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Volumn 20, Issue 20, 2009, Pages 4313-4323

Glycosylation regulates pannexin intermixing and cellular localization

Author keywords

[No Author keywords available]

Indexed keywords

DYE; GLYCOPROTEIN; PROTEIN PANX1; PROTEIN PANX2; PROTEIN PANX3; UNCLASSIFIED DRUG;

EID: 70350112277     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E09-01-0067     Document Type: Article
Times cited : (160)

References (37)
  • 1
    • 4143127920 scopus 로고    scopus 로고
    • Pannexin membrane channels are mechanosensitive conduits for ATP
    • DOI 10.1016/j.febslet.2004.07.009, PII S001457930400866X
    • Bao, L., Locovei, S., and Dahl, G. (2004). Pannexin membrane channels are mechanosensitive conduits for ATP. FEBS Lett. 572, 65-68. (Pubitemid 39092514)
    • (2004) FEBS Letters , vol.572 , Issue.1-3 , pp. 65-68
    • Bao, L.1    Locovei, S.2    Dahl, G.3
  • 3
    • 2942564430 scopus 로고    scopus 로고
    • Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence
    • DOI 10.1002/pmic.200300771
    • Blom, N., Sicheritz-Ponten, T., Gupta, R., Gammeltoft, S., and Brunak, S. (2004). Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence. Proteomics 4, 1633-1649. (Pubitemid 38738322)
    • (2004) Proteomics , vol.4 , Issue.6 , pp. 1633-1649
    • Blom, N.1    Sicheritz-Ponten, T.2    Gupta, R.3    Gammeltoft, S.4    Brunak, So.5
  • 4
    • 35748965595 scopus 로고    scopus 로고
    • Pannexin1 channels contain a glycosylation site that targets the hexamer to the plasma membrane
    • Boassa, D., Ambrosi, C., Qiu, F., Dahl, G., Gaietta, G., and Sosinsky, G. (2007). Pannexin1 channels contain a glycosylation site that targets the hexamer to the plasma membrane. J. Biol. Chem. 282, 31733-31743.
    • (2007) J. Biol. Chem. , vol.282 , pp. 31733-31743
    • Boassa, D.1    Ambrosi, C.2    Qiu, F.3    Dahl, G.4    Gaietta, G.5    Sosinsky, G.6
  • 5
    • 42649085323 scopus 로고    scopus 로고
    • Trafficking dynamics of glycosylated Pannexin1 proteins
    • Boassa, D., Qiu, F., Dahl, G., and Sosinsky, G. (2008). Trafficking dynamics of glycosylated Pannexin1 proteins. Cell. Commun. Adhes. 15, 119-132.
    • (2008) Cell. Commun. Adhes. , vol.15 , pp. 119-132
    • Boassa, D.1    Qiu, F.2    Dahl, G.3    Sosinsky, G.4
  • 6
    • 14844334146 scopus 로고    scopus 로고
    • Pharmacological properties of homomeric and heteromeric pannexin hemichannels expressed in Xenopus oocytes
    • DOI 10.1111/j.1471-4159.2004.02947.x
    • Bruzzone, R., Barbe, M. T., Jakob, N. J., and Monver, H. (2005). Pharmacological properties of homomeric and heteromeric pannexin hemichannels expressed in Xenopus oocytes. J. Neurochem. 92, 1033-1043. (Pubitemid 40344294)
    • (2005) Journal of Neurochemistry , vol.92 , Issue.5 , pp. 1033-1043
    • Bruzzone, R.1    Barbe, M.T.2    Jakob, N.J.3    Monyer, H.4
  • 7
    • 33748936354 scopus 로고    scopus 로고
    • Structure and function of gap junctions in the developing brain
    • DOI 10.1007/s00441-006-0287-0
    • Bruzzone, R., and Dermietzel, R. (2006). Structure and function of gap junctions in the developing brain. Cell Tissue Res. 26, 239-248. (Pubitemid 44435805)
    • (2006) Cell and Tissue Research , vol.326 , Issue.2 , pp. 239-248
    • Bruzzone, R.1    Dermietzel, R.2
  • 9
    • 0028568176 scopus 로고
    • TopPred II: An improved software for membrane protein structure predictions
    • Claros, M. G., and Heijne, G. V. (1994). TopPred II: an improved software for membrane protein structure predictions. CABIOS 10, 685-686.
    • (1994) CABIOS , vol.10 , pp. 685-686
    • Claros, M.G.1    Heijne, G.V.2
  • 12
    • 34249082403 scopus 로고    scopus 로고
    • Connexin channel permeability to cytoplasmic molecules
    • Harris, A. L. (2007). Connexin channel permeability to cytoplasmic molecules. Prog. Biophys. Mol. Biol. 94, 120-143.
