메뉴 건너뛰기




Volumn 5, Issue , 2015, Pages

In vivo linking of membrane lipids and the anion transporter band 3 with thiourea-modified amphiphilic lipid probes

Author keywords

[No Author keywords available]

Indexed keywords

AMINE; ANION TRANSPORT PROTEIN; CHOLESTEROL; LIGAND; MEMBRANE LIPID; MEMBRANE PROTEIN; PHOSPHOLIPID; THIOUREA;

EID: 84948844693     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep17427     Document Type: Article
Times cited : (3)

References (35)
  • 1
    • 66249083118 scopus 로고    scopus 로고
    • Emerging roles for lipids in shaping membrane-protein function
    • Phillips, R., Ursell, T., Wiggins, P. & Sens, P. Emerging roles for lipids in shaping membrane-protein function. Nature 459, 379-385 (2009)
    • (2009) Nature , vol.459 , pp. 379-385
    • Phillips, R.1    Ursell, T.2    Wiggins, P.3    Sens, P.4
  • 2
    • 0038364008 scopus 로고    scopus 로고
    • Lipid-protein interactions in biological membranes: A structural perspective
    • Lee, A. G. Lipid-protein interactions in biological membranes: a structural perspective. Biochim. Biophys. Acta 1612, 1-40 (2003)
    • (2003) Biochim. Biophys. Acta , vol.1612 , pp. 1-40
    • Lee, A.G.1
  • 3
    • 82955248059 scopus 로고    scopus 로고
    • Uncovering the intimate relationship between lipids, cholesterol and GPCR activation
    • Oates, J. & Watts, A. Uncovering the intimate relationship between lipids, cholesterol and GPCR activation. Curr. Opin. Struct. Biol. 21, 802-807 (2011)
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 802-807
    • Oates, J.1    Watts, A.2
  • 4
    • 84899434664 scopus 로고    scopus 로고
    • Non-covalent binding of membrane lipids to membrane proteins
    • Yeagle, P. L. Non-covalent binding of membrane lipids to membrane proteins. Biochim. Biophys. Acta 1838, 1548-1559 (2014)
    • (2014) Biochim. Biophys. Acta , vol.1838 , pp. 1548-1559
    • Yeagle, P.L.1
  • 5
    • 84901936908 scopus 로고    scopus 로고
    • Membrane proteins bind lipids selectively to modulate their structure and function
    • Laganowsky, A. et al. Membrane proteins bind lipids selectively to modulate their structure and function. Nature 510, 172-175 (2014)
    • (2014) Nature , vol.510 , pp. 172-175
    • Laganowsky, A.1
  • 6
    • 84875850730 scopus 로고    scopus 로고
    • Protein organic chemistry and applications for labeling and engineering in live-cell systems
    • Takaoka, Y., Ojida, A. & Hamachi, I. Protein organic chemistry and applications for labeling and engineering in live-cell systems. Angew. Chem. Int. Ed. Engl 52, 4088-4106 (2013)
    • (2013) Angew. Chem. Int. Ed. Engl , vol.52 , pp. 4088-4106
    • Takaoka, Y.1    Ojida, A.2    Hamachi, I.3
  • 7
    • 84861327779 scopus 로고    scopus 로고
    • Electrophilic natural products and their biological targets
    • Gersch, M., Kreuzer, J. & Sieber, S. A. Electrophilic natural products and their biological targets. Nat. Prod. Rep. 29, 659-682 (2012)
    • (2012) Nat. Prod. Rep. , vol.29 , pp. 659-682
    • Gersch, M.1    Kreuzer, J.2    Sieber, S.A.3
  • 8
    • 50649112213 scopus 로고    scopus 로고
    • Activity-based protein profiling: From enzyme chemistry to proteomic chemistry
    • Cravatt, B. F., Wright, A. T. & Kozarich, J. W. Activity-based protein profiling: from enzyme chemistry to proteomic chemistry. Annu. Rev. Biochem. 77, 383-414 (2008)
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 383-414
    • Cravatt, B.F.1    Wright, A.T.2    Kozarich, J.W.3
  • 9
    • 84856402803 scopus 로고    scopus 로고
    • How chemoproteomics can enable drug discovery and development
