling-mediated control of ubiquitin ligases in endocytosis
    • Polo S, (2012) Signaling-mediated control of ubiquitin ligases in endocytosis. BMC Biol 10: 25
    • (2012) BMC Biol , vol.10 , pp. 25
    • Polo, S.1
  • 60
    • 2942575037 scopus 로고    scopus 로고
    • Structure of the Rab7:REP-1 complex: Insights into the mechanism of Rab prenylation and choroideremia disease
    • Rak A, Pylypenko O, Niculae A, Pyatkov K, Goody RS, Alexandrov K, (2004) Structure of the Rab7:REP-1 complex: insights into the mechanism of Rab prenylation and choroideremia disease. Cell 117: 749-760
    • (2004) Cell , vol.117 , pp. 749-760
    • Rak, A.1    Pylypenko, O.2    Niculae, A.3    Pyatkov, K.4    Goody, R.S.5    Alexandrov, K.6
  • 61
    • 34548183872 scopus 로고    scopus 로고
    • Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips
    • Rappsilber J, Mann M, Ishihama Y, (2007) Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips. Nat Protoc 2: 1896-1906
    • (2007) Nat Protoc , vol.2 , pp. 1896-1906
    • Rappsilber, J.1    Mann, M.2    Ishihama, Y.3
  • 62
    • 84880880724 scopus 로고    scopus 로고
    • New insights into pre-BCR and BCR signalling with relevance to B cell malignancies
    • Rickert RC, (2013) New insights into pre-BCR and BCR signalling with relevance to B cell malignancies. Nat Rev Immunol 13: 578-591
    • (2013) Nat Rev Immunol , vol.13 , pp. 578-591
    • Rickert, R.C.1
  • 63
    • 80051631238 scopus 로고    scopus 로고
    • GProX, a user-friendly platform for bioinformatics analysis and visualization of quantitative proteomics data
    • Rigbolt KTG, Vanselow JT, Blagoev B, (2011) GProX, a user-friendly platform for bioinformatics analysis and visualization of quantitative proteomics data. Mol Cell Proteomics 10: O110.007450
    • (2011) Mol Cell Proteomics , vol.10 , pp. O110007450
    • Rigbolt, K.T.G.1    Vanselow, J.T.2    Blagoev, B.3
  • 67
    • 84922537688 scopus 로고    scopus 로고
    • Ultradeep human phosphoproteome reveals a distinct regulatory nature of Tyr and Ser/Thr-based signaling
    • Sharma K, D'Souza RC, Tyanova S, Schaab C, Wisniewski JR, Cox J, Mann M, (2014) Ultradeep human phosphoproteome reveals a distinct regulatory nature of Tyr and Ser/Thr-based signaling. Cell Rep 8: 1585-1594
    • (2014) Cell Rep , vol.8 , pp. 1585-1594
    • Sharma, K.1    D'Souza, R.C.2    Tyanova, S.3    Schaab, C.4    Wisniewski, J.R.5    Cox, J.6    Mann, M.7
  • 70
    • 2342629277 scopus 로고    scopus 로고
    • The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes
    • Sun L, Deng L, Ea CK, Xia ZP, Chen ZJ, (2004) The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes. Mol Cell 14: 289-301
    • (2004) Mol Cell , vol.14 , pp. 289-301
    • Sun, L.1    Deng, L.2    Ea, C.K.3    Xia, Z.P.4    Chen, Z.J.5
  • 72
    • 84859416334 scopus 로고    scopus 로고
    • The Ankrd 13 family of UIM-bearing proteins regulates EGF receptor endocytosis from the plasma membrane
    • Tanno H, Yamaguchi T, Goto E, Ishido S, Komada M, (2012) The Ankrd 13 family of UIM-bearing proteins regulates EGF receptor endocytosis from the plasma membrane. Mol Biol Cell 23: 1343-1353
    • (2012) Mol Biol Cell , vol.23 , pp. 1343-1353
    • Tanno, H.1    Yamaguchi, T.2    Goto, E.3    Ishido, S.4    Komada, M.5
  • 76
    • 80054033461 scopus 로고    scopus 로고
    • A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles
    • M111 013284
    • Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C, (2011) A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles. Mol Cell Proteomics 10: M111 013284
    • (2011) Mol Cell Proteomics , vol.10
    • Wagner, S.A.1    Beli, P.2    Weinert, B.T.3    Nielsen, M.L.4    Cox, J.5    Mann, M.6    Choudhary, C.7
  • 77
    • 0037147182 scopus 로고    scopus 로고
    • A distinct signaling pathway used by the IgG-containing B cell antigen receptor
    • Wakabayashi C, Adachi T, Wienands J, Tsubata T, (2002) A distinct signaling pathway used by the IgG-containing B cell antigen receptor. Science 298: 2392-2395
