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Volumn 29, Issue 13, 2013, Pages 1623-1630

Self-interaction of transmembrane helices representing pre-clusters from the human single-span membrane proteins

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; PROTEOME;

EID: 84879934872     PISSN: 13674803     EISSN: 14602059     Source Type: Journal    
DOI: 10.1093/bioinformatics/btt247     Document Type: Conference Paper
Times cited : (15)

References (47)
  • 1
    • 2342449189 scopus 로고    scopus 로고
    • Experimental measurement of the strength of a C alpha-H O bond in a lipid bilayer
    • Arbely, E. and Arkin, I.T. (2004) Experimental measurement of the strength of a C alpha-H. . .O bond in a lipid bilayer. J. Am. Chem. Soc., 126, 5362-5363.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 5362-5363
    • Arbely, E.1    Arkin, I.T.2
  • 2
    • 84873292211 scopus 로고    scopus 로고
    • Architecture and membrane interactions of the EGF receptor
    • Arkhipov, A. et al. (2013) Architecture and membrane interactions of the EGF receptor. Cell, 152, 557-569.
    • (2013) Cell , vol.152 , pp. 557-569
    • Arkhipov, A.1
  • 3
    • 76249120625 scopus 로고    scopus 로고
    • Consensus motif for integrin transmembrane helix association
    • Berger, B.W. et al. (2010) Consensus motif for integrin transmembrane helix association. Proc. Natl Acad. Sci. USA, 107, 703-708.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 703-708
    • Berger, B.W.1
  • 4
    • 0031956790 scopus 로고    scopus 로고
    • The dimerization motif of the glycophorin A transmembrane segment in membranes: Importance of glycine residues
    • Brosig, B. and Langosch, D. (1998) The dimerization motif of the glycophorin A transmembrane segment in membranes: Importance of glycine residues. Protein Sci., 7, 1052-1056.
    • (1998) Protein Sci. , vol.7 , pp. 1052-1056
    • Brosig, B.1    Langosch, D.2
  • 5
    • 36148934115 scopus 로고    scopus 로고
    • Structural elements necessary for oligomerization trafficking, and cell sorting function of paraxial protocadherin
    • Chen, X. et al. (2007) Structural elements necessary for oligomerization, trafficking, and cell sorting function of paraxial protocadherin. J. Biol. Chem., 282, 32128-32137.
    • (2007) J. Biol. Chem. , vol.282 , pp. 32128-32137
    • Chen, X.1
  • 6
    • 77953594623 scopus 로고    scopus 로고
    • Transmembrane helix-helix interactions involved in ErbB receptor signaling
    • Cymer, F. and Schneider, D. (2010) Transmembrane helix-helix interactions involved in ErbB receptor signaling. Cell Adh. Migr., 4, 299-312.
    • (2010) Cell Adh. Migr. , vol.4 , pp. 299-312
    • Cymer, F.1    Schneider, D.2
  • 7
    • 84857529575 scopus 로고    scopus 로고
    • Transmembrane helix-helix interactions are modulated by the sequence context and by lipid bilayer properties
    • Cymer, F. et al. (2012) Transmembrane helix-helix interactions are modulated by the sequence context and by lipid bilayer properties. Biochim. Biophys. Acta, 1818, 963-973.
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 963-973
    • Cymer, F.1
  • 8
    • 0036301006 scopus 로고    scopus 로고
    • Motifs of serine and threonine can drive association of transmembrane helices
    • Dawson, J.P. et al. (2002) Motifs of serine and threonine can drive association of transmembrane helices. J. Mol. Biol., 316, 799-805.
    • (2002) J. Mol. Biol. , vol.316 , pp. 799-805
    • Dawson, J.P.1
  • 9
    • 67349094494 scopus 로고    scopus 로고
    • Two GxxxG-like motifs facilitate promiscuous interactions of the human ErbB transmembrane domains
    • Escher, C. et al. (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
  • 10
    • 0029450142 scopus 로고
    • Binding domain regulation of MHC class II molecule assembly, trafficking, fate, and function
    • Germain, R.N. (1995) Binding domain regulation of MHC class II molecule assembly, trafficking, fate, and function. Semin. Immunol., 7, 361-372.
