메뉴 건너뛰기




Volumn 24, Issue 18, 2013, Pages 2834-2848

Two tyrosine-based sorting signals in the Cx43 C-terminus cooperate to mediate gap junction endocytosis

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; AMINO ACID; CLATHRIN; COMPLEMENTARY DNA; CONNEXIN 43; EPIDERMAL GROWTH FACTOR RECEPTOR; GREEN FLUORESCENT PROTEIN; LOW DENSITY LIPOPROTEIN RECEPTOR; MEMBRANE PROTEIN; MUTANT PROTEIN; POLYPEPTIDE; PROTEIN DAB2; TYROSINE; UBIQUITIN PROTEIN LIGASE E3; UBIQUITIN PROTEIN LIGASE NEDD4; UNCLASSIFIED DRUG;

EID: 84884468083     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E13-02-0111     Document Type: Article
Times cited : (47)

References (68)
  • 2
    • 56649099046 scopus 로고    scopus 로고
    • Acute internalization of gap junctions in vascular endothelial cells in response to inflammatory mediator-induced G-protein coupled receptor activation
    • Baker SM, Kim N, Gumpert AM, Segretain D, Falk MM (2008). Acute internalization of gap junctions in vascular endothelial cells in response to inflammatory mediator-induced G-protein coupled receptor activation. FEBS Lett 582, 4039-4046.
    • (2008) FEBS Lett , vol.582 , pp. 4039-4046
    • Baker, S.M.1    Kim, N.2    Gumpert, A.M.3    Segretain, D.4    Falk, M.M.5
  • 3
    • 84861592770 scopus 로고    scopus 로고
    • Gap junctions and hemichannels in signal transmission, function and development of bone
    • Batra N, Kar R, Jiang JX (2012). Gap junctions and hemichannels in signal transmission, function and development of bone. Biochim Biophys Acta 1818, 1909-1918.
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 1909-1918
    • Batra, N.1    Kar, R.2    Jiang, J.X.3
  • 7
    • 78649490996 scopus 로고    scopus 로고
    • Trafficking and recycling of the connexin43 gap junction protein during mitosis
    • Boassa D, Solan JL, Papas A, Thornton P, Lampe PD, Sosinsky GE (2011). Trafficking and recycling of the connexin43 gap junction protein during mitosis. Traffic 11, 1471-1486.
    • (2011) Traffic , vol.11 , pp. 1471-1486
    • Boassa, D.1    Solan, J.L.2    Papas, A.3    Thornton, P.4    Lampe, P.D.5    Sosinsky, G.E.6
  • 8
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • DOI 10.1146/annurev.biochem.72.121801.161800
    • Bonifacino JS, Traub LM (2003). Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu Rev Biochem 72, 395-447. (Pubitemid 36930451)
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 9
    • 79959687376 scopus 로고    scopus 로고
    • Ubiquitin-mediated internalization of connexin43 is independent of the canonical endocytic tyrosine-sorting signal
    • Catarino S, Ramalho JS, Marques C, Pereira P, Girao H (2011). Ubiquitin-mediated internalization of connexin43 is independent of the canonical endocytic tyrosine-sorting signal. Biochem J 437, 255-267.
    • (2011) Biochem J , vol.437 , pp. 255-267
    • Catarino, S.1    Ramalho, J.S.2    Marques, C.3    Pereira, P.4    Girao, H.5
  • 10
    • 81755171483 scopus 로고    scopus 로고
    • Adaptor protein complex-2 (AP-2) and epsin-1 mediate protease-activated receptor-1 internalization via phosphorylation- and ubiquitination-dependent sorting signals
    • Chen B, Dores MR, Grimsey N, Canto I, Barker BL, Trejo J (2011). Adaptor protein complex-2 (AP-2) and epsin-1 mediate protease-activated receptor-1 internalization via phosphorylation- and ubiquitination-dependent sorting signals. J Biol Chem 286, 40760-40770.
    • (2011) J Biol Chem , vol.286 , pp. 40760-40770
    • Chen, B.1    Dores, M.R.2    Grimsey, N.3    Canto, I.4    Barker, B.L.5    Trejo, J.6
  • 11
    • 84864634144 scopus 로고    scopus 로고
    • The first five seconds in the life of a clathrin-coated pit
    • Cocucci E, Aguet F, Boulant S, Kirchhausen T (2012). The first five seconds in the life of a clathrin-coated pit. Cell 150, 495-507.
