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Volumn 34, Issue 2, 2015, Pages 251-265

Quantitative comparison of a human cancer cell surface proteome between interphase and mitosis

Author keywords

Cell cycle; Cell rounding; Cell surface; PCDH7; SILAC

Indexed keywords

CADHERIN; PROTEOME; BIOLOGICAL MARKER; MEMBRANE PROTEIN; PCDH7 PROTEIN, HUMAN;

EID: 84921263737     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.15252/embj.201385162     Document Type: Article
Times cited : (36)

References (61)
  • 1
    • 0017334127 scopus 로고
    • Role of the coated endocytic vesicle in the uptake of receptor-bound low density lipoprotein in human fibroblasts
    • Anderson RG, Brown MS, Goldstein JL (1977) Role of the coated endocytic vesicle in the uptake of receptor-bound low density lipoprotein in human fibroblasts. Cell 10: 351-364
    • (1977) Cell , vol.10 , pp. 351-364
    • Anderson, R.G.1    Brown, M.S.2    Goldstein, J.L.3
  • 2
    • 41149127192 scopus 로고    scopus 로고
    • A label-free quantification method by MS/MS TIC compared to SILAC and spectral counting in a proteomics screen
    • Asara JM, Christofk HR, Freimark LM, Cantley LC (2008) A label-free quantification method by MS/MS TIC compared to SILAC and spectral counting in a proteomics screen. Proteomics 8: 994-999
    • (2008) Proteomics , vol.8 , pp. 994-999
    • Asara, J.M.1    Christofk, H.R.2    Freimark, L.M.3    Cantley, L.C.4
  • 3
    • 0037263378 scopus 로고    scopus 로고
    • Challenging accepted ion channel biology: P64 and the CLIC family of putative intracellular anion channel proteins
    • Review
    • Ashley RH (2003) Challenging accepted ion channel biology: p64 and the CLIC family of putative intracellular anion channel proteins (Review). Mol Membr Biol 20: 1-11
    • (2003) Mol Membr Biol , vol.20 , pp. 1-11
    • Ashley, R.H.1
  • 4
    • 0037316303 scopus 로고    scopus 로고
    • A comparison of normalization methods for high density oligonucleotide array data based on variance and bias
    • Bolstad BM, Irizarry RA, Astrand M, Speed TP (2003) A comparison of normalization methods for high density oligonucleotide array data based on variance and bias. Bioinformatics 19: 185-193
    • (2003) Bioinformatics , vol.19 , pp. 185-193
    • Bolstad, B.M.1    Irizarry, R.A.2    Astrand, M.3    Speed, T.P.4
  • 5
    • 34249288541 scopus 로고    scopus 로고
    • Endosomal recycling controls plasma membrane area during mitosis
    • Boucrot E, Kirchhausen T (2007) Endosomal recycling controls plasma membrane area during mitosis. Proc Natl Acad Sci USA 104: 7939-7944
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 7939-7944
    • Boucrot, E.1    Kirchhausen, T.2
  • 6
    • 40949104848 scopus 로고    scopus 로고
    • Isolation of endoplasmic reticulum, mitochondria, and mitochondria-associated membrane fractions from transfected cells and from human cytomegalovirus-infected primary fibroblasts
    • Chapter 3: Unit 3.27
    • Bozidis P, Williamson CD, Colberg-Poley AM (2007) Isolation of endoplasmic reticulum, mitochondria, and mitochondria-associated membrane fractions from transfected cells and from human cytomegalovirus-infected primary fibroblasts. Curr Protoc Cell Biol Chapter 3: Unit 3.27
    • (2007) Curr Protoc Cell Biol
    • Bozidis, P.1    Williamson, C.D.2    Colberg-Poley, A.M.3
  • 7
    • 5444274954 scopus 로고    scopus 로고
    • Identification of the protein binding region of S-trityl-L-cysteine, a new potent inhibitor of the mitotic kinesin Eg5
    • Brier S, Lemaire D, Debonis S, Forest E, Kozielski F (2004) Identification of the protein binding region of S-trityl-L-cysteine, a new potent inhibitor of the mitotic kinesin Eg5. Biochemistry 43: 13072-13082
    • (2004) Biochemistry , vol.43 , pp. 13072-13082
    • Brier, S.1    Lemaire, D.2    Debonis, S.3    Forest, E.4    Kozielski, F.5
  • 8