    • (1995) Semin. Immunol. , vol.7 , pp. 361-372
    • Germain, R.N.1
  • 11
    • 0010564906 scopus 로고
    • Interaction between proteins localized in membranes
    • Grasberger, B. et al. (1986) Interaction between proteins localized in membranes. Proc. Natl Acad. Sci. USA, 83, 6258-6262.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 6258-6262
    • Grasberger, B.1
  • 12
    • 0033515557 scopus 로고    scopus 로고
    • A heptad motif of leucine residues found in membrane proteins can drive self-assembly of artificial transmembrane segments
    • Gurezka, R. et al. (1999) A heptad motif of leucine residues found in membrane proteins can drive self-assembly of artificial transmembrane segments. J. Biol. Chem., 274, 9265-9270.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9265-9270
    • Gurezka, R.1
  • 13
    • 77449104569 scopus 로고    scopus 로고
    • Ionic interactions promote transmembrane helix-helix association depending on sequence context
    • Herrmann, J.R. et al. (2010) Ionic interactions promote transmembrane helix-helix association depending on sequence context. J. Mol. Biol., 396, 452-461.
    • (2010) J. Mol. Biol. , vol.396 , pp. 452-461
    • Herrmann, J.R.1
  • 14
    • 33751342912 scopus 로고    scopus 로고
    • Self-interaction of a SNARE transmembrane domain promotes the hemifusion-to-fusion transition
    • Hofmann, M.W. et al. (2006) Self-interaction of a SNARE transmembrane domain promotes the hemifusion-to-fusion transition. J. Mol. Biol., 364, 1048-1060.
    • (2006) J. Mol. Biol. , vol.364 , pp. 1048-1060
    • Hofmann, M.W.1
  • 15
    • 0033490984 scopus 로고    scopus 로고
    • Mutations affecting transmembrane segment interactions impair adhesiveness of E-cadherin
    • Huber, O. et al. (1999) Mutations affecting transmembrane segment interactions impair adhesiveness of E-cadherin. J. Cell Sci., 112, 4415-4423.
    • (1999) J. Cell Sci. , vol.112 , pp. 4415-4423
    • Huber, O.1
  • 16
    • 34547857813 scopus 로고    scopus 로고
    • Aromatic and cation-pi interactions enhance helix-helix association in a membrane environment
    • Johnson, R.M. et al. (2007) Aromatic and cation-pi interactions enhance helix-helix association in a membrane environment. Biochemistry, 46, 9208-9214.
    • (2007) Biochemistry , vol.46 , pp. 9208-9214
    • Johnson, R.M.1
  • 17
    • 2142657817 scopus 로고    scopus 로고
    • A combined transmembrane topology and signal peptide prediction method
    • Käll, L. et al. (2004) A combined transmembrane topology and signal peptide prediction method. J. Mol. Biol., 338, 1027-1036.
    • (2004) J. Mol. Biol. , vol.338 , pp. 1027-1036
    • Käll, L.1
  • 18
    • 0030661912 scopus 로고    scopus 로고
    • Dimerization of the synaptic vesicle protein synaptobrevin (vesicle-associated membrane protein) II depends on specific residues within the transmembrane segment
    • Laage, R. and Langosch, D. (1997) Dimerization of the synaptic vesicle protein synaptobrevin (vesicle-associated membrane protein) II depends on specific residues within the transmembrane segment. Eur. J. Biochem., 249, 540-546.
    • (1997) Eur. J. Biochem. , vol.249 , pp. 540-546
    • Laage, R.1    Langosch, D.2
  • 19
    • 0034625384 scopus 로고    scopus 로고
    • A conserved membrane-spanning amino acid motif drives homomeric and supports heteromeric assembly of presynaptic SNARE proteins
    • Laage, R. et al. (2000) A conserved membrane-spanning amino acid motif drives homomeric and supports heteromeric assembly of presynaptic SNARE proteins. J. Biol. Chem., 275, 17481-17487.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17481-17487
    • Laage, R.1
  • 20
    • 0030575833 scopus 로고    scopus 로고
    • Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator
    • Langosch, D. et al. (1996) Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator. J. Mol. Biol., 263, 525-530.
    • (1996) J. Mol. Biol. , vol.263 , pp. 525-530
    • Langosch, D.1
  • 21
    • 65649127175 scopus 로고    scopus 로고
    • The structure of the integrin alphaIIbbeta3 transmembrane complex explains integrin transmembrane signalling
    • Lau, T.L. et al. (2009) The structure of the integrin alphaIIbbeta3 transmembrane complex explains integrin transmembrane signalling. EMBO J., 28, 1351-1361.
    • (2009) EMBO J. , vol.28 , pp. 1351-1361
    • Lau, T.L.1
  • 22
    • 84855465724 scopus 로고    scopus 로고
    • Transmembrane helix dimerization: Beyond the search for sequence motifs
    • Li, E. et al. (2012) Transmembrane helix dimerization: Beyond the search for sequence motifs. Biochim. Biophys. Acta, 1818, 183-193.