    • (2007) Prog. Biophys. Mol. Biol. , vol.94 , pp. 120-143
    • Harris, A.L.1
  • 13
    • 33751572168 scopus 로고    scopus 로고
    • Pannexin1 is expressed by neurons and glia but does not form functional gap junctions
    • DOI 10.1002/glia.20435
    • Huang, Y., Grinspan, J. B., Abrams, C. K., and Scherer, S. S. (2007a). Pannexin1 is expressed by neurons and glia but does not form functional gap junctions. Glia 55, 46-56. (Pubitemid 44845508)
    • (2007) GLIA , vol.55 , Issue.1 , pp. 46-56
    • Huang, Y.1    Grinspan, J.B.2    Abrams, C.K.3    Scherer, S.S.4
  • 15
    • 33644826498 scopus 로고    scopus 로고
    • Pathways and control of connexin oligomerization
    • Koval, M. (2006). Pathways and control of connexin oligomerization. Trends Cell Biol. 16, 159-166.
    • (2006) Trends Cell Biol. , vol.16 , pp. 159-166
    • Koval, M.1
  • 16
    • 41649104490 scopus 로고    scopus 로고
    • Caveolin-1 and -2 interact with connexin43 and regulate gap junctional intercellular communication in keratinocytes
    • Langlois, S., Cowan, K. N., Shao, Q., Cowan, B. J., and Laird, D. W. (2008). Caveolin-1 and -2 interact with connexin43 and regulate gap junctional intercellular communication in keratinocytes. Mol. Biol. Cell 19, 912-928.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 912-928
    • Langlois, S.1    Cowan, K.N.2    Shao, Q.3    Cowan, B.J.4    Laird, D.W.5
  • 17
    • 33646748700 scopus 로고    scopus 로고
    • Pannexin 1 in erythrocytes: Function without a gap
    • Locovei, S., Bao, L., and Dahl, G. (2006). Pannexin 1 in erythrocytes: function without a gap. Proc. Natl. Acad. Sci. USA 103, 7655-7659.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7655-7659
    • Locovei, S.1    Bao, L.2    Dahl, G.3
  • 18
    • 59649088329 scopus 로고    scopus 로고
    • Pharmacological characterization of pannexin-1 currents expressed in mammalian cells
    • Ma, W., Hui, H., Pelegrin, P., and Surprenant, A. (2008). Pharmacological characterization of pannexin-1 currents expressed in mammalian cells. J. Pharmacol. Exp. Ther. 328, 409-418.
    • (2008) J. Pharmacol. Exp. Ther. , vol.328 , pp. 409-418
    • Ma, W.1    Hui, H.2    Pelegrin, P.3    Surprenant, A.4
  • 20
    • 33750473352 scopus 로고    scopus 로고
    • 7 receptor
    • DOI 10.1038/sj.emboj.7601378, PII 7601378
    • Pelegrin, P., and Surprenant, A. (2006). Pannexin-1 mediates large pore formation and interleukin-1beta release by the ATP-gated P2X7 receptor. EMBO J. 25, 5071-5082. (Pubitemid 44658525)
    • (2006) EMBO Journal , vol.25 , Issue.21 , pp. 5071-5082
    • Pelegrin, P.1    Surprenant, A.2
  • 21
    • 34047270416 scopus 로고    scopus 로고
    • Pannexin-1 couples to maitotoxin- and nigericin-induced interleukin-1beta release through a dye uptake-independent pathway
    • Pelegrin, P., and Surprenant, A. (2007). Pannexin-1 couples to maitotoxin- and nigericin-induced interleukin-1beta release through a dye uptake-independent pathway. J. Biol. Chem. 282, 2386-2394.
    • (2007) J. Biol. Chem. , vol.282 , pp. 2386-2394
    • Pelegrin, P.1    Surprenant, A.2
  • 22
    • 36549084087 scopus 로고    scopus 로고
    • Pannexin 1 and pannexin 3 are glycoproteins that exhibit many distinct characteristics from the connexin family of gap junction proteins
    • DOI 10.1242/jcs.009514
    • Penuela, S., Bhalla, R., Gong, X.-Q., Cowan, K. N., Celetti, S. J., Cowan, B. J., Bai, D., Shao, Q., and Laird, D. W. (2007). Pannexin 1 and pannexin 3 are glycoproteins that exhibit many distinct characteristics from the connexin family of gap junction proteins. J. Cell Sci. 120, 3772-3783. (Pubitemid 350187359)
    • (2007) Journal of Cell Science , vol.120 , Issue.21 , pp. 3772-3783
    • Penuela, S.1    Bhalla, R.2    Gong, X.-Q.3    Cowan, K.N.4    Celetti, S.J.5    Cowan, B.J.6    Bai, D.7    Shao, Q.8    Laird, D.W.9