    • 0033860695 scopus 로고    scopus 로고
    • The EGF receptor: A nexus for trafficking and signaling
    • Carpenter G (2000) The EGF receptor: a nexus for trafficking and signaling. BioEssays 22: 697-707
    • (2000) BioEssays , vol.22 , pp. 697-707
    • Carpenter, G.1
  • 9
    • 33748305676 scopus 로고    scopus 로고
    • Crosstalk between different adhesion molecules
    • Chen X, Gumbiner BM (2006a) Crosstalk between different adhesion molecules. Curr Opin Cell Biol 18: 572-578
    • (2006) Curr Opin Cell Biol , vol.18 , pp. 572-578
    • Chen, X.1    Gumbiner, B.M.2
  • 10
    • 33746056119 scopus 로고    scopus 로고
    • Paraxial protocadherin mediates cell sorting and tissue morphogenesis by regulating C-cadherin adhesion activity
    • Chen X, Gumbiner BM (2006b) Paraxial protocadherin mediates cell sorting and tissue morphogenesis by regulating C-cadherin adhesion activity. J Cell Biol 174: 301-313
    • (2006) J Cell Biol , vol.174 , pp. 301-313
    • Chen, X.1    Gumbiner, B.M.2
  • 11
    • 77954048885 scopus 로고    scopus 로고
    • A protocadherin-cadherin-FLRT3 complex controls cell adhesion and morphogenesis
    • Chen X, Koh E, Yoder M, Gumbiner BM (2009) A protocadherin-cadherin-FLRT3 complex controls cell adhesion and morphogenesis. PLoS One 4: e8411
    • (2009) PLoS One , vol.4 , pp. e8411
    • Chen, X.1    Koh, E.2    Yoder, M.3    Gumbiner, B.M.4
  • 12
    • 8844261143 scopus 로고    scopus 로고
    • Cell surface biology mediated by low affinity multivalent protein-glycan interactions
    • Collins BE, Paulson JC (2004) Cell surface biology mediated by low affinity multivalent protein-glycan interactions. Curr Opin Chem Biol 8: 617-625
    • (2004) Curr Opin Chem Biol , vol.8 , pp. 617-625
    • Collins, B.E.1    Paulson, J.C.2
  • 13
    • 67649400942 scopus 로고    scopus 로고
    • A practical guide to the MaxQuant computational platform for SILAC-based quantitative proteomics
    • Cox J, Matic I, Hilger M, Nagaraj N, Selbach M, Olsen JV, Mann M (2009) A practical guide to the MaxQuant computational platform for SILAC-based quantitative proteomics. Nat Protoc 4: 698-705
    • (2009) Nat Protoc , vol.4 , pp. 698-705
    • Cox, J.1    Matic, I.2    Hilger, M.3    Nagaraj, N.4    Selbach, M.5    Olsen, J.V.6    Mann, M.7
  • 15
    • 70350018450 scopus 로고    scopus 로고
    • Dynamic changes in Rap1 activity are required for cell retraction and spreading during mitosis
    • Dao VT, Dupuy AG, Gavet O, Caron E, de Gunzburg J (2009) Dynamic changes in Rap1 activity are required for cell retraction and spreading during mitosis. J Cell Sci 122: 2996-3004
    • (2009) J Cell Sci , vol.122 , pp. 2996-3004
    • Dao, V.T.1    Dupuy, A.G.2    Gavet, O.3    Caron, E.4    De Gunzburg, J.5
  • 16
    • 84891773596 scopus 로고    scopus 로고
    • N-linked glycosylation enrichment for in-depth cell surface proteomics of diffuse large B-cell lymphoma subtypes
    • Deeb SJ, Cox J, Schmidt-Supprian M, Mann M (2014) N-linked glycosylation enrichment for in-depth cell surface proteomics of diffuse large B-cell lymphoma subtypes. Mol Cell Proteomics 13: 240-251
    • (2014) Mol Cell Proteomics , vol.13 , pp. 240-251
    • Deeb, S.J.1    Cox, J.2    Schmidt-Supprian, M.3    Mann, M.4
  • 19
    • 55749099458 scopus 로고    scopus 로고
    • Biotinylation reagents for the study of cell surface proteins
    • Elia G (2008) Biotinylation reagents for the study of cell surface proteins. Proteomics 8: 4012-4024
    • (2008) Proteomics , vol.8 , pp. 4012-4024
    • Elia, G.1
  • 20
    • 69249106881 scopus 로고    scopus 로고
    • Pathways and mechanisms of endocytic recycling
    • Grant BD, Donaldson JG (2009) Pathways and mechanisms of endocytic recycling. Nat Rev Mol Cell Biol 10: 597-608
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 597-608
    • Grant, B.D.1    Donaldson, J.G.2
  • 22
    • 0026561134 scopus 로고
