메뉴 건너뛰기




Volumn 45, Issue 5, 2011, Pages 823-832

Bacterial synthesis, purification, and solubilization of transmembrane segments of ErbB family receptors

Author keywords

bacterial expression; detergent solubilization; ErbB; membrane protein; NMR; purification

Indexed keywords

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 80053646132     PISSN: 00268933     EISSN: 16083245     Source Type: Journal    
DOI: 10.1134/S0026893311040066     Document Type: Article
Times cited : (6)

References (55)
  • 1
    • 0034600849 scopus 로고    scopus 로고
    • The ErbB signaling network: Receptor heterodimerization in development and cancer
    • Olayioye M. A., Neve R. M., Lane H. A., Hynes N. E. 2000. The ErbB signaling network: Receptor heterodimerization in development and cancer. EMBO J. 19, 3159-3167.
    • (2000) EMBO J , vol.19 , pp. 3159-3167
    • Olayioye, M.A.1    Neve, R.M.2    Lane, H.A.3    Hynes, N.E.4
  • 3
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger J. 2000. Cell signaling by receptor tyrosine kinases. Cell. 103, 211-225.
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 4
    • 0023942517 scopus 로고
    • Growth factor receptor tyrosine kinases
    • Yarden Y., Ullrich A. 1988. Growth factor receptor tyrosine kinases. Annu. Rev. Biochem. 57, 443-478.
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 443-478
    • Yarden, Y.1    Ullrich, A.2
  • 6
    • 0028328538 scopus 로고
    • The type I growth factor receptors in human breast cancer
    • Rajkumar T., Gullick W. J. 1994. The type I growth factor receptors in human breast cancer. Breast Cancer Res. Treat. 29, 3-9.
    • (1994) Breast Cancer Res. Treat. , vol.29 , pp. 3-9
    • Rajkumar, T.1    Gullick, W.J.2
  • 7
    • 33645130990 scopus 로고    scopus 로고
    • Signaling through ERBB receptors: Multiple layers of diversity and control
    • Warren C. M., Landgraf R. 2006. Signaling through ERBB receptors: Multiple layers of diversity and control. Cell. Signal. 18, 923-933.
    • (2006) Cell. Signal , vol.18 , pp. 923-933
    • Warren, C.M.1    Landgraf, R.2
  • 8
    • 0035979763 scopus 로고    scopus 로고
    • Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain
    • Moriki T., Maruyama H., Maruyama I. N. 2001. Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain. J. Mol. Biol. 311, 1011-1026.
    • (2001) J. Mol. Biol. , vol.311 , pp. 1011-1026
    • Moriki, T.1    Maruyama, H.2    Maruyama, I.N.3
  • 9
    • 0037429725 scopus 로고    scopus 로고
    • The ErbB receptors and their role in cancer progression
    • Holbro T., Civenni G., Hynes N. E. 2003. The ErbB receptors and their role in cancer progression. Exp. Cell Res. 284, 99-110.
    • (2003) Exp. Cell Res. , vol.284 , pp. 99-110
    • Holbro, T.1    Civenni, G.2    Hynes, N.E.3
  • 10
    • 0033063774 scopus 로고    scopus 로고
    • The epidermal growth factor receptor and its inhibition in cancer therapy
    • Woodburn J. R. 1999. The epidermal growth factor receptor and its inhibition in cancer therapy. Pharmacol. Ther. 82, 241-250.
    • (1999) Pharmacol. Ther. , vol.82 , pp. 241-250
    • Woodburn, J.R.1
  • 12
    • 16844369407 scopus 로고    scopus 로고
    • Absence of HER4 expression predicts recurrence of ductal carcinoma in situ of the breast
    • Barnes N. L., Khavari S., Boland G. P., Cramer A., Knox W. F., Bundred N. J. 2005. Absence of HER4 expression predicts recurrence of ductal carcinoma in situ of the breast. Clin. Cancer Res. 11, 2163-2168.
    • (2005) Clin. Cancer Res , vol.11 , pp. 2163-2168