  • 23
    • 48449084041 scopus 로고    scopus 로고
    • Diverse subcellular distribution profiles of pannexin1 and pannexin3
    • Penuela, S., Celetti, S. J., Bhalla, R., Shao, Q., and Laird, D. W. (2008). Diverse subcellular distribution profiles of pannexin1 and pannexin3. Cell. Commun. Adhes. 15, 133-142.
    • (2008) Cell. Commun. Adhes. , vol.15 , pp. 133-142
    • Penuela, S.1    Celetti, S.J.2    Bhalla, R.3    Shao, Q.4    Laird, D.W.5
  • 26
    • 33749003106 scopus 로고    scopus 로고
    • Pannexin expression in the cerebellum
    • Ray, A., Zoidl, G., Wahle, P., and Dermietzel, R. (2006). Pannexin expression in the cerebellum. Cerebellum 5, 189-192.
    • (2006) Cerebellum , vol.5 , pp. 189-192
    • Ray, A.1    Zoidl, G.2    Wahle, P.3    Dermietzel, R.4
  • 27
    • 21844440311 scopus 로고    scopus 로고
    • Site-specific and developmental expression of pannexin1 in the mouse nervous system
    • Ray, A., Zoidl, G., Weickert, S., Wahle, P., and Dermietzel, R. (2005). Site-specific and developmental expression of pannexin1 in the mouse nervous system. Eur. J. Neurosci. 21, 3277-3290.
    • (2005) Eur. J. Neurosci. , vol.21 , pp. 3277-3290
    • Ray, A.1    Zoidl, G.2    Weickert, S.3    Wahle, P.4    Dermietzel, R.5
  • 29
    • 20444411484 scopus 로고    scopus 로고
    • Connexin phosphorylation as a regulatory event linked to gap junction channel assembly
    • Solan, J. L., and Lampe, P. D. (2005). Connexin phosphorylation as a regulatory event linked to gap junction channel assembly. Biochim. Biophys. Acta 1711, 154-163.
    • (2005) Biochim. Biophys. Acta , vol.1711 , pp. 154-163
    • Solan, J.L.1    Lampe, P.D.2
  • 30
    • 52649150872 scopus 로고    scopus 로고
    • Pannexins are new molecular candidates for assembling gap junctions in the cochlea
    • Tang, W., Ahmad, S., Shestopalov, V. I., and Lin, X. (2008). Pannexins are new molecular candidates for assembling gap junctions in the cochlea. Neuroreport 19, 1253-1257.
    • (2008) Neuroreport , vol.19 , pp. 1253-1257
    • Tang, W.1    Ahmad, S.2    Shestopalov, V.I.3    Lin, X.4
  • 31
    • 0023161248 scopus 로고
    • Peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase and endo-beta-N-acetylglucosaminidase from Flavobacterium meningosepticum
    • Tarentino, A. L., and Plummer, T.H.J. (1987). Peptide-N4-(N-acetyl-beta- glucosaminyl) asparagine amidase and endo-beta-N-acetylglucosaminidase from Flavobacterium meningosepticum. Methods Enzymol. 138, 770-778.
    • (1987) Methods Enzymol. , vol.138 , pp. 770-778
    • Tarentino, A.L.1    Plummer, T.H.J.2
  • 32
    • 0032964297 scopus 로고    scopus 로고
    • Blast 2 sequences - a new tool for comparing protein and nucleotide sequences
    • Tatusova, T. A., and Madden, T. L. (1999). Blast 2 sequences - a new tool for comparing protein and nucleotide sequences. FEMS Microbiol. Lett. 174, 247-250.
    • (1999) FEMS Microbiol. Lett. , vol.174 , pp. 247-250
    • Tatusova, T.A.1    Madden, T.L.2
  • 34
    • 33646584876 scopus 로고    scopus 로고
    • Ischemia opens neuronal gap junction hemichannels
    • DOI 10.1126/science.1126241
    • Thompson, R. J., Zhou, N., and MacVicar, B. A. (2006). Ischemia opens neuronal gap junction hemichannels. Science 312, 924-927. (Pubitemid 43727327)
    • (2006) Science , vol.312 , Issue.5775 , pp. 924-927
    • Thompson, R.J.1    Zhou, N.2    MacVicar, B.A.3
  • 35
    • 27644494198 scopus 로고    scopus 로고
    • Pannexin1 and pannexin2 expression in the developing and mature rat brain
    • Vogt, A., Hormuzdi, S. G., and Monyer, H. (2005). Pannexin1 and pannexin2 expression in the developing and mature rat brain. Mol. Brain Res. 141, 113-120.
    • (2005) Mol. Brain Res. , vol.141 , pp. 113-120
    • Vogt, A.1    Hormuzdi, S.G.2    Monyer, H.3


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