메뉴 건너뛰기




Volumn 1788, Issue 9, 2009, Pages 1813-1821

Functional studies of membrane-bound and purified human Hedgehog receptor Patched expressed in yeast

Author keywords

Fluorinated surfactants; Heterologous expression; Membrane receptor; Patched; Sonic Hedgehog

Indexed keywords

LIGAND; MEMBRANE RECEPTOR; PROTEIN PATCHED; SONIC HEDGEHOG PROTEIN; SURFACTANT;

EID: 68749094054     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2009.05.009     Document Type: Article
Times cited : (14)

References (36)
  • 1
    • 0035577854 scopus 로고    scopus 로고
    • Hedgehog signaling in animal development: paradigms and principles
    • Ingham P.W., and McMahon A.P. Hedgehog signaling in animal development: paradigms and principles. Genes Dev. 15 (2001) 3059-3087
    • (2001) Genes Dev. , vol.15 , pp. 3059-3087
    • Ingham, P.W.1    McMahon, A.P.2
  • 2
    • 9244221172 scopus 로고    scopus 로고
    • Tissue repair and stem cell renewal in carcinogenesis
    • Beachy P.A., Karhadkar S.S., and Berman D.M. Tissue repair and stem cell renewal in carcinogenesis. Nature 432 (2004) 324-331
    • (2004) Nature , vol.432 , pp. 324-331
    • Beachy, P.A.1    Karhadkar, S.S.2    Berman, D.M.3
  • 3
    • 0024468746 scopus 로고
    • The Drosophila patched gene encodes a putative membrane protein required for segmental patterning
    • Hooper J.E., and Scott M.P. The Drosophila patched gene encodes a putative membrane protein required for segmental patterning. Cell 59 (1989) 751-765
    • (1989) Cell , vol.59 , pp. 751-765
    • Hooper, J.E.1    Scott, M.P.2
  • 5
    • 0035374351 scopus 로고    scopus 로고
    • The sonic hedgehog receptor patched associates with caveolin-1 in cholesterol-rich microdomains of the plasma membrane
    • Karpen H.E., Bukowski J.T., Hughes T., Gratton J.P., Sessa W.C., and Gailani M.R. The sonic hedgehog receptor patched associates with caveolin-1 in cholesterol-rich microdomains of the plasma membrane. J. Biol. Chem. 276 (2001) 19503-19511
    • (2001) J. Biol. Chem. , vol.276 , pp. 19503-19511
    • Karpen, H.E.1    Bukowski, J.T.2    Hughes, T.3    Gratton, J.P.4    Sessa, W.C.5    Gailani, M.R.6
  • 6
    • 0035902140 scopus 로고    scopus 로고
    • The Hedgehog and Wnt signalling pathways in cancer
    • Taipale J., and Beachy P.A. The Hedgehog and Wnt signalling pathways in cancer. Nature 411 (2001) 349-354
    • (2001) Nature , vol.411 , pp. 349-354
    • Taipale, J.1    Beachy, P.A.2
  • 7
    • 34547110771 scopus 로고    scopus 로고
    • Patched1 regulates hedgehog signaling at the primary cilium
    • Rohatgi R., Milenkovic L., and Scott M.P. Patched1 regulates hedgehog signaling at the primary cilium. Science 317 (2007) 372-376
    • (2007) Science , vol.317 , pp. 372-376
    • Rohatgi, R.1    Milenkovic, L.2    Scott, M.P.3
  • 8
    • 0035979797 scopus 로고    scopus 로고
    • Overexpression of mammalian integral membrane proteins for structural studies
    • Tate C.G. Overexpression of mammalian integral membrane proteins for structural studies. FEBS Lett. 504 (2001) 94-98
    • (2001) FEBS Lett. , vol.504 , pp. 94-98
    • Tate, C.G.1
  • 9
    • 0036932867 scopus 로고    scopus 로고
    • Heterologous expression and purification systems for structural proteomics of mammalian membrane proteins
    • Mus-Veteau I. Heterologous expression and purification systems for structural proteomics of mammalian membrane proteins. Compar. Funct. Genom. 3 (2002) 511-517