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 183-193
    • Li, E.1
  • 23
    • 0035940359 scopus 로고    scopus 로고
    • Oligomerization of the integrin alphaIIbbeta3: Roles of the transmembrane and cytoplasmic domains
    • Li, R. et al. (2001) Oligomerization of the integrin alphaIIbbeta3: Roles of the transmembrane and cytoplasmic domains. Proc. Natl Acad. Sci. USA, 98, 12462-12467.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 12462-12467
    • Li, R.1
  • 24
    • 0038644597 scopus 로고    scopus 로고
    • Activation of integrin alphaIIbbeta3 by modulation of transmembrane helix associations
    • Li, R. et al. (2003) Activation of integrin alphaIIbbeta3 by modulation of transmembrane helix associations. Science, 300, 795-798.
    • (2003) Science , vol.300 , pp. 795-798
    • Li, R.1
  • 25
    • 2942700100 scopus 로고    scopus 로고
    • Dimerization of the transmembrane domain of Integrin alphaIIb subunit in cell membranes
    • Li, R. et al. (2004) Dimerization of the transmembrane domain of Integrin alphaIIb subunit in cell membranes. J. Biol. Chem., 279, 26666-26673.
    • (2004) J. Biol. Chem. , vol.279 , pp. 26666-26673
    • Li, R.1
  • 26
    • 33748306120 scopus 로고    scopus 로고
    • Integrin structures and conformational signaling
    • Luo, B.H. and Springer, T.A. (2006) Integrin structures and conformational signaling. Curr. Opin. Cell Biol., 18, 579-586.
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 579-586
    • Luo, B.H.1    Springer, T.A.2
  • 27
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: Structure and implications
    • MacKenzie, K.R. et al. (1997) A transmembrane helix dimer: Structure and implications. Science, 276, 131-133.
    • (1997) Science , vol.276 , pp. 131-133
    • MacKenzie, K.R.1
  • 29
    • 0033790343 scopus 로고    scopus 로고
    • Helical membrane protein folding stability, and evolution
    • Popot, J.L. and Engelman, D.M. (2000) Helical membrane protein folding, stability, and evolution. Annu. Rev. Biochem., 69, 881-922.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 881-922
    • Popot, J.L.1    Engelman, D.M.2
  • 30
    • 38849122877 scopus 로고    scopus 로고
    • Surface recognition elements of membrane protein oligomerization
    • Rath, A. and Deber, C.M. (2008) Surface recognition elements of membrane protein oligomerization. Proteins, 70, 786-793.
    • (2008) Proteins , vol.70 , pp. 786-793
    • Rath, A.1    Deber, C.M.2
  • 31
    • 0034201441 scopus 로고    scopus 로고
    • Emboss: The European molecular biology open software suite
    • Rice, P. et al. (2000) EMBOSS: The European molecular biology open software suite. Trends Genet., 16, 276-277.
    • (2000) Trends Genet. , vol.16 , pp. 276-277
    • Rice, P.1
  • 32
    • 28444469781 scopus 로고    scopus 로고
    • Tryptophan supports interaction of transmembrane helices
    • Ridder, A. et al. (2005) Tryptophan supports interaction of transmembrane helices. J. Mol. Biol., 354, 894-902.
    • (2005) J. Mol. Biol. , vol.354 , pp. 894-902
    • Ridder, A.1
  • 33
    • 84862023866 scopus 로고    scopus 로고
    • Homotypic interaction and amino acid distribution of unilaterally conserved transmembrane helices
    • Ried, C.L. et al. (2012) Homotypic interaction and amino acid distribution of unilaterally conserved transmembrane helices. J. Mol. Biol., 420, 251-257.
    • (2012) J. Mol. Biol. , vol.420 , pp. 251-257
    • Ried, C.L.1
  • 34
    • 0032962457 scopus 로고    scopus 로고
    • Twilight zone of protein sequence alignments
    • Rost, B. (1999) Twilight zone of protein sequence alignments. Protein Eng., 12, 85-94.
    • (1999) Protein Eng. , vol.12 , pp. 85-94
    • Rost, B.1
  • 35
    • 1442349917 scopus 로고    scopus 로고
    • The composition rather than position of polar residues (QxxS) drives aspartate receptor transmembrane domain dimerization in vivo
    • Sal-Man, N. et al. (2004) The composition rather than position of polar residues (QxxS) drives aspartate receptor transmembrane domain dimerization in vivo. Biochemistry, 43, 2309-2313.
    • (2004) Biochemistry , vol.43 , pp. 2309-2313
    • Sal-Man, N.1
  • 36
    • 0029440613 scopus 로고
    • The structure ofMHC class II: A role for dimer of dimers
    • Schafer, P.H. et al. (1995) The structure ofMHC class II: A role for dimer of dimers. Semin. Immunol., 7, 389-398.
