메뉴 건너뛰기




Volumn 21, Issue 8, 2014, Pages 1013-1022

LDAI-based chemical labeling of intact membrane proteins and its pulse-chase analysis under live cell conditions

Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN COUPLED RECEPTOR; GLYCOSYLPHOSPHATIDYLINOSITOL; IMIDAZOLE; MEMBRANE PROTEIN; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; RECEPTOR PROTEIN; IMIDAZOLE DERIVATIVE; LIGAND;

EID: 84919664417     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2014.07.013     Document Type: Article
Times cited : (67)

References (49)
  • 3
    • 10544221237 scopus 로고    scopus 로고
    • Ligand-induced phosphorylation/dephosphorylation of the endogenous bradykinin B2 receptor from human fibroblasts
    • A. Blaukat, S.A. Alla, M.J. Lohse, and W. Müller-Esterl Ligand-induced phosphorylation/dephosphorylation of the endogenous bradykinin B2 receptor from human fibroblasts J. Biol. Chem. 271 1996 32366 32374
    • (1996) J. Biol. Chem. , vol.271 , pp. 32366-32374
    • Blaukat, A.1    Alla, S.A.2    Lohse, M.J.3    Müller-Esterl, W.4
  • 5
    • 84856004739 scopus 로고    scopus 로고
    • An activity-based imaging probe for the integral membrane hydrolase KIAA1363
    • J.W. Chang, R.E. Moellering, and B.F. Cravatt An activity-based imaging probe for the integral membrane hydrolase KIAA1363 Angew. Chem. Int. Ed. Engl. 51 2012 966 970
    • (2012) Angew. Chem. Int. Ed. Engl. , vol.51 , pp. 966-970
    • Chang, J.W.1    Moellering, R.E.2    Cravatt, B.F.3
  • 6
    • 18744401100 scopus 로고    scopus 로고
    • Site-specific labeling of cell surface proteins with biophysical probes using biotin ligase
    • I. Chen, M. Howarth, W. Lin, and A.Y. Ting Site-specific labeling of cell surface proteins with biophysical probes using biotin ligase Nat. Methods 2 2005 99 104
    • (2005) Nat. Methods , vol.2 , pp. 99-104
    • Chen, I.1    Howarth, M.2    Lin, W.3    Ting, A.Y.4
  • 7
    • 58249094845 scopus 로고    scopus 로고
    • Hypoxia-inducible carbonic anhydrase IX and XII promote tumor cell growth by counteracting acidosis through the regulation of the intracellular pH
    • J. Chiche, K. Ilc, J. Laferrière, E. Trottier, F. Dayan, N.M. Mazure, M.C. Brahimi-Horn, and J. Pouysségur Hypoxia-inducible carbonic anhydrase IX and XII promote tumor cell growth by counteracting acidosis through the regulation of the intracellular pH Cancer Res. 69 2009 358 368
    • (2009) Cancer Res. , vol.69 , pp. 358-368
    • Chiche, J.1    Ilc, K.2    Laferrière, J.3    Trottier, E.4    Dayan, F.5    Mazure, N.M.6    Brahimi-Horn, M.C.7    Pouysségur, J.8
  • 8
    • 11244309014 scopus 로고    scopus 로고
    • Proteolysis: From the lysosome to ubiquitin and the proteasome
    • A. Ciechanover Proteolysis: from the lysosome to ubiquitin and the proteasome Nat. Rev. Mol. Cell Biol. 6 2005 79 87
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 79-87
    • Ciechanover, A.1
  • 10
    • 0025740371 scopus 로고
    • The conversion of the human membrane-associated folate binding protein (folate receptor) to the soluble folate binding protein by a membrane-associated metalloprotease
    • P.C. Elwood, J.C. Deutsch, and J.F. Kolhouse The conversion of the human membrane-associated folate binding protein (folate receptor) to the soluble folate binding protein by a membrane-associated metalloprotease J. Biol. Chem. 266 1991 2346 2353
    • (1991) J. Biol. Chem. , vol.266 , pp. 2346-2353
    • Elwood, P.C.1    Deutsch, J.C.2    Kolhouse, J.F.3