    • Barnes, N.L.1    Khavari, S.2    Boland, G.P.3    Cramer, A.4    Knox, W.F.5    Bundred, N.J.6
  • 14
    • 0037145061 scopus 로고    scopus 로고
    • Ligand-induced, receptor-mediated dimerization and activation of EGF receptor
    • Schlessinger J. 2002. Ligand-induced, receptor-mediated dimerization and activation of EGF receptor. Cell. 110, 669-672.
    • (2002) Cell , vol.110 , pp. 669-672
    • Schlessinger, J.1
  • 15
    • 55449102296 scopus 로고    scopus 로고
    • All EGF(ErbB) receptors have preformed homo- and heterodimeric structures in living cells
    • Tao R. H., Maruyama I. N. 2008. All EGF(ErbB) receptors have preformed homo- and heterodimeric structures in living cells. J. Cell Sci. 121, 3207-3217.
    • (2008) J. Cell Sci. , vol.121 , pp. 3207-3217
    • Tao, R.H.1    Maruyama, I.N.2
  • 17
    • 33847118661 scopus 로고    scopus 로고
    • A dimerization hierarchy in the transmembrane domains of the HER receptor family
    • Duneau J. P., Vegh A. P., Sturgis J. N. 2007. A dimerization hierarchy in the transmembrane domains of the HER receptor family. Biochemistry. 46, 2010-2019.
    • (2007) Biochemistry , vol.46 , pp. 2010-2019
    • Duneau, J.P.1    Vegh, A.P.2    Sturgis, J.N.3
  • 18
    • 0037085373 scopus 로고    scopus 로고
    • The single transmembrane domains of ErbB receptors self-associate in cell membranes
    • Mendrola J. M., Berger M. B., King M. C., Lemmon M. A. 2002. The single transmembrane domains of ErbB receptors self-associate in cell membranes. J. Biol. Chem. 277, 4704-4712.
    • (2002) J. Biol. Chem. , vol.277 , pp. 4704-4712
    • Mendrola, J.M.1    Berger, M.B.2    King, M.C.3    Lemmon, M.A.4
  • 19
    • 33646889068 scopus 로고    scopus 로고
    • Role of receptor tyrosine kinase transmembrane domains in cell signaling and human pathologies
    • Li E., Hristova K. 2006. Role of receptor tyrosine kinase transmembrane domains in cell signaling and human pathologies. Biochemistry. 45, 6241-6251.
    • (2006) Biochemistry , vol.45 , pp. 6241-6251
    • Li, E.1    Hristova, K.2
  • 20
    • 0036996692 scopus 로고    scopus 로고
    • Polar mutations in membrane proteins as a biophysical basis for disease
    • Partridge A. W., Therien A. G., Deber C. M. 2002. Polar mutations in membrane proteins as a biophysical basis for disease. Biopolymers. 66, 350-358.
    • (2002) Biopolymers , vol.66 , pp. 350-358
    • Partridge, A.W.1    Therien, A.G.2    Deber, C.M.3
  • 22
    • 67349094494 scopus 로고    scopus 로고
    • Two GxxxG-like motifs facilitate promiscuous interactions of the human ErbB transmembrane domains
    • Escher C., Cymer F., Schneider D. 2009. Two GxxxG-like motifs facilitate promiscuous interactions of the human ErbB transmembrane domains. J. Mol. Biol. 389, 10-16.
    • (2009) J. Mol. Biol. , vol.389 , pp. 10-16
    • Escher, C.1    Cymer, F.2    Schneider, D.3
  • 23
    • 33646902110 scopus 로고    scopus 로고
    • Folding and stability of alphahelical integral membrane proteins
    • Mackenzie K. R. 2006. Folding and stability of alphahelical integral membrane proteins. Chem. Rev. 106, 1931-1977.
    • (2006) Chem. Rev. , vol.106 , pp. 1931-1977
    • Mackenzie, K.R.1
  • 24
    • 0034711953 scopus 로고    scopus 로고
    • The GxxxG motif: a framework for transmembrane helix-helix association
    • Russ W. P., Engelman D. M. 2000. The GxxxG motif: a framework for transmembrane helix-helix association. J. Mol. Biol. 296, 911-919.
    • (2000) J. Mol. Biol. , vol.296 , pp. 911-919
    • Russ, W.P.1    Engelman, D.M.2
  • 25
    • 0042931286 scopus 로고    scopus 로고