    • (2002) Compar. Funct. Genom. , vol.3 , pp. 511-517
    • Mus-Veteau, I.1
  • 10
    • 33749420875 scopus 로고    scopus 로고
    • Human receptors patched and smoothened partially transduce hedgehog signal when expressed in Drosophila cells
    • De Rivoyre M., Ruel L., Varjosalo M., Loubat A., Bidet M., Therond P., and Mus-Veteau I. Human receptors patched and smoothened partially transduce hedgehog signal when expressed in Drosophila cells. J. Biol. Chem. 281 (2006) 28584-28595
    • (2006) J. Biol. Chem. , vol.281 , pp. 28584-28595
    • De Rivoyre, M.1    Ruel, L.2    Varjosalo, M.3    Loubat, A.4    Bidet, M.5    Therond, P.6    Mus-Veteau, I.7
  • 11
    • 0034176255 scopus 로고    scopus 로고
    • Use of chemical chaperones in the yeast Saccharomyces cerevisiae to enhance heterologous membrane protein expression: high-yield expression and purification of human P-glycoprotein
    • Figler R.A., Omote H., Nakamoto R.K., and Al-Shawi M.K. Use of chemical chaperones in the yeast Saccharomyces cerevisiae to enhance heterologous membrane protein expression: high-yield expression and purification of human P-glycoprotein. Arch. Biochem. Biophys. 376 (2000) 34-46
    • (2000) Arch. Biochem. Biophys. , vol.376 , pp. 34-46
    • Figler, R.A.1    Omote, H.2    Nakamoto, R.K.3    Al-Shawi, M.K.4
  • 12
    • 14244253570 scopus 로고    scopus 로고
    • Human receptor Smoothened, a mediator of Hedgehog signalling, expressed in its native conformation in yeast
    • De Rivoyre M., Bonino F., Ruel L., Bidet M., Therond P., and Mus-Veteau I. Human receptor Smoothened, a mediator of Hedgehog signalling, expressed in its native conformation in yeast. FEBS Lett. 579 (2005) 1529-1533
    • (2005) FEBS Lett. , vol.579 , pp. 1529-1533
    • De Rivoyre, M.1    Bonino, F.2    Ruel, L.3    Bidet, M.4    Therond, P.5    Mus-Veteau, I.6
  • 13
    • 0026703547 scopus 로고
    • A simple and efficient procedure for transformation of yeasts
    • Elble R. A simple and efficient procedure for transformation of yeasts. Biotechniques 13 (1992) 18-20
    • (1992) Biotechniques , vol.13 , pp. 18-20
    • Elble, R.1
  • 14
    • 0000511093 scopus 로고
    • New perfluoroalkylated telomeric non ionic surfactants synthesis physicochemical and biological properties
    • Pavia A.A., Pucci B., Riess J.G., and Zarif L. New perfluoroalkylated telomeric non ionic surfactants synthesis physicochemical and biological properties. Makromol. Chem. 193 (1992) 2505-2517
    • (1992) Makromol. Chem. , vol.193 , pp. 2505-2517
    • Pavia, A.A.1    Pucci, B.2    Riess, J.G.3    Zarif, L.4
  • 15
    • 0032075801 scopus 로고    scopus 로고
    • Stabilization of integral membrane proteins in aqueous solution using fluorinated surfactants
    • Chabaud E., Barthelemy P., Mora N., Popot J.L., and Pucci B. Stabilization of integral membrane proteins in aqueous solution using fluorinated surfactants. Biochimie 80 (1998) 515-530
    • (1998) Biochimie , vol.80 , pp. 515-530
    • Chabaud, E.1    Barthelemy, P.2    Mora, N.3    Popot, J.L.4    Pucci, B.5
  • 16
    • 0036411421 scopus 로고    scopus 로고
    • High expression and anterograde axonal transport of aminoterminal sonic hedgehog in the adult hamster brain
    • Traiffort E., Moya K.L., Faure H., Hassig R., and Ruat M. High expression and anterograde axonal transport of aminoterminal sonic hedgehog in the adult hamster brain. Eur. J. Neurosci. 14 (2001) 839-850