    • (2012) Cell , vol.150 , pp. 495-507
    • Cocucci, E.1    Aguet, F.2    Boulant, S.3    Kirchhausen, T.4
  • 12
    • 0037123766 scopus 로고    scopus 로고
    • Molecular architecture and functional model of the endocytic AP2 complex
    • DOI 10.1016/S0092-8674(02)00735-3
    • Collins BM, McCoy AJ, Kent HM, Evans PR, Owen DJ (2002). Molecular architecture and functional model of the endocytic AP2 complex. Cell 109, 523-535. (Pubitemid 34564478)
    • (2002) Cell , vol.109 , Issue.4 , pp. 523-535
    • Collins, B.M.1    McCoy, A.J.2    Kent, H.M.3    Evans, P.R.4    Owen, D.J.5
  • 13
    • 0034474693 scopus 로고    scopus 로고
    • Connexin-specific distribution within gap junctions revealed in living cells
    • Falk MM (2000). Connexin-specific distribution within gap junctions revealed in living cells. J Cell Sci 113, 4109-4120. (Pubitemid 32194535)
    • (2000) Journal of Cell Science , vol.113 , Issue.22 , pp. 4109-4120
    • Falk, M.M.1
  • 14
    • 67749088129 scopus 로고    scopus 로고
    • Gap junction turnover is achieved by the internalization of small endocytic double-membrane vesicles
    • Falk MM, Baker SM, Gumpert AM, Segretain D, Buckheit RWIII (2009). Gap junction turnover is achieved by the internalization of small endocytic double-membrane vesicles. Mol Biol Cell 20, 3342-3352.
    • (2009) Mol Biol Cell , vol.20 , pp. 3342-3352
    • Falk, M.M.1    Baker, S.M.2    Gumpert, A.M.3    Segretain, D.4    Buckheit III, R.W.5
  • 15
    • 84866740839 scopus 로고    scopus 로고
    • Degradation of endocytosed gap junctions by autophagosomal and endo-/lysosomal pathways: A perspective
    • Falk MM, Fong JT, Kells RM, O'Laughlin MC, Kowal TJ, Thevenin AF (2012). Degradation of endocytosed gap junctions by autophagosomal and endo-/lysosomal pathways: a perspective. J Membr Biol 245, 465-476.
    • (2012) J Membr Biol , vol.245 , pp. 465-476
    • Falk, M.M.1    Fong, J.T.2    Kells, R.M.3    O'Laughlin, M.C.4    Kowal, T.J.5    Thevenin, A.F.6
  • 16
    • 0019603292 scopus 로고
    • Five-hour half-life of mouse liver gap-junction protein
    • Fallon RF, Goodenough DA (1981). Five-hour half-life of mouse liver gap-junction protein. J Cell Biol 90, 521-526.
    • (1981) J Cell Biol , vol.90 , pp. 521-526
    • Fallon, R.F.1    Goodenough, D.A.2
  • 19
    • 84866735822 scopus 로고    scopus 로고
    • Smad ubiquitination regulatory factor-2 controls gap junction intercellular communication by modulating endocytosis and degradation of connexin43
    • Fykerud TA, Kjenseth A, Schink KO, Sirnes S, Bruun J, Omori Y, Brech A, Rivedal E, Leithe E (2012). Smad ubiquitination regulatory factor-2 controls gap junction intercellular communication by modulating endocytosis and degradation of connexin43. J Cell Sci 125, 3966-3976.
    • (2012) J Cell Sci , vol.125 , pp. 3966-3976
    • Fykerud, T.A.1    Kjenseth, A.2    Schink, K.O.3    Sirnes, S.4    Bruun, J.5    Omori, Y.6    Brech, A.7    Rivedal, E.8    Leithe, E.9
  • 21
    • 0029165125 scopus 로고
    • Preparation, characterization, and structure of half gap junctional layers split with urea and EGTA
    • Ghoshroy S, Goodenough DA, Sosinsky GE (1995). Preparation, characterization, and structure of half gap junctional layers split with urea and EGTA. J Membr Biol 146, 15-28.
    • (1995) J Membr Biol , vol.146 , pp. 15-28
    • Ghoshroy, S.1    Goodenough, D.A.2    Sosinsky, G.E.3
  • 23
    • 59349109991 scopus 로고    scopus 로고
    • Molecular reorganization of Cx43, Zo-1 and Src complexes during the endocytosis of gap junction plaques in response to a non-genomic carcinogen
    • Gilleron J, Fiorini C, Carette D, Avondet C, Falk MM, Segretain D, Pointis G (2008). Molecular reorganization of Cx43, Zo-1 and Src complexes during the endocytosis of gap junction plaques in response to a non-genomic carcinogen. J Cell Sci 121, 4069-4078.