  • 11
    • 84857850984 scopus 로고    scopus 로고
    • Ligand-directed acyl imidazole chemistry for labeling of membrane-bound proteins on live cells
    • S.H. Fujishima, R. Yasui, T. Miki, A. Ojida, and I. Hamachi Ligand-directed acyl imidazole chemistry for labeling of membrane-bound proteins on live cells J. Am. Chem. Soc. 134 2012 3961 3964
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 3961-3964
    • Fujishima, S.H.1    Yasui, R.2    Miki, T.3    Ojida, A.4    Hamachi, I.5
  • 13
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • B.A. Griffin, S.R. Adams, and R.Y. Tsien Specific covalent labeling of recombinant protein molecules inside live cells Science 281 1998 269 272
    • (1998) Science , vol.281 , pp. 269-272
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 14
    • 0028795941 scopus 로고
    • Recombinant human NMDA homomeric NR1 receptors expressed in mammalian cells form a high-affinity glycine antagonist binding site
    • S. Grimwood, B. Le Bourdellès, and P.J. Whiting Recombinant human NMDA homomeric NR1 receptors expressed in mammalian cells form a high-affinity glycine antagonist binding site J. Neurochem. 64 1995 525 530
    • (1995) J. Neurochem. , vol.64 , pp. 525-530
    • Grimwood, S.1    Le Bourdellès, B.2    Whiting, P.J.3
  • 15
    • 0025949276 scopus 로고
    • Mechanisms of plasma membrane protein degradation: Recycling proteins are degraded more rapidly than those confined to the cell surface
    • J.F. Hare, and K. Taylor Mechanisms of plasma membrane protein degradation: recycling proteins are degraded more rapidly than those confined to the cell surface Proc. Natl. Acad. Sci. USA 88 1991 5902 5906
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5902-5906
    • Hare, J.F.1    Taylor, K.2
  • 16
    • 84866384527 scopus 로고    scopus 로고
    • Traceless affinity labeling of endogenous proteins for functional analysis in living cells
    • T. Hayashi, and I. Hamachi Traceless affinity labeling of endogenous proteins for functional analysis in living cells Acc. Chem. Res. 45 2012 1460 1469
    • (2012) Acc. Chem. Res. , vol.45 , pp. 1460-1469
    • Hayashi, T.1    Hamachi, I.2
  • 17
    • 0032886585 scopus 로고    scopus 로고
    • Fluorescent and biotinylated probes for B2 bradykinin receptors: Agonists and antagonists
    • J. Howl Fluorescent and biotinylated probes for B2 bradykinin receptors: agonists and antagonists Peptides 20 1999 515 518
    • (1999) Peptides , vol.20 , pp. 515-518
    • Howl, J.1
  • 18
    • 0032514685 scopus 로고    scopus 로고
    • Down-regulation of transmembrane carbonic anhydrases in renal cell carcinoma cell lines by wild-type von Hippel-Lindau transgenes
    • S.V. Ivanov, I. Kuzmin, M.H. Wei, S. Pack, L. Geil, B.E. Johnson, E.J. Stanbridge, and M.I. Lerman Down-regulation of transmembrane carbonic anhydrases in renal cell carcinoma cell lines by wild-type von Hippel-Lindau transgenes Proc. Natl. Acad. Sci. USA 95 1998 12596 12601
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12596-12601
    • Ivanov, S.V.1    Kuzmin, I.2    Wei, M.H.3    Pack, S.4    Geil, L.5    Johnson, B.E.6    Stanbridge, E.J.7    Lerman, M.I.8
  • 19
    • 1542395808 scopus 로고    scopus 로고
    • Pulse-chase labeling techniques for the analysis of protein maturation and degradation
    • P. Bross, N. Gregersen, Humana Press Totowa, NJ