    • (2002) Science , vol.298 , pp. 2392-2395
    • Wakabayashi, C.1    Adachi, T.2    Wienands, J.3    Tsubata, T.4
  • 79
    • 34247866419 scopus 로고    scopus 로고
    • Engagement of the B-cell antigen receptor activates STAT through Lyn in a Jak-independent pathway
    • Wang L, Kurosaki T, Corey SJ, (2007) Engagement of the B-cell antigen receptor activates STAT through Lyn in a Jak-independent pathway. Oncogene 26: 2851-2859
    • (2007) Oncogene , vol.26 , pp. 2851-2859
    • Wang, L.1    Kurosaki, T.2    Corey, S.J.3
  • 81
    • 84883307077 scopus 로고    scopus 로고
    • Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation
    • Weinert BT, Scholz C, Wagner SA, Iesmantavicius V, Su D, Daniel JA, Choudhary C, (2013) Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation. Cell Rep 4: 842-851
    • (2013) Cell Rep , vol.4 , pp. 842-851
    • Weinert, B.T.1    Scholz, C.2    Wagner, S.A.3    Iesmantavicius, V.4    Su, D.5    Daniel, J.A.6    Choudhary, C.7
  • 82
  • 83
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • Wisniewski JR, Zougman A, Nagaraj N, Mann M, (2009) Universal sample preparation method for proteome analysis. Nat Methods 6: 359-U360
    • (2009) Nat Methods , vol.6 , pp. 359-U360
    • Wisniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4
  • 84
    • 42949098959 scopus 로고    scopus 로고
    • NEMO recognition of ubiquitinated Bcl10 is required for T cell receptor-mediated NF-kappaB activation
    • Wu CJ, Ashwell JD, (2008) NEMO recognition of ubiquitinated Bcl10 is required for T cell receptor-mediated NF-kappaB activation. Proc Natl Acad Sci USA 105: 3023-3028
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 3023-3028
    • Wu, C.J.1    Ashwell, J.D.2
  • 85
    • 78651225388 scopus 로고    scopus 로고
    • Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling
    • Xu G, Paige JS, Jaffrey SR, (2010) Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling. Nat Biotechnol 28: 868-873
    • (2010) Nat Biotechnol , vol.28 , pp. 868-873
    • Xu, G.1    Paige, J.S.2    Jaffrey, S.R.3
  • 88
    • 84875185728 scopus 로고    scopus 로고
    • Targeting pathological B cell receptor signalling in lymphoid malignancies
    • Young RM, Staudt LM, (2013) Targeting pathological B cell receptor signalling in lymphoid malignancies. Nat Rev Drug Discov 12: 229-243
    • (2013) Nat Rev Drug Discov , vol.12 , pp. 229-243
    • Young, R.M.1    Staudt, L.M.2
  • 89
    • 34447503930 scopus 로고    scopus 로고
    • Phosphorylation of Bcl10 negatively regulates T-cell receptor-mediated NF-kappaB activation
    • Zeng H, Di L, Fu G, Chen Y, Gao X, Xu L, Lin X, Wen R, (2007) Phosphorylation of Bcl10 negatively regulates T-cell receptor-mediated NF-kappaB activation. Mol Cell Biol 27: 5235-5245
    • (2007) Mol Cell Biol , vol.27 , pp. 5235-5245
    • Zeng, H.1    Di, L.2    Fu, G.3    Chen, Y.4    Gao, X.5    Xu, L.6    Lin, X.7    Wen, R.8
  • 90
    • 67249150119 scopus 로고    scopus 로고
    • Rab7: Roles in membrane trafficking and disease
    • Zhang M, Chen L, Wang S, Wang T, (2009) Rab7: roles in membrane trafficking and disease. Biosci Rep 29: 193-209
    • (2009) Biosci Rep , vol.29 , pp. 193-209
    • Zhang, M.1    Chen, L.2    Wang, S.3    Wang, T.4
  • 91
    • 84875208164 scopus 로고    scopus 로고
    • Robust phosphoproteome enrichment using monodisperse microsphere-based immobilized titanium (IV) ion affinity chromatography
    • Zhou H, Ye M, Dong J, Corradini E, Cristobal A, Heck AJ, Zou H, Mohammed S, (2013) Robust phosphoproteome enrichment using monodisperse microsphere-based immobilized titanium (IV) ion affinity chromatography. Nat Protoc 8: 461-480
    • (2013) Nat Protoc , vol.8 , pp. 461-480
    • Zhou, H.1    Ye, M.2    Dong, J.3    Corradini, E.4    Cristobal, A.5    Heck, A.J.6    Zou, H.7    Mohammed, S.8


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