    • (2008) J Cell Sci , vol.121 , pp. 4069-4078
    • Gilleron, J.1    Fiorini, C.2    Carette, D.3    Avondet, C.4    Falk, M.M.5    Segretain, D.6    Pointis, G.7
  • 24
    • 70449519976 scopus 로고    scopus 로고
    • Eps15 interacts with ubiquitinated Cx43 and mediates its internalization
    • Girao H, Catarino S, Pereira P (2009). Eps15 interacts with ubiquitinated Cx43 and mediates its internalization. Exp Cell Res 315, 3587-3597.
    • (2009) Exp Cell Res , vol.315 , pp. 3587-3597
    • Girao, H.1    Catarino, S.2    Pereira, P.3
  • 25
    • 0031283282 scopus 로고    scopus 로고
    • 3 connexin gene leads to proteolysis and cataractogenesis in mice
    • DOI 10.1016/S0092-8674(00)80471-7
    • Gong X, Li E, Klier G, Huang Q, Wu Y, Lei H, Kumar NM, Horwitz J, Gilula NB (1997). Disruption of ?3connexin gene leads to proteolysis and cataractogenesis in mice. Cell 91, 833-843. (Pubitemid 28007739)
    • (1997) Cell , vol.91 , Issue.6 , pp. 833-843
    • Gong, X.1    Li, E.2    Klier, G.3    Huang, Q.4    Wu, Y.5    Lei, H.6    Kumar, N.M.7    Horwitz, J.8    Gilula, N.B.9
  • 26
    • 0016194153 scopus 로고
    • The splitting of hepatocyte gap junctions and zonulae occludentes with hypertonic disaccharides
    • Goodenough DA, Gilula NB (1974). The splitting of hepatocyte gap junctions and zonulae occludentes with hypertonic disaccharides. J Cell Biol 61, 575-590.
    • (1974) J Cell Biol , vol.61 , pp. 575-590
    • Goodenough, D.A.1    Gilula, N.B.2
  • 27
    • 84884471848 scopus 로고    scopus 로고
    • Duolink- "in-cell Co-IP" for visualization of protein interactions in situ
    • Gullberg M, Goransson C, Fredriksson S (2011). Duolink-"In-cell Co-IP" for visualization of protein interactions in situ. Nat Methods 8.
    • (2011) Nat Methods , vol.8
    • Gullberg, M.1    Goransson, C.2    Fredriksson, S.3
  • 28
    • 48749126178 scopus 로고    scopus 로고
    • Double-membrane gap junction internalization requires the clathrin-mediated endocytic machinery
    • Gumpert AM, Varco JS, Baker SM, Piehl M, Falk MM (2008). Double-membrane gap junction internalization requires the clathrin-mediated endocytic machinery. FEBS Lett 582, 2887-2892.
    • (2008) FEBS Lett , vol.582 , pp. 2887-2892
    • Gumpert, A.M.1    Varco, J.S.2    Baker, S.M.3    Piehl, M.4    Falk, M.M.5
  • 29
    • 1842588906 scopus 로고    scopus 로고
    • Lipids as targeting signals: Lipid rafts and intracellular trafficking
    • DOI 10.1111/j.1600-0854.2004.0181.x
    • Helms JB, Zurzolo C (2004). Lipids as targeting signals: lipid rafts and intracellular trafficking. Traffic 5, 247-254. (Pubitemid 38455748)
    • (2004) Traffic , vol.5 , Issue.4 , pp. 247-254
    • Helms, J.B.1    Zurzolo, C.2
  • 31
    • 0023684064 scopus 로고
    • A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions
    • Higuchi R, Krummel B, Saiki RK (1988). A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions. Nucleic Acids Res 16, 7351-7367.