    • A. Jansens, and I. Braakman Pulse-chase labeling techniques for the analysis of protein maturation and degradation P. Bross, N. Gregersen, Protein Misfolding and Diease 2003 Humana Press Totowa, NJ 133 145
    • (2003) Protein Misfolding and Diease , pp. 133-145
    • Jansens, A.1    Braakman, I.2
  • 20
    • 0344401038 scopus 로고
    • Receptor-mediated folate accumulation is regulated by the cellular folate content
    • B.A. Kamen, and A. Capdevila Receptor-mediated folate accumulation is regulated by the cellular folate content Proc. Natl. Acad. Sci. USA 83 1986 5983 5987
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 5983-5987
    • Kamen, B.A.1    Capdevila, A.2
  • 21
    • 0023009070 scopus 로고
    • The interrelationship of the soluble and membrane-associated folate-binding proteins in human KB cells
    • M.A. Kane, P.C. Elwood, R.M. Portillo, A.C. Antony, and J.F. Kolhouse The interrelationship of the soluble and membrane-associated folate-binding proteins in human KB cells J. Biol. Chem. 261 1986 15625 15631
    • (1986) J. Biol. Chem. , vol.261 , pp. 15625-15631
    • Kane, M.A.1    Elwood, P.C.2    Portillo, R.M.3    Antony, A.C.4    Kolhouse, J.F.5
  • 22
  • 23
    • 0000096835 scopus 로고    scopus 로고
    • Click Chemistry: Diverse Chemical Function from a Few Good Reactions
    • H.C. Kolb, M.G. Finn, and K.B. Sharpless Click Chemistry: Diverse Chemical Function from a Few Good Reactions Angew. Chem. Int. Ed. Engl. 40 2001 2004 2021
    • (2001) Angew. Chem. Int. Ed. Engl. , vol.40 , pp. 2004-2021
    • Kolb, H.C.1    Finn, M.G.2    Sharpless, K.B.3
  • 24
    • 80053319803 scopus 로고    scopus 로고
    • Copper-free Sonogashira cross-coupling for functionalization of alkyne-encoded proteins in aqueous medium and in bacterial cells
    • N. Li, R.K.V. Lim, S. Edwardraja, and Q. Lin Copper-free Sonogashira cross-coupling for functionalization of alkyne-encoded proteins in aqueous medium and in bacterial cells J. Am. Chem. Soc. 133 2011 15316 15319
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 15316-15319
    • Li, N.1    Lim, R.K.V.2    Edwardraja, S.3    Lin, Q.4
  • 25
    • 0037418882 scopus 로고    scopus 로고
    • Development and use of fluorescent protein markers in living cells
    • J. Lippincott-Schwartz, and G.H. Patterson Development and use of fluorescent protein markers in living cells Science 300 2003 87 91
    • (2003) Science , vol.300 , pp. 87-91
    • Lippincott-Schwartz, J.1    Patterson, G.H.2
  • 27
    • 6444236841 scopus 로고    scopus 로고
    • Bradykinin receptor ligands: Therapeutic perspectives
    • F. Marceau, and D. Regoli Bradykinin receptor ligands: therapeutic perspectives Nat. Rev. Drug Discov. 3 2004 845 852
    • (2004) Nat. Rev. Drug Discov. , vol.3 , pp. 845-852
    • Marceau, F.1    Regoli, D.2
  • 28
    • 84877767312 scopus 로고    scopus 로고
    • One-step construction of caged carbonic anhydrase i using a ligand-directed acyl imidazole-based protein labeling method
    • K. Matsuo, Y. Kioi, R. Yasui, Y. Takaoka, T. Miki, S. Fujishima, and I. Hamachi One-step construction of caged carbonic anhydrase I using a ligand-directed acyl imidazole-based protein labeling method Chem. Sci. 4 2013 2573 2580
    • (2013) Chem. Sci. , vol.4 , pp. 2573-2580
    • Matsuo, K.1    Kioi, Y.2    Yasui, R.3    Takaoka, Y.4    Miki, T.5    Fujishima, S.6    Hamachi, I.7
  • 29
    • 33644522718 scopus 로고    scopus 로고
    • Human bradykinin B2 receptor sialylation and N-glycosylation participate with disulfide bonding in surface receptor dimerization