    • Electron microscopic observations on the maintenance of the tight junction during cell division in the epithelium of the mouse small intestine
    • Jinguji Y, Ishikawa H (1992) Electron microscopic observations on the maintenance of the tight junction during cell division in the epithelium of the mouse small intestine. Cell Struct Funct 17: 27-37
    • (1992) Cell Struct Funct , vol.17 , pp. 27-37
    • Jinguji, Y.1    Ishikawa, H.2
  • 23
    • 0016785953 scopus 로고
    • HeLa cell plasma membranes. Changes in membrane protein composition during the cell cycle
    • Johnsen S, Stokke T, Prydz H (1975) HeLa cell plasma membranes. Changes in membrane protein composition during the cell cycle. Exp Cell Res 93: 245-251
    • (1975) Exp Cell Res , vol.93 , pp. 245-251
    • Johnsen, S.1    Stokke, T.2    Prydz, H.3
  • 25
    • 79959735228 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics identifies substrates and functional modules of Aurora and Polo-like kinase activities in mitotic cells
    • Kettenbach AN, Schweppe DK, Faherty BK, Pechenick D, Pletnev AA, Gerber SA (2011) Quantitative phosphoproteomics identifies substrates and functional modules of Aurora and Polo-like kinase activities in mitotic cells. Sci Signal 4: rs5
    • (2011) Sci Signal , vol.4 , pp. rs5
    • Kettenbach, A.N.1    Schweppe, D.K.2    Faherty, B.K.3    Pechenick, D.4    Pletnev, A.A.5    Gerber, S.A.6
  • 27
    • 0742286873 scopus 로고    scopus 로고
    • Studies on endocytic mechanisms of the Menkes copper-translocating P-type ATPase (ATP7A; MNK). Endocytosis of the Menkes protein
    • Lane C, Petris MJ, Benmerah A, Greenough M, Camakaris J (2004) Studies on endocytic mechanisms of the Menkes copper-translocating P-type ATPase (ATP7A; MNK). Endocytosis of the Menkes protein. Biometals 17: 87-98
    • (2004) Biometals , vol.17 , pp. 87-98
    • Lane, C.1    Petris, M.J.2    Benmerah, A.3    Greenough, M.4    Camakaris, J.5
  • 28
    • 84865273423 scopus 로고    scopus 로고
    • Protocadherins mediate dendritic self-avoidance in the mammalian nervous system
    • Lefebvre JL, Kostadinov D, Chen WV, Maniatis T, Sanes JR (2012) Protocadherins mediate dendritic self-avoidance in the mammalian nervous system. Nature 488: 517-521
    • (2012) Nature , vol.488 , pp. 517-521
    • Lefebvre, J.L.1    Kostadinov, D.2    Chen, W.V.3    Maniatis, T.4    Sanes, J.R.5
  • 29
    • 0037455574 scopus 로고    scopus 로고
    • RhoA is required for cortical retraction and rigidity during mitotic cell rounding
    • Maddox AS, Burridge K (2003) RhoA is required for cortical retraction and rigidity during mitotic cell rounding. J Cell Biol 160: 255-265
    • (2003) J Cell Biol , vol.160 , pp. 255-265
    • Maddox, A.S.1    Burridge, K.2
  • 30
    • 15744362477 scopus 로고    scopus 로고
    • Junctional adhesion molecule 1 regulates epithelial cell morphology through effects on beta1 integrins and Rap1 activity
    • Mandell KJ, Babbin BA, Nusrat A, Parkos CA (2005) Junctional adhesion molecule 1 regulates epithelial cell morphology through effects on beta1 integrins and Rap1 activity. J Biol Chem 280: 11665-11674
    • (2005) J Biol Chem , vol.280 , pp. 11665-11674
    • Mandell, K.J.1    Babbin, B.A.2    Nusrat, A.3    Parkos, C.A.4
  • 32
    • 84865102938 scopus 로고    scopus 로고
    • Changes in Ect 2 localization couple actomyosin-dependent cell shape changes to mitotic progression
    • Matthews HK, Delabre U, Rohn JL, Guck J, Kunda P, Baum B (2012) Changes in Ect 2 localization couple actomyosin-dependent cell shape changes to mitotic progression. Dev Cell 23: 371-383
    • (2012) Dev Cell , vol.23 , pp. 371-383
    • Matthews, H.K.1    Delabre, U.2    Rohn, J.L.3    Guck, J.4    Kunda, P.5    Baum, B.6
  • 33
    • 60749121708 scopus 로고    scopus 로고
    • Cdk1 and cell morphology: Connections and directions