    • (1988) Nucleic Acids Res , vol.16 , pp. 7351-7367
    • Higuchi, R.1    Krummel, B.2    Saiki, R.K.3
  • 32
    • 28644434657 scopus 로고    scopus 로고
    • Zonula occludens-1 alters connexin43 gap junction size and organization by influencing channel accretion
    • DOI 10.1091/mbc.E05-08-0737
    • Hunter AW, Barker RJ, Zhu C, Gourdie RG (2005). Zonula occludens-1 alters connexin43 gap junction size and organization by influencing channel accretion. Mol Biol Cell 16, 5686-5698. (Pubitemid 41752218)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.12 , pp. 5686-5698
    • Hunter, A.W.1    Barker, R.J.2    Zhu, C.3    Gourdie, R.G.4
  • 33
    • 0346496133 scopus 로고    scopus 로고
    • Fusion of GFP to the carboxyl terminus of connexin43 increases gap junction size in HeLa cells
    • Hunter AW, Jourdan J, Gourdie RG (2003). Fusion of GFP to the carboxyl terminus of connexin43 increases gap junction size in HeLa cells. Cell Commun Adhes 10, 211-214. (Pubitemid 38081374)
    • (2003) Cell Communication and Adhesion , vol.10 , Issue.4-6 , pp. 211-214
    • Hunter, A.W.1    Jourdan, J.2    Gourdie, R.G.3
  • 34
    • 84875156443 scopus 로고    scopus 로고
    • Phosphorylation on serines 279 and 282 of connexin43 regulates endocytosis and gap junction assembly in pancreatic cancer cells
    • Johnson KE, Mitra S, Katoch P, Kelsey LS, Johnson KR, Mehta PP (2013). Phosphorylation on serines 279 and 282 of connexin43 regulates endocytosis and gap junction assembly in pancreatic cancer cells. Mol Biol Cell 24, 715-733.
    • (2013) Mol Biol Cell , vol.24 , pp. 715-733
    • Johnson, K.E.1    Mitra, S.2    Katoch, P.3    Kelsey, L.S.4    Johnson, K.R.5    Mehta, P.P.6
  • 35
    • 0035085580 scopus 로고    scopus 로고
    • The origin of annular junctions: A mechanism of gap junction internalization
    • Jordan K, Chodock R, Hand AR, Laird DW (2001). The origin of annular junctions: a mechanism of gap junction internalization. J Cell Sci 114, 763-773. (Pubitemid 32237149)
    • (2001) Journal of Cell Science , vol.114 , Issue.4 , pp. 763-773
    • Jordan, K.1    Chodock, R.2    Hand, A.R.3    Laird, D.W.4
  • 36
    • 0036654536 scopus 로고    scopus 로고
    • GJB2 (connexin 26) variants and nonsyndromic sensorineural hearing loss: A HuGE review
    • DOI 10.1097/00125817-200207000-00004
    • Kenneson A, Van Naarden Braun K, Boyle C (2002). GJB2 (connexin 26) variants and nonsyndromic sensorineural hearing loss: a HuGE review. Genet Med 4, 258-274. (Pubitemid 44698560)
    • (2002) Genetics in Medicine , vol.4 , Issue.4 , pp. 258-274
    • Kenneson, A.1    Van Naarden Braun, K.2    Boyle, C.3
  • 37
    • 33749455320 scopus 로고    scopus 로고
    • A single common portal for clathrin-mediated endocytosis of distinct cargo governed by cargo-selective adaptors
    • DOI 10.1091/mbc.E06-05-0421
    • Keyel PA, Mishra SK, Roth R, Heuser JE, Watkins SC, Traub LM (2006). A single common portal for clathrin-mediated endocytosis of distinct cargo governed by cargo-selective adaptors. Mol Biol Cell 17, 4300-4317. (Pubitemid 44522050)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.10 , pp. 4300-4317
    • Keyel, P.A.1    Mishra, S.K.2    Roth, R.3    Heuser, J.E.4    Watkins, S.C.5    Traub, L.M.6
  • 38
    • 0018570734 scopus 로고
    • Evidence for the participation of actin microfilaments and bristle coats in the internalization of gap junction membrane
    • DOI 10.1083/jcb.83.3.576
    • Larsen WJ, Tung HN, Murray SA, Swenson CA (1979). Evidence for the participation of actin microfilaments and bristle coats in the internalization of gap junction membrane. J Cell Biol 83, 576-587. (Pubitemid 10178662)
    • (1979) Journal of Cell Biology , vol.83 , Issue.3 , pp. 576-587
    • Larsen, W.J.1    Tung, H.2    Murray, S.A.3    Swenson, C.A.4
  • 39
    • 0036677449 scopus 로고    scopus 로고
    • Dynamic trafficking and delivery of connexons to the plasma membrane and accretion to gap junctions in living cells
    • Lauf U, Giepmans BN, Lopez P, Braconnot S, Chen SC, Falk MM (2002). Dynamic trafficking and delivery of connexons to the plasma membrane and accretion to gap junctions in living cells. Proc Natl Acad Sci USA 99, 10446-10451.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 10446-10451
    • Lauf, U.1    Giepmans, B.N.2    Lopez, P.3    Braconnot, S.4    Chen, S.C.5    Falk, M.M.6
  • 41
    • 70450277811 scopus 로고    scopus 로고
    • Ubiquitylation of the gap junction protein connexin-43 signals its trafficking from early endosomes to lysosomes in a process mediated by Hrs and Tsg101
    • Leithe E, Kjenseth A, Sirnes S, Stenmark H, Brech A, Rivedal E (2009). Ubiquitylation of the gap junction protein connexin-43 signals its trafficking from early endosomes to lysosomes in a process mediated by Hrs and Tsg101. J Cell Sci 122, 3883-3893.