    • S. Michineau, F. Alhenc-Gelas, and R.M. Rajerison Human bradykinin B2 receptor sialylation and N-glycosylation participate with disulfide bonding in surface receptor dimerization Biochemistry 45 2006 2699 2707
    • (2006) Biochemistry , vol.45 , pp. 2699-2707
    • Michineau, S.1    Alhenc-Gelas, F.2    Rajerison, R.M.3
  • 30
    • 84856252572 scopus 로고    scopus 로고
    • No-wash protein labeling with designed fluorogenic probes and application to real-time pulse-chase analysis
    • S. Mizukami, S. Watanabe, Y. Akimoto, and K. Kikuchi No-wash protein labeling with designed fluorogenic probes and application to real-time pulse-chase analysis J. Am. Chem. Soc. 134 2012 1623 1629
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 1623-1629
    • Mizukami, S.1    Watanabe, S.2    Akimoto, Y.3    Kikuchi, K.4
  • 32
    • 77955840000 scopus 로고    scopus 로고
    • Selective covalent labeling of tag-fused GPCR proteins on live cell surface with a synthetic probe for their functional analysis
    • H. Nonaka, S.H. Fujishima, S.H. Uchinomiya, A. Ojida, and I. Hamachi Selective covalent labeling of tag-fused GPCR proteins on live cell surface with a synthetic probe for their functional analysis J. Am. Chem. Soc. 132 2010 9301 9309
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 9301-9309
    • Nonaka, H.1    Fujishima, S.H.2    Uchinomiya, S.H.3    Ojida, A.4    Hamachi, I.5
  • 34
    • 84878254691 scopus 로고    scopus 로고
    • NMDA receptor subunit diversity: Impact on receptor properties, synaptic plasticity and disease
    • P. Paoletti, C. Bellone, and Q. Zhou NMDA receptor subunit diversity: impact on receptor properties, synaptic plasticity and disease Nat. Rev. Neurosci. 14 2013 383 400
    • (2013) Nat. Rev. Neurosci. , vol.14 , pp. 383-400
    • Paoletti, P.1    Bellone, C.2    Zhou, Q.3
  • 35
    • 0033617468 scopus 로고    scopus 로고
    • Bradykinin-induced internalization of the human B2 receptor requires phosphorylation of three serine and two threonine residues at its carboxyl tail
    • A. Pizard, A. Blaukat, W. Müller-Esterl, F. Alhenc-Gelas, and R.M. Rajerison Bradykinin-induced internalization of the human B2 receptor requires phosphorylation of three serine and two threonine residues at its carboxyl tail J. Biol. Chem. 274 1999 12738 12747
    • (1999) J. Biol. Chem. , vol.274 , pp. 12738-12747
    • Pizard, A.1    Blaukat, A.2    Müller-Esterl, W.3    Alhenc-Gelas, F.4    Rajerison, R.M.5
  • 37
    • 48249141055 scopus 로고    scopus 로고
    • Selective functionalization of a genetically encoded alkene-containing protein via "photoclick chemistry" in bacterial cells
    • W. Song, Y. Wang, J. Qu, and Q. Lin Selective functionalization of a genetically encoded alkene-containing protein via "photoclick chemistry" in bacterial cells J. Am. Chem. Soc. 130 2008 9654 9655
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 9654-9655
    • Song, W.1    Wang, Y.2    Qu, J.3    Lin, Q.4
  • 39
    • 38849143765 scopus 로고    scopus 로고
    • Carbonic anhydrases: Novel therapeutic applications for inhibitors and activators
    • C.T. Supuran Carbonic anhydrases: novel therapeutic applications for inhibitors and activators Nat. Rev. Drug Discov. 7 2008 168 181
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 168-181
    • Supuran, C.T.1
  • 40
    • 84875850730 scopus 로고    scopus 로고
    • Protein organic chemistry and applications for labeling and engineering in live-cell systems