    • Sequence motifs, polar interactions and conformational changes in helical membrane proteins
    • Curran A. R., Engelman D. M. 2003. Sequence motifs, polar interactions and conformational changes in helical membrane proteins. Curr. Opin. Struct. Biol. 13, 412-417.
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 412-417
    • Curran, A.R.1    Engelman, D.M.2
  • 26
    • 33846688205 scopus 로고    scopus 로고
    • Prediction and simulation of motion in pairs of transmembrane alpha-helices
    • Enosh A., Fleishman S. J., Ben-Tal N., Halperin D. 2007. Prediction and simulation of motion in pairs of transmembrane alpha-helices. Bioinformatics. 23, 212-218.
    • (2007) Bioinformatics , vol.23 , pp. 212-218
    • Enosh, A.1    Fleishman, S.J.2    Ben-Tal, N.3    Halperin, D.4
  • 27
    • 0037199467 scopus 로고    scopus 로고
    • Transmembrane interactions in the activation of the Neu receptor tyrosine kinase
    • Smith S. O., Smith C., Shekar S., Peersen O., Ziliox M., Aimoto S. 2002. Transmembrane interactions in the activation of the Neu receptor tyrosine kinase. Biochemistry. 41, 9321-9332.
    • (2002) Biochemistry , vol.41 , pp. 9321-9332
    • Smith, S.O.1    Smith, C.2    Shekar, S.3    Peersen, O.4    Ziliox, M.5    Aimoto, S.6
  • 28
    • 18744378545 scopus 로고    scopus 로고
    • A putative molecular-activation switch in the transmembrane domain of erbB2
    • Fleishman S. J., Schlessinger J., Ben-Tal N. 2002. A putative molecular-activation switch in the transmembrane domain of erbB2. Proc. Natl. Acad. Sci. U. S. A. 99, 15937-15940.
    • (2002) Proc. Natl. Acad. Sci. U. S. A , vol.99 , pp. 15937-15940
    • Fleishman, S.J.1    Schlessinger, J.2    Ben-Tal, N.3
  • 29
    • 0033615077 scopus 로고    scopus 로고
    • Receptor signaling: When dimerization is not enough
    • Jiang G., Hunter T. 1999. Receptor signaling: When dimerization is not enough. Curr. Biol. 9, 568-571.
    • (1999) Curr. Biol. , vol.9 , pp. 568-571
    • Jiang, G.1    Hunter, T.2
  • 32
    • 36148942092 scopus 로고    scopus 로고
    • Breaking the bottleneck: Eukaryotic membrane protein expression for high-resolution structural studies
    • Midgett C. R., Madden D. R. 2007. Breaking the bottleneck: Eukaryotic membrane protein expression for high-resolution structural studies. J. Struct. Biol. 160, 265-274.
    • (2007) J. Struct. Biol. , vol.160 , pp. 265-274
    • Midgett, C.R.1    Madden, D.R.2
  • 33
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: Structure and implications
    • MacKenzie K. R., Prestegard J. H., Engelman D. M. 1997. A transmembrane helix dimer: Structure and implications. Science. 276, 131-133.
    • (1997) Science , vol.276 , pp. 131-133
    • Mackenzie, K.R.1    Prestegard, J.H.2    Engelman, D.M.3
  • 35
    • 67049171187 scopus 로고    scopus 로고
    • Structural basis for dimerization of the BNIP3 transmembrane domain
    • Sulistijo E. S., Mackenzie K. R. 2009. Structural basis for dimerization of the BNIP3 transmembrane domain. Biochemistry. 48, 5106-5120.
    • (2009) Biochemistry , vol.48 , pp. 5106-5120
    • Sulistijo, E.S.1    Mackenzie, K.R.2
  • 41
    • 0029820642 scopus 로고    scopus 로고
    • Transmembrane region of the epidermal growth factor receptor: Behavior and interactions via 2H NMR
    • Rigby A. C., Barber K. R., Shaw G. S., Grant C. W. 1996. Transmembrane region of the epidermal growth factor receptor: Behavior and interactions via 2H NMR. Biochemistry. 35, 12591-12601.
    • (1996) Biochemistry , vol.35 , pp. 12591-12601
    • Rigby, A.C.1    Barber, K.R.2    Shaw, G.S.3    Grant, C.W.4