    • Moellering, R. E. & Cravatt, B. F. How chemoproteomics can enable drug discovery and development. Chem. Biol. 19, 11-22 (2012)
    • (2012) Chem. Biol. , vol.19 , pp. 11-22
    • Moellering, R.E.1    Cravatt, B.F.2
  • 10
    • 84874654262 scopus 로고    scopus 로고
    • Chemical tagging of a drug target using 5-sulfonyl tetrazole
    • Otsuki, S. et al. Chemical tagging of a drug target using 5-sulfonyl tetrazole. Bioorg. Med. Chem. Lett. 23, 1608-1611 (2013)
    • (2013) Bioorg. Med. Chem. Lett. , vol.23 , pp. 1608-1611
    • Otsuki, S.1
  • 11
    • 58549118993 scopus 로고    scopus 로고
    • Photocrosslinking and click chemistry enable the specific detection of proteins interacting with phospholipids at the membrane interface
    • Gubbens, J. et al. Photocrosslinking and click chemistry enable the specific detection of proteins interacting with phospholipids at the membrane interface. Chem. Biol. 16, 3-14 (2009)
    • (2009) Chem. Biol. , vol.16 , pp. 3-14
    • Gubbens, J.1
  • 12
    • 84874644958 scopus 로고    scopus 로고
    • Proteome-wide mapping of cholesterol-interacting proteins in mammalian cells
    • Hulce, J. J., Cognetta, A. B., Niphakis, M. J., Tully, S. E. & Cravatt, B. F. Proteome-wide mapping of cholesterol-interacting proteins in mammalian cells. Nat. Methods 10, 259-264 (2013)
    • (2013) Nat. Methods , vol.10 , pp. 259-264
    • Hulce, J.J.1    Cognetta, A.B.2    Niphakis, M.J.3    Tully, S.E.4    Cravatt, B.F.5
  • 13
    • 84875750803 scopus 로고    scopus 로고
    • In vivo profiling and visualization of cellular protein-lipid interactions using bifunctional fatty acids
    • Haberkant, P. et al. In vivo profiling and visualization of cellular protein-lipid interactions using bifunctional fatty acids. Angew. Chem. Int. Ed. Engl. 52, 4033-4038 (2013)
    • (2013) Angew. Chem. Int. Ed. Engl. , vol.52 , pp. 4033-4038
    • Haberkant, P.1
  • 15
    • 77952306521 scopus 로고    scopus 로고
    • Membrane cholesterol in the function and organization of G-protein coupled receptors
    • Paila, Y. D. & Chattopadhyay, A. Membrane cholesterol in the function and organization of G-protein coupled receptors. Subcell. Biochem. 51, 439-466 (2010)
    • (2010) Subcell. Biochem. , vol.51 , pp. 439-466
    • Paila, Y.D.1    Chattopadhyay, A.2
  • 16
    • 0021338371 scopus 로고
    • The Pharmacological Efficacy of a Rigid Non-Phospholipid Liposome Drug Delivery System
    • Patel, K. R., Li, M. P., Schuh, J. R. & Baldeschwieler, J. D. The Pharmacological Efficacy of a Rigid Non-Phospholipid Liposome Drug Delivery System. Biochim. Biophys. Acta 797, 20-26 (1984)
    • (1984) Biochim. Biophys. Acta , vol.797 , pp. 20-26
    • Patel, K.R.1    Li, M.P.2    Schuh, J.R.3    Baldeschwieler, J.D.4
  • 17
    • 0023456179 scopus 로고
    • Hemolytic-Activity of Polyoxyethylene Cholesteryl Ethers
    • Miyajima, K., Baba, T. & Nakagaki, M. Hemolytic-Activity of Polyoxyethylene Cholesteryl Ethers. Colloid and Polymer Science 265, 943-949 (1987)
    • (1987) Colloid and Polymer Science , vol.265 , pp. 943-949
    • Miyajima, K.1    Baba, T.2    Nakagaki, M.3
  • 18
    • 0030688948 scopus 로고    scopus 로고
    • Cholesterol derivative of poly(ethylene glycol) inhibits clathrin-independent, but not clathrin-dependent endocytosis
    • Ishiwata, H., Sato, S. B., Vertut-Doi, A., Hamashima, Y. & Miyajima, K. Cholesterol derivative of poly(ethylene glycol) inhibits clathrin-independent, but not clathrin-dependent endocytosis. Biochim. Biophys. Acta 1359, 123-135 (1997)
    • (1997) Biochim. Biophys. Acta , vol.1359 , pp. 123-135
    • Ishiwata, H.1    Sato, S.B.2    Vertut-Doi, A.3    Hamashima, Y.4    Miyajima, K.5