    • Moseley JB, Nurse P (2009) Cdk1 and cell morphology: connections and directions. Curr Opin Cell Biol 21: 82-88
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 82-88
    • Moseley, J.B.1    Nurse, P.2
  • 34
    • 84859416790 scopus 로고    scopus 로고
    • FCH domain only-2 organizes clathrin-coated structures and interacts with Disabled-2 for low-density lipoprotein receptor endocytosis
    • Mulkearns EE, Cooper JA (2012) FCH domain only-2 organizes clathrin-coated structures and interacts with Disabled-2 for low-density lipoprotein receptor endocytosis. Mol Biol Cell 23: 1330-1342
    • (2012) Mol Biol Cell , vol.23 , pp. 1330-1342
    • Mulkearns, E.E.1    Cooper, J.A.2
  • 35
    • 0043092241 scopus 로고    scopus 로고
    • Characterization of the endosomal sorting signal of the cation-dependent mannose 6-phosphate receptor
    • Nair P, Schaub BE, Rohrer J (2003) Characterization of the endosomal sorting signal of the cation-dependent mannose 6-phosphate receptor. J Biol Chem 278: 24753-24758
    • (2003) J Biol Chem , vol.278 , pp. 24753-24758
    • Nair, P.1    Schaub, B.E.2    Rohrer, J.3
  • 36
    • 84881663995 scopus 로고    scopus 로고
    • Epithelial junctions maintain tissue architecture by directing planar spindle orientation
    • Nakajima Y, Meyer EJ, Kroesen A, McKinney SA, Gibson MC (2013) Epithelial junctions maintain tissue architecture by directing planar spindle orientation. Nature 500: 359-362
    • (2013) Nature , vol.500 , pp. 359-362
    • Nakajima, Y.1    Meyer, E.J.2    Kroesen, A.3    McKinney, S.A.4    Gibson, M.C.5
  • 37
    • 0035235736 scopus 로고    scopus 로고
    • Mitotic kinases as regulators of cell division and its checkpoints
    • Nigg EA (2001) Mitotic kinases as regulators of cell division and its checkpoints. Nat Rev Mol Cell Biol 2: 21-32
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 21-32
    • Nigg, E.A.1
  • 38
    • 0025246110 scopus 로고
    • Universal control mechanism regulating onset of M-phase
    • Nurse P (1990) Universal control mechanism regulating onset of M-phase. Nature 344: 503-508
    • (1990) Nature , vol.344 , pp. 503-508
    • Nurse, P.1
  • 40
    • 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
  • 42
    • 36849078884 scopus 로고    scopus 로고
    • Endothelin-converting enzyme-1 regulates endosomal sorting of calcitonin receptor-like receptor and beta-arrestins
    • Padilla BE, Cottrell GS, Roosterman D, Pikios S, Muller L, Steinhoff M, Bunnett NW (2007) Endothelin-converting enzyme-1 regulates endosomal sorting of calcitonin receptor-like receptor and beta-arrestins. J Cell Biol 179: 981-997
    • (2007) J Cell Biol , vol.179 , pp. 981-997
    • Padilla, B.E.1    Cottrell, G.S.2    Roosterman, D.3    Pikios, S.4    Muller, L.5    Steinhoff, M.6    Bunnett, N.W.7
  • 43
    • 0027090017 scopus 로고
    • Fibronectin receptors are functional on mitotic Chinese hamster ovary cells
    • Pomies P, Block MR (1992) Fibronectin receptors are functional on mitotic Chinese hamster ovary cells. Biochem Biophys Res Commun 189: 1429-1436
    • (1992) Biochem Biophys Res Commun , vol.189 , pp. 1429-1436
    • Pomies, P.1    Block, M.R.2
  • 46
    • 84871954135 scopus 로고    scopus 로고
    • Glycoproteomics enabled by tagging sialic acid- or galactose-terminated glycans
    • Ramya TN, Weerapana E, Cravatt BF, Paulson JC (2013) Glycoproteomics enabled by tagging sialic acid- or galactose-terminated glycans. Glycobiology 23: 211-221
    • (2013) Glycobiology , vol.23 , pp. 211-221
    • Ramya, T.N.1    Weerapana, E.2    Cravatt, B.F.3    Paulson, J.C.4
  • 47
    • 0035960736 scopus 로고    scopus 로고
    • An epithelial cell destined for apoptosis signals its neighbors to extrude it by an actin- and myosin-dependent mechanism
    • Rosenblatt J, Raff MC, Cramer LP (2001) An epithelial cell destined for apoptosis signals its neighbors to extrude it by an actin- and myosin-dependent mechanism. Curr Biol 11: 1847-1857