  • 42
    • 0032575092 scopus 로고    scopus 로고
    • Sequence-related behaviour of transmembrane domains from class I receptor tyrosine kinases
    • Jones D. H., Barber K. R., Grant C. W. 1998. Sequence-related behaviour of transmembrane domains from class I receptor tyrosine kinases. Biochim. Biophys. Acta. 1371, 199-212.
    • (1998) Biochim. Biophys. Acta. , vol.1371 , pp. 199-212
    • Jones, D.H.1    Barber, K.R.2    Grant, C.W.3
  • 43
    • 0037472804 scopus 로고    scopus 로고
    • Comparison of proto-oncogenic and mutant forms of the transmembrane region of the Neu receptor in TFE
    • Houliston R. S., Hodges R. S., Sharom F. J., Davis J. H. 2003. Comparison of proto-oncogenic and mutant forms of the transmembrane region of the Neu receptor in TFE. FEBS Lett. 535, 39-43.
    • (2003) FEBS Lett , vol.535 , pp. 39-43
    • Houliston, R.S.1    Hodges, R.S.2    Sharom, F.J.3    Davis, J.H.4
  • 44
    • 33646409069 scopus 로고    scopus 로고
    • Revisited and large-scale synthesis and purification of the mutated and wild type neu/erbB-2 membrane-spanning segment
    • Khemtémourian L., Lavielle S., Bathany K., Schmitter J. M., Dufourc E. J. 2006. Revisited and large-scale synthesis and purification of the mutated and wild type neu/erbB-2 membrane-spanning segment. J. Pept. Sci. 12, 361-368.
    • (2006) J. Pept. Sci. , vol.12 , pp. 361-368
    • Khemtémourian, L.1    Lavielle, S.2    Bathany, K.3    Schmitter, J.M.4    Dufourc, E.J.5
  • 45
    • 0034701030 scopus 로고    scopus 로고
    • Expression and membrane assembly of a transmembrane region from Neu
    • Jones D. H., Ball E. H., Sharpe S., Barber K. R., Grant C. W. 2000. Expression and membrane assembly of a transmembrane region from Neu. Biochemistry. 39, 1870-1878.
    • (2000) Biochemistry , vol.39 , pp. 1870-1878
    • Jones, D.H.1    Ball, E.H.2    Sharpe, S.3    Barber, K.R.4    Grant, C.W.5
  • 46
    • 0034732721 scopus 로고    scopus 로고
    • Val(659) → Glu mutation within the transmembrane domain of ErbB-2: Effects measured by (2)H NMR in fluid phospholipid bilayers
    • Sharpe S., Barber K. R., Grant C. W. 2000. Val(659) → Glu mutation within the transmembrane domain of ErbB-2: Effects measured by (2)H NMR in fluid phospholipid bilayers. Biochemistry. 39, 6572-6580.
    • (2000) Biochemistry , vol.39 , pp. 6572-6580
    • Sharpe, S.1    Barber, K.R.2    Grant, C.W.3
  • 50
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama N., Woody R. W. 2000. Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287, 252-260.
    • (2000) Anal. Biochem , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 52
    • 70349745154 scopus 로고    scopus 로고
    • Recent advances in the application of solution NMR spectroscopy to multi-span integral membrane proteins
    • Kim H. J., Howell S. C., van Horn W. D., Jeon Y. H., Sanders C. R. 2009. Recent advances in the application of solution NMR spectroscopy to multi-span integral membrane proteins. Prog. Nucl. Magn. Reson. Spectrosc. 55, 335-360.
    • (2009) Prog. Nucl. Magn. Reson. Spectrosc. , vol.55 , pp. 335-360
    • Kim, H.J.1    Howell, S.C.2    van Horn, W.D.3    Jeon, Y.H.4    Sanders, C.R.5
  • 54
    • 33645509371 scopus 로고    scopus 로고
    • Magnetic resonance investigations of lipid motion in isotropic bicelles
    • Andersson A., Mäler L. 2005. Magnetic resonance investigations of lipid motion in isotropic bicelles. Langmuir. 21, 7702-7709.
    • (2005) Langmuir , vol.21 , pp. 7702-7709
    • Andersson, A.1    Mäler, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.