    • (2001) Eur. J. Neurosci. , vol.14 , pp. 839-850
    • Traiffort, E.1    Moya, K.L.2    Faure, H.3    Hassig, R.4    Ruat, M.5
  • 17
    • 0032321834 scopus 로고    scopus 로고
    • High-level expression of mouse Mdr3 P-glycoprotein in yeast Pichia pastoris and characterization of ATPase activity
    • Beaudet L., Urbatsch L., and Gros P. High-level expression of mouse Mdr3 P-glycoprotein in yeast Pichia pastoris and characterization of ATPase activity. Methods Enzymol. 292 (1998) 397-413
    • (1998) Methods Enzymol. , vol.292 , pp. 397-413
    • Beaudet, L.1    Urbatsch, L.2    Gros, P.3
  • 19
    • 20444383119 scopus 로고    scopus 로고
    • Functional studies with membrane-bound and detergent-solubilized alpha2-adrenergic receptors expressed in Sf9 cells
    • Sen S., Jaakola V.P., Pirila P., Finel M., and Goldman A. Functional studies with membrane-bound and detergent-solubilized alpha2-adrenergic receptors expressed in Sf9 cells. Biochim. Biophys. Acta 1712 (2005) 62-70
    • (2005) Biochim. Biophys. Acta , vol.1712 , pp. 62-70
    • Sen, S.1    Jaakola, V.P.2    Pirila, P.3    Finel, M.4    Goldman, A.5
  • 20
    • 1942532324 scopus 로고    scopus 로고
    • Hemifluorinated surfactants: a non-dissociating environment for handling membrane proteins in aqueous solutions?
    • Breyton C., Chabaud E., Chaudier Y., Pucci B., and Popot J.L. Hemifluorinated surfactants: a non-dissociating environment for handling membrane proteins in aqueous solutions?. FEBS Lett. 564 (2004) 312-318
    • (2004) FEBS Lett. , vol.564 , pp. 312-318
    • Breyton, C.1    Chabaud, E.2    Chaudier, Y.3    Pucci, B.4    Popot, J.L.5
  • 21
    • 34247620784 scopus 로고    scopus 로고
    • New tensio-active molecules stabilize a human G protein-coupled receptor in solution
    • Damian M., Perino S., Polidori A., Martin A., Serre L., Pucci B., and Baneres J.L. New tensio-active molecules stabilize a human G protein-coupled receptor in solution. FEBS Lett. 581 (2007) 1944-1950
    • (2007) FEBS Lett. , vol.581 , pp. 1944-1950
    • Damian, M.1    Perino, S.2    Polidori, A.3    Martin, A.4    Serre, L.5    Pucci, B.6    Baneres, J.L.7
  • 22
    • 34147158906 scopus 로고    scopus 로고
    • Fluorinated and hemifluorinated surfactants as alternatives to detergents for membrane protein cell-free synthesis
    • Park K.H., Berrier C., Lebaupain F., Pucci B., Popot J.L., Ghazi A., and Zito F. Fluorinated and hemifluorinated surfactants as alternatives to detergents for membrane protein cell-free synthesis. Biochem. J. 403 (2007) 183-187
    • (2007) Biochem. J. , vol.403 , pp. 183-187
    • Park, K.H.1    Berrier, C.2    Lebaupain, F.3    Pucci, B.4    Popot, J.L.5    Ghazi, A.6    Zito, F.7
  • 23
    • 0035830632 scopus 로고    scopus 로고
    • Vesicular monoamine transporters heterologously expressed in the yeast Saccharomyces cerevisiae display high-affinity tetrabenazine binding
    • Yelin R., and Schuldiner S. Vesicular monoamine transporters heterologously expressed in the yeast Saccharomyces cerevisiae display high-affinity tetrabenazine binding. Biochim. Biophys. Acta 1510 (2001) 426-441
    • (2001) Biochim. Biophys. Acta , vol.1510 , pp. 426-441
    • Yelin, R.1    Schuldiner, S.2
  • 24
    • 3543088051 scopus 로고    scopus 로고
    • Decreases in yeast expression yields of the human adenosine A2a receptor are a result of translational or post-translational events