    • (2009) J Cell Sci , vol.122 , pp. 3883-3893
    • Leithe, E.1    Kjenseth, A.2    Sirnes, S.3    Stenmark, H.4    Brech, A.5    Rivedal, E.6
  • 42
    • 33749386740 scopus 로고    scopus 로고
    • Ubiquitin protein ligase Nedd4 binds to connexin43 by a phosphorylation-modulated process
    • DOI 10.1242/jcs.03149
    • Leykauf K, Salek M, Bomke J, Frech M, Lehmann WD, Durst M, Alonso A (2006). Ubiquitin protein ligase Nedd4 binds to connexin43 by a phosphorylation-modulated process. J Cell Sci 119, 3634-3642. (Pubitemid 44501867)
    • (2006) Journal of Cell Science , vol.119 , Issue.17 , pp. 3634-3642
    • Leykauf, K.1    Salek, M.2    Bomke, J.3    Frech, M.4    Lehmann, W.-D.5    Durst, M.6    Alonso, A.7
  • 44
    • 0344420042 scopus 로고    scopus 로고
    • Protein Kinase Cγ Regulation of Gap Junction Activity through Caveolin-1-Containing Lipid Rafts
    • DOI 10.1167/iovs.03-0296
    • Lin D, Zhou J, Zelenka PS, Takemoto DJ (2003). Protein kinase C? regulation of gap junction activity through caveolin-1-containing lipid rafts. Invest Ophthalmol Vis Sci 44, 5259-5268. (Pubitemid 37475397)
    • (2003) Investigative Ophthalmology and Visual Science , vol.44 , Issue.12 , pp. 5259-5268
    • Lin, D.1    Zhou, J.2    Zelenka, P.S.3    Takemoto, D.J.4
  • 46
    • 33947314576 scopus 로고    scopus 로고
    • Regulation of receptor trafficking by GRKs and arrestins
    • DOI 10.1146/annurev.physiol.69.022405.154712
    • Moore CA, Milano SK, Benovic JL (2007). Regulation of receptor trafficking by GRKs and arrestins. Annu Rev Physiol 69, 451-482. (Pubitemid 46457651)
    • (2007) Annual Review of Physiology , vol.69 , pp. 451-482
    • Moore, C.A.C.1    Milano, S.K.2    Benovic, J.L.3
  • 48
    • 0035099375 scopus 로고    scopus 로고
    • Disabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts with AP-2
    • DOI 10.1034/j.1600-0854.2001.020206.x
    • Morris SM, Cooper JA (2001). Disabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts with AP-2. Traffic 2, 111-123. (Pubitemid 32219864)
    • (2001) Traffic , vol.2 , Issue.2 , pp. 111-123
    • Morris, S.M.1    Cooper, J.A.2
  • 52
    • 35848947024 scopus 로고    scopus 로고
    • Clathrin: An amazing multifunctional dreamcoat
    • Pauly BS, Drubin DG (2007). Clathrin: an amazing multifunctional dreamcoat. Cell Host Microbe 2, 288-290.
    • (2007) Cell Host Microbe , vol.2 , pp. 288-290
    • Pauly, B.S.1    Drubin, D.G.2
  • 53
    • 33846817049 scopus 로고    scopus 로고
    • Internalization of large double-membrane intercellular vesicles by a clathrin-dependent endocytic process
    • DOI 10.1091/mbc.E06-06-0487
    • Piehl M, Lehmann C, Gumpert A, Denizot JP, Segretain D, Falk MM (2007). Internalization of large double-membrane intercellular vesicles by a clathrin-dependent endocytic process. Mol Biol Cell 18, 337-347. (Pubitemid 46213205)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.2 , pp. 337-347
    • Piehl, M.1    Lehmann, C.2    Gumpert, A.3    Denizot, J.-P.4    Segretain, D.5    Falk, M.M.6
  • 55
    • 79955501784 scopus 로고    scopus 로고
    • Connexin43 connexon to gap junction transition is regulated by zonula occludens-1
    • Rhett JM, Jourdan J, Gourdie RG (2011). Connexin43 connexon to gap junction transition is regulated by