  • 19
    • 2542493177 scopus 로고    scopus 로고
    • Distribution and transport of cholesterol-rich membrane domains monitored by a membrane-impermeant fluorescent polyethylene glycol-derivatized cholesterol
    • Sato, S. B. et al. Distribution and transport of cholesterol-rich membrane domains monitored by a membrane-impermeant fluorescent polyethylene glycol-derivatized cholesterol. J. Biol. Chem. 279, 23790-23796 (2004)
    • (2004) J. Biol. Chem. , vol.279 , pp. 23790-23796
    • Sato, S.B.1
  • 20
    • 0015236352 scopus 로고
    • Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane
    • Fairbanks, G., Steck, T. L. & Wallach, D. F. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry 10, 2606-2617 (1971)
    • (1971) Biochemistry , vol.10 , pp. 2606-2617
    • Fairbanks, G.1    Steck, T.L.2    Wallach, D.F.3
  • 21
    • 0018181781 scopus 로고
    • Influence of increased membrane cholesterol on membrane fluidity and cell function in human red blood cells
    • Cooper, R. A. Influence of increased membrane cholesterol on membrane fluidity and cell function in human red blood cells. J. Supramol. Struct. 8, 413-430 (1978)
    • (1978) J. Supramol. Struct. , vol.8 , pp. 413-430
    • Cooper, R.A.1
  • 22
    • 84861329313 scopus 로고    scopus 로고
    • Refined views of multi-protein complexes in the erythrocyte membrane
    • Mankelow, T. J., Satchwell, T. J. & Burton, N. M. Refined views of multi-protein complexes in the erythrocyte membrane. Blood Cells Mol. Dis. 49, 1-10 (2012)
    • (2012) Blood Cells Mol. Dis. , vol.49 , pp. 1-10
    • Mankelow, T.J.1    Satchwell, T.J.2    Burton, N.M.3
  • 23
    • 79953737352 scopus 로고    scopus 로고
    • Modelling the structure of the red cell membrane
    • Burton, N. M. & Bruce, L. J. Modelling the structure of the red cell membrane. Biochem. Cell Biol. 89, 200-215 (2011)
    • (2011) Biochem. Cell Biol. , vol.89 , pp. 200-215
    • Burton, N.M.1    Bruce, L.J.2
  • 24
    • 84856697704 scopus 로고    scopus 로고
    • Analysis of the mobilities of band 3 populations associated with ankyrin protein and junctional complexes in intact murine erythrocytes
    • Kodippili, G. C. et al. Analysis of the mobilities of band 3 populations associated with ankyrin protein and junctional complexes in intact murine erythrocytes. J. Biol. Chem. 287, 4129-4138 (2012)
    • (2012) J. Biol. Chem. , vol.287 , pp. 4129-4138
    • Kodippili, G.C.1
  • 25
    • 0017744051 scopus 로고
    • Band 3-protein from human erythrocyte membranes strongly interacts with cholesterol
    • Klappauf, E. & Schubert, D. Band 3-protein from human erythrocyte membranes strongly interacts with cholesterol. FEBS Lett. 80, 423-425 (1977)
    • (1977) FEBS Lett. , vol.80 , pp. 423-425
    • Klappauf, E.1    Schubert, D.2
  • 26
    • 0020364518 scopus 로고
    • Band 3 protein-cholesterol interactions in erythrocyte membranes. Possible role in anion transport and dependency on membrane phospholipids
    • Schubert, D. & Boss, K. Band 3 protein-cholesterol interactions in erythrocyte membranes. Possible role in anion transport and dependency on membrane phospholipid. FEBS Lett. 150, 4-8 (1982)
    • (1982) FEBS Lett. , vol.150 , pp. 4-8
    • Schubert, D.1    Boss, K.2
  • 27
    • 0020441513 scopus 로고
    • Influence of cholesterol on the rotation and self-association of band 3 in the human erythrocyte membrane
    • Muhlebach, T. & Cherry, R. J. Influence of cholesterol on the rotation and self-association of band 3 in the human erythrocyte membrane. Biochemistry 21, 4225-4228 (1982)
    • (1982) Biochemistry , vol.21 , pp. 4225-4228
