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Original

Projection Structure of a N-Terminal Deletion Mutant of Connexin 26 Channel with Decreased Central Pore Density

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Pages 85-93 | Received 15 Oct 2007, Accepted 04 Jan 2008, Published online: 11 Jul 2009

REFERENCES

  • Beahm D L, Oshima A, Gaietta G M, Hand G M, Smock A E, Zucker S N, Toloue M M, Chandrasekhar A, Nicholson B J, Sosinsky G E. Mutation of a conserved threonine in the third transmembrane helix of α-and β-connexins creates a dominant-negative closed gap junction channel. J Biol Chem 2006; 281: 7994–8009
  • Buehler L K, Stauffer K A, Gilula N B, Kumar N M. Single channel behavior of recombinant β2 gap junction connexons reconstituted into planar lipid bilayers. Biophys J 1995; 68: 1767–1775
  • Cheng A, Schweissinger D, Dawood F, Kumar N, Yeager M. Projection structure of full length connexin 43 by electron cryo-crystallography. Cell Commun Adhes 2003; 10: 187–191
  • The CCP4 suite: Programs for protein crystallography. Acta Crys 1994; D50: 760–763, Collaborative Computational Project, Number 4
  • Crowther R A, Henderson R, Smith J M. MRC image processing programs. J Struct Biol 1996; 116: 9–16
  • Delmar M, Coombs W, Sorgen P, Duffy H S, Taffet S M. Structural bases for the chemical regulation of Connexin43 channels. Cardiovasc Res 2004; 62: 268–275
  • Fleishman S J, Unger V M, Yeager M, Ben-Tal N. A Cα model for the transmembrane α helices of gap junction intercellular channels. Mol Cell 2004; 15: 879–888
  • Fujiyoshi Y, Mizusaki T, Morikawa K, Yamagishi H, Aoki Y, Kihara H, Harada Y. Development of a superfluid helium stage for high-resolution electron microscopy. Ultramicroscopy 1991; 38: 241–251
  • Harris A L. Emerging issues of connexin channels: Biophysics fills the gap. Q Rev Biophys 2001; 34: 325–472
  • Hwa H L, Ko T M, Hsu C J, Huang C H, Chiang Y L, Oong J L, Chen C C, Hsu C K. Mutation spectrum of the connexin 26 (GJB2) gene in Taiwanese patients with prelingual deafness. Genet Med 2003; 5: 161–165
  • Kenna M A, Wu B L, Cotanche D A, Korf B R, Rehm H L. Connexin 26 studies in patients with sensorineural hearing loss. Arch Otolaryngol Head Neck Surg 2001; 127: 1037–1042
  • Kistler J, Bond J, Donaldson P, Engel A. Two distinct levels of gap junction assembly in vitro. J Struct Biol 1993; 110: 28–38
  • Kistler J, Goldie K, Donaldson P, Engel A. Reconstitution of native-type noncrystalline lens fiber gap junctions from isolated hemichannels. J Cell Biol 1994; 126: 1047–1058
  • Kyle J W, Haemmerling B, Budzik J, Lopez-Domowicz D, Berthoud V M, Hanck D A, Beyer E C. A full length N-terminus is required for connexin37 channel function but not gap junction plaque formation. Biophys J 2007; 444a, Abstract Issue
  • Matthews B W. Solvent content of protein crystals. J Mol Biol 1968; 33: 491–497
  • Mese G, Londin E, Mui R, Brink P R, White T W. Altered gating properties of functional Cx26 mutants associated with recessive non-syndromic hearing loss. Hum Genet 2004; 115: 191–199
  • Oh S, Rubin J B, Bennett M V, Verselis V K, Bargiello T A. Molecular determinants of electrical rectification of single channel conductance in gap junctions formed by connexins 26 and 32. J Gen Physiol 1999; 114: 339–364
  • Oh S, Abrams C K, Verselis V K, Bargiello T A. Stoichiometry of transjunctional voltage-gating polarity reversal by a negative charge substitution in the amino terminus of a connexin32 chimera. J Gen Physiol 2000; 116: 13–31
  • Oh S, Rivkin S, Tang Q, Verselis V K, Bargiello T A. Determinants of gating polarity of a connexin 32 hemichannel. Biophys J 2004; 87: 912–928
  • Oshima A, Doi T, Mitsuoka K, Maeda S, Fujiyoshi Y. Roles of Met-34, Cys-64, and Arg-75 in the assembly of human connexin 26. Implication for key amino acid residues for channel formation and function. J Biol Chem 2003; 278: 1807–1816
  • Oshima A, Tani K, Hiroaki Y, Fujiyoshi Y, Sosinsky G E. Three-dimensional structure of a human connexin26 gap junction channel reveals a plug in the vestibule. Proc Natl Acad Sci U S A 2007; 104: 10034–10039
  • Purnick P E, Benjamin D C, Verselis V K, Bargiello T A, Dowd T L. Structure of the amino terminus of a gap junction protein. Arch Biochem Biophys 2000a; 381: 181–190
  • Purnick P E, Oh S, Abrams C K, Verselis V K, Bargiello T A. Reversal of the gating polarity of gap junctions by negative charge substitutions in the N-terminus of connexin 32. Biophys J 2000b; 79: 2403–2415
  • Sosinsky G E, Nicholson B J. Structural organization of gap junction channels. Biochim Biophys Acta 2005; 1711: 99–125
  • Stauffer K A, Kumar N M, Gilula N B, Unwin N. Isolation and purification of gap junction channels. J Cell Biol 1991; 115: 141–150
  • Stauffer K A. The gap junction proteins β1-connexin (connexin-32) and β2-connexin (connexin-26) can form heteromeric hemichannels. J Biol Chem 1995; 270: 6768–6772
  • Unger V M, Kumar N M, Gilula N B, Yeager M. Projection structure of a gap junction membrane channel at 7 Å resolution. Nat Struct Biol 1997; 4: 39–43
  • Unger V M, Kumar N M, Gilula N B, Yeager M. Three-dimensional structure of a recombinant gap junction membrane channel. Science 1999; 283: 1176–1180
  • Unwin P NT, Ennis P D. Two configurations of a channel-forming membrane protein. Nature 1984; 307: 609–613
  • Unwin P NT, Zampighi G. Structure of the junction between communicating cells. Nature 1980; 283: 545–549
  • Verselis V K, Ginter C S, Bargiello T A. Opposite voltage gating polarities of two closely related connexins. Nature 1994; 368: 348–351

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