    • Niebauer R.T., Wedekind A., and Robinson A.S. Decreases in yeast expression yields of the human adenosine A2a receptor are a result of translational or post-translational events. Protein. Expr. Purif. 37 (2004) 134-143
    • (2004) Protein. Expr. Purif. , vol.37 , pp. 134-143
    • Niebauer, R.T.1    Wedekind, A.2    Robinson, A.S.3
  • 25
    • 0029948270 scopus 로고    scopus 로고
    • Biochemical evidence that patched is the Hedgehog receptor
    • Marigo V., Davey R.A., Zuo Y., Cunningham J.M., and Tabin C.J. Biochemical evidence that patched is the Hedgehog receptor. Nature 384 (1996) 176-179
    • (1996) Nature , vol.384 , pp. 176-179
    • Marigo, V.1    Davey, R.A.2    Zuo, Y.3    Cunningham, J.M.4    Tabin, C.J.5
  • 26
    • 0029004233 scopus 로고
    • Floor plate and motor neuron induction by different concentrations of the amino-terminal cleavage product of sonic hedgehog autoproteolysis
    • Roelink H., Porter J.A., Chiang C., Tanabe Y., Chang D.T., Beachy P.A., and Jessell T.M. Floor plate and motor neuron induction by different concentrations of the amino-terminal cleavage product of sonic hedgehog autoproteolysis. Cell 81 (1995) 445-455
    • (1995) Cell , vol.81 , pp. 445-455
    • Roelink, H.1    Porter, J.A.2    Chiang, C.3    Tanabe, Y.4    Chang, D.T.5    Beachy, P.A.6    Jessell, T.M.7
  • 27
    • 4143052387 scopus 로고    scopus 로고
    • Functional expression of heterologous proteins in yeast: insights into Ca2+ signaling and Ca2+-transporting ATPases
    • Ton V.K., and Rao R. Functional expression of heterologous proteins in yeast: insights into Ca2+ signaling and Ca2+-transporting ATPases. Am. J. Physiol. Cell. Physiol. 287 (2004) C580-589
    • (2004) Am. J. Physiol. Cell. Physiol. , vol.287
    • Ton, V.K.1    Rao, R.2
  • 29
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution
    • Toyoshima C., Nakasako M., Nomura H., and Ogawa H. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution. Nature 405 (2000) 647-655
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 30
    • 23244456428 scopus 로고    scopus 로고
    • Crystal structure of a mammalian voltage-dependent Shaker family K+ channel
    • Long S.B., Campbell E.B., and Mackinnon R. Crystal structure of a mammalian voltage-dependent Shaker family K+ channel. Science 309 (2005) 897-903
    • (2005) Science , vol.309 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    Mackinnon, R.3
  • 31
    • 36248982122 scopus 로고    scopus 로고
    • Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment
    • Long S.B., Tao X., Campbell E.B., and MacKinnon R. Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment. Nature 450 (2007) 376-382
    • (2007) Nature , vol.450 , pp. 376-382
    • Long, S.B.1    Tao, X.2    Campbell, E.B.3    MacKinnon, R.4
  • 33
    • 34547631962 scopus 로고    scopus 로고
    • Crystal structure of a human membrane protein involved in cysteinyl leukotriene biosynthesis
    • Ago H., Kanaoka Y., Irikura D., Lam B.K., Shimamura T., Austen K.F., and Miyano M. Crystal structure of a human membrane protein involved in cysteinyl leukotriene biosynthesis. Nature 448 (2007) 609-612
    • (2007) Nature , vol.448 , pp. 609-612
    • Ago, H.1    Kanaoka, Y.2    Irikura, D.3    Lam, B.K.4    Shimamura, T.5    Austen, K.F.6    Miyano, M.7
  • 36


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.