    • Muhlebach, T.1    Cherry, R.J.2
  • 28
    • 0028006541 scopus 로고
    • Red blood cell band 3. Lysine 539 and lysine 851 react with the same H2DIDS (4, 4 -diisothiocyanodihydrostilbene-2, 2 -disulfonic acid) molecule
    • Okubo, K., Kang, D., Hamasaki, N. & Jennings, M. L. Red blood cell band 3. Lysine 539 and lysine 851 react with the same H2DIDS (4, 4 -diisothiocyanodihydrostilbene-2, 2 -disulfonic acid) molecule. J. Biol. Chem. 269, 1918-1926 (1994)
    • (1994) J. Biol. Chem. 269 , pp. 1918-1926
    • Okubo, K.1    Kang, D.2    Hamasaki, N.3    Jennings, M.L.4
  • 29
    • 33745738625 scopus 로고    scopus 로고
    • The Functional Role of Arginine 901 at the C-terminus of the Human Anion Transporter Band 3 Protein
    • Takazaki, S. et al. The functional role of arginine 901 at the C-terminus of the human anion transporter band 3 protein. J. Biochem. 139, 903-912 (2006)
    • (2006) J. Biochem. , Issue.139 , pp. 903-912
    • Takazaki, S.1
  • 30
    • 0035207136 scopus 로고    scopus 로고
    • Mechanistic basis for site-site interactions in inhibitor and substrate binding to band 3 (AE1): Evidence distinguishing allosteric from electrostatic effects
    • Salhany, J. M. Mechanistic basis for site-site interactions in inhibitor and substrate binding to band 3 (AE1): evidence distinguishing allosteric from electrostatic effects. Blood Cells Mol. Dis. 27, 901-912 (2001)
    • (2001) Blood Cells Mol. Dis. , vol.27 , pp. 901-912
    • Salhany, J.M.1
  • 31
    • 84856004739 scopus 로고    scopus 로고
    • An activity-based imaging probe for the integral membrane hydrolase KIAA1363
    • Chang, J. W., Moellering, R. E. & Cravatt, B. F. An activity-based imaging probe for the integral membrane hydrolase KIAA1363. Angew. Chem. Int. Ed. Engl. 51, 966-970 (2012)
    • (2012) Angew. Chem. Int. Ed. Engl. , vol.51 , pp. 966-970
    • Chang, J.W.1    Moellering, R.E.2    Cravatt, B.F.3
  • 32
    • 84919664417 scopus 로고    scopus 로고
    • LDAI-based chemical labeling of intact membrane proteins and its pulse-chase analysis under live cell conditions
    • Miki, T. et al. LDAI-based chemical labeling of intact membrane proteins and its pulse-chase analysis under live cell conditions. Chem. Biol. 21, 1013-1022 (2014)
    • (2014) Chem. Biol. , vol.21 , pp. 1013-1022
    • Miki, T.1
  • 33
    • 77952305288 scopus 로고    scopus 로고
    • Cholesterol interaction with proteins that partition into membrane domains: An overview
    • Epand, R. M., Thomas, A., Brasseur, R. & Epand, R. F. Cholesterol interaction with proteins that partition into membrane domains: an overview. Subcell. Biochem. 51, 253-278 (2010)
    • (2010) Subcell. Biochem. , vol.51 , pp. 253-278
    • Epand, R.M.1    Thomas, A.2    Brasseur, R.3    Epand, R.F.4
  • 34
    • 84874427933 scopus 로고    scopus 로고
    • Mapping the functional binding sites of cholesterol in beta2-adrenergic receptor by long-time molecular dynamics simulations
    • Cang, X. et al. Mapping the functional binding sites of cholesterol in beta2-adrenergic receptor by long-time molecular dynamics simulations. J. Phys. Chem. B 117, 1085-1094 (2013)
    • (2013) J. Phys. Chem. B , vol.117 , pp. 1085-1094
    • Cang, X.1
  • 35
    • 84903316607 scopus 로고    scopus 로고
    • Fat & fabulous: Bifunctional lipids in the spotlight
    • Haberkant, P. & Holthuis, J. C. Fat & fabulous: bifunctional lipids in the spotlight. Biochim. Biophys. Acta 1841, 1022-1030 (2014).
    • (2014) Biochim. Biophys. Acta , vol.1841 , pp. 1022-1030
    • Haberkant, P.1    Holthuis, J.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.