    • (1995) Semin. Immunol. , vol.7 , pp. 389-398
    • Schafer, P.H.1
  • 37
    • 1642396353 scopus 로고    scopus 로고
    • Involvement of transmembrane domain interactions in signal transduction by alpha/beta integrins
    • Schneider, D. and Engelman, D.M. (2004) Involvement of transmembrane domain interactions in signal transduction by alpha/beta integrins. J. Biol. Chem., 279, 9840-9846.
    • (2004) J. Biol. Chem. , vol.279 , pp. 9840-9846
    • Schneider, D.1    Engelman, D.M.2
  • 38
    • 4143085058 scopus 로고    scopus 로고
    • Folding of helical membrane proteins: The role of polar GxxxG-like and proline motifs
    • Senes, A. et al. (2004) Folding of helical membrane proteins: The role of polar, GxxxG-like and proline motifs. Curr. Opin. Struct. Biol., 14, 465-479.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 465-479
    • Senes, A.1
  • 39
    • 0344413478 scopus 로고    scopus 로고
    • Active and inactive orientations of the transmembrane and cytosolic domains of the erythropoietin receptor dimer
    • Seubert, N. et al. (2003) Active and inactive orientations of the transmembrane and cytosolic domains of the erythropoietin receptor dimer, Mol. cell, 12, 1239-1250.
    • (2003) Mol. cell , vol.12 , pp. 1239-1250
    • Seubert, N.1
  • 40
    • 0035811042 scopus 로고    scopus 로고
    • Structure of the transmembrane dimer interface of glycophorin A in membrane bilayers
    • Smith, S.O. et al. (2001) Structure of the transmembrane dimer interface of glycophorin A in membrane bilayers. Biochemistry, 40, 6553-6558.
    • (2001) Biochemistry , vol.40 , pp. 6553-6558
    • Smith, S.O.1
  • 41
    • 0019887799 scopus 로고
    • Identification of common molecular subsequences
    • Smith, T.F. and Waterman, M.S. (1981) Identification of common molecular subsequences. J. Mol. Biol., 147, 195-197.
    • (1981) J. Mol. Biol. , vol.147 , pp. 195-197
    • Smith, T.F.1    Waterman, M.S.2
  • 42
    • 65249144553 scopus 로고    scopus 로고
    • A scissors mechanism for stimulation of SNARE-mediated lipid mixing by cholesterol
    • Tong, J. et al. (2009) A scissors mechanism for stimulation of SNARE-mediated lipid mixing by cholesterol. Proc. Natl Acad. Sci. USA, 106, 5141-5146.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 5141-5146
    • Tong, J.1
  • 43
    • 38549097071 scopus 로고    scopus 로고
    • The universal protein resource (UniProt)
    • UniProt Consortium. (2008) The universal protein resource (UniProt). Nucleic Acids Res., 36, D190-D195.
    • (2008) Nucleic Acids Res. , vol.36
  • 44
    • 35548974250 scopus 로고    scopus 로고
    • Phenylalanine promotes interaction of transmembrane domains via GxxxG motifs
    • Unterreitmeier, S. et al. (2007) Phenylalanine promotes interaction of transmembrane domains via GxxxG motifs. J. Mol. Biol., 374, 705-718.
    • (2007) J. Mol. Biol. , vol.374 , pp. 705-718
    • Unterreitmeier, S.1
  • 45
    • 78751526817 scopus 로고    scopus 로고
    • Tests of integrin transmembrane domain homo-oligomerization during integrin ligand binding and signaling
    • Wang, W. et al. (2011) Tests of integrin transmembrane domain homo-oligomerization during integrin ligand binding and signaling. J. Biol. Chem., 286, 1860-1867.
    • (2011) J. Biol. Chem. , vol.286 , pp. 1860-1867
    • Wang, W.1
  • 46
    • 78649668571 scopus 로고    scopus 로고
    • Focus on composition and interaction potential of singlepass transmembrane domains
    • Worch, R. et al. (2010) Focus on composition and interaction potential of singlepass transmembrane domains. Proteomics, 10, 4196-4208.
    • (2010) Proteomics , vol.10 , pp. 4196-4208
    • Worch, R.1
  • 47
    • 33847233683 scopus 로고    scopus 로고
    • How important are transmembrane helices of bitopic membrane proteins?
    • Zviling, M. et al. (2007) How important are transmembrane helices of bitopic membrane proteins?. Biochim. Biophys. Acta, 1768, 387-392.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 387-392
    • Zviling, M.1


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