    • Y. Takaoka, A. Ojida, and I. Hamachi Protein organic chemistry and applications for labeling and engineering in live-cell systems Angew. Chem. Int. Ed. Engl. 52 2013 4088 4106
    • (2013) Angew. Chem. Int. Ed. Engl. , vol.52 , pp. 4088-4106
    • Takaoka, Y.1    Ojida, A.2    Hamachi, I.3
  • 41
    • 84856433232 scopus 로고    scopus 로고
    • Native FKBP12 engineering by ligand-directed tosyl chemistry: Labeling properties and application to photo-cross-linking of protein complexes in vitro and in living cells
    • T. Tamura, S. Tsukiji, and I. Hamachi Native FKBP12 engineering by ligand-directed tosyl chemistry: labeling properties and application to photo-cross-linking of protein complexes in vitro and in living cells J. Am. Chem. Soc. 134 2012 2216 2226
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 2216-2226
    • Tamura, T.1    Tsukiji, S.2    Hamachi, I.3
  • 42
    • 84877248493 scopus 로고    scopus 로고
    • Fluorophore labeling of native FKBP12 by ligand-directed tosyl chemistry allows detection of its molecular interactions in vitro and in living cells
    • T. Tamura, Y. Kioi, T. Miki, S. Tsukiji, and I. Hamachi Fluorophore labeling of native FKBP12 by ligand-directed tosyl chemistry allows detection of its molecular interactions in vitro and in living cells J. Am. Chem. Soc. 135 2013 6782 6785
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 6782-6785
    • Tamura, T.1    Kioi, Y.2    Miki, T.3    Tsukiji, S.4    Hamachi, I.5
  • 45
    • 16244377468 scopus 로고    scopus 로고
    • Carbonic anhydrase inhibitors. Inhibition of the transmembrane isozyme XII with sulfonamides-A new target for the design of antitumor and antiglaucoma drugs?
    • D. Vullo, A. Innocenti, I. Nishimori, J. Pastorek, A. Scozzafava, S. Pastoreková, and C.T. Supuran Carbonic anhydrase inhibitors. Inhibition of the transmembrane isozyme XII with sulfonamides-a new target for the design of antitumor and antiglaucoma drugs? Bioorg. Med. Chem. Lett. 15 2005 963 969
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , pp. 963-969
    • Vullo, D.1    Innocenti, A.2    Nishimori, I.3    Pastorek, J.4    Scozzafava, A.5    Pastoreková, S.6    Supuran, C.T.7
  • 47
    • 0035859892 scopus 로고    scopus 로고
    • Crystal structure of the dimeric extracellular domain of human carbonic anhydrase XII, a bitopic membrane protein overexpressed in certain cancer tumor cells
    • D.A. Whittington, A. Waheed, B. Ulmasov, G.N. Shah, J.H. Grubb, W.S. Sly, and D.W. Christianson Crystal structure of the dimeric extracellular domain of human carbonic anhydrase XII, a bitopic membrane protein overexpressed in certain cancer tumor cells Proc. Natl. Acad. Sci. USA 98 2001 9545 9550
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9545-9550
    • Whittington, D.A.1    Waheed, A.2    Ulmasov, B.3    Shah, G.N.4    Grubb, J.H.5    Sly, W.S.6    Christianson, D.W.7
  • 49
    • 17544376275 scopus 로고    scopus 로고
    • Isolation and characterization of a folate receptor-directed metalloprotease from human placenta
    • X.Y. Yang, J.Y. Mackins, Q.J. Li, and A.C. Antony Isolation and characterization of a folate receptor-directed metalloprotease from human placenta J. Biol. Chem. 271 1996 11493 11499
    • (1996) J. Biol. Chem. , vol.271 , pp. 11493-11499
    • Yang, X.Y.1    Mackins, J.Y.2    Li, Q.J.3    Antony, A.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.