    • (2001) Curr Biol , vol.11 , pp. 1847-1857
    • Rosenblatt, J.1    Raff, M.C.2    Cramer, L.P.3
  • 48
    • 41449088027 scopus 로고    scopus 로고
    • Mitosis: Moesin and the importance of being round
    • Rosenblatt J (2008) Mitosis: moesin and the importance of being round. Curr Biol 18: R292-R293
    • (2008) Curr Biol , vol.18 , pp. R292-R293
    • Rosenblatt, J.1
  • 50
    • 77957039206 scopus 로고    scopus 로고
    • Combinatorial homophilic interaction between gamma-protocadherin multimers greatly expands the molecular diversity of cell adhesion
    • Schreiner D, Weiner JA (2010) Combinatorial homophilic interaction between gamma-protocadherin multimers greatly expands the molecular diversity of cell adhesion. Proc Natl Acad Sci USA 107: 14893-14898
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 14893-14898
    • Schreiner, D.1    Weiner, J.A.2
  • 52
    • 33745867225 scopus 로고    scopus 로고
    • S-trityl-L-cysteine is a reversible, tight binding inhibitor of the human kinesin Eg5 that specifically blocks mitotic progression
    • Skoufias DA, DeBonis S, Saoudi Y, Lebeau L, Crevel I, Cross R, Wade RH, Hackney D, Kozielski F (2006) S-trityl-L-cysteine is a reversible, tight binding inhibitor of the human kinesin Eg5 that specifically blocks mitotic progression. J Biol Chem 281: 17559-17569
    • (2006) J Biol Chem , vol.281 , pp. 17559-17569
    • Skoufias, D.A.1    DeBonis, S.2    Saoudi, Y.3    Lebeau, L.4    Crevel, I.5    Cross, R.6    Wade, R.H.7    Hackney, D.8    Kozielski, F.9
  • 53
    • 0016266233 scopus 로고
    • Inhibition of growth by masking of arginine moieties in protein at the cell surface
    • Stein SM, Berestecky JM (1974) Inhibition of growth by masking of arginine moieties in protein at the cell surface. Cancer Res 34: 3112-3116
    • (1974) Cancer Res , vol.34 , pp. 3112-3116
    • Stein, S.M.1    Berestecky, J.M.2
  • 56
    • 84861148456 scopus 로고    scopus 로고
    • Tracking mechanics and volume of globular cells with atomic force microscopy using a constant-height clamp
    • Stewart MP, Toyoda Y, Hyman AA, Muller DJ (2012) Tracking mechanics and volume of globular cells with atomic force microscopy using a constant-height clamp. Nat Protoc 7: 143-154
    • (2012) Nat Protoc , vol.7 , pp. 143-154
    • Stewart, M.P.1    Toyoda, Y.2    Hyman, A.A.3    Muller, D.J.4
  • 57
    • 80051976269 scopus 로고    scopus 로고
    • Atomic force microscopy to study mechanics of living mitotic mammalian cells
    • Toyoda Y, Stewart MP, Hyman AA, Muller DJ (2011) Atomic force microscopy to study mechanics of living mitotic mammalian cells. Jpn J Appl Phys 50: 08LA01-1-08LA01-6
    • (2011) Jpn J Appl Phys , vol.50 , pp. 08LA011-08LA016
    • Toyoda, Y.1    Stewart, M.P.2    Hyman, A.A.3    Muller, D.J.4
  • 58
    • 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: 359-362
    • (2009) Nat Methods , vol.6 , pp. 359-362
    • Wisniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4
  • 60
    • 61449097424 scopus 로고    scopus 로고
    • High-efficiency labeling of sialylated glycoproteins on living cells
    • Zeng Y, Ramya TN, Dirksen A, Dawson PE, Paulson JC (2009) High-efficiency labeling of sialylated glycoproteins on living cells. Nat Methods 6: 207-209
    • (2009) Nat Methods , vol.6 , pp. 207-209
    • Zeng, Y.1    Ramya, T.N.2    Dirksen, A.3    Dawson, P.E.4    Paulson, J.C.5
  • 61
    • 77958450147 scopus 로고    scopus 로고
    • Chemoaffinity revisited: Dscams, protocadherins, and neural circuit assembly
    • Zipursky SL, Sanes JR (2010) Chemoaffinity revisited: dscams, protocadherins, and neural circuit assembly. Cell 143: 343-353
    • (2010) Cell , vol.143 , pp. 343-353
    • Zipursky, S.L.1    Sanes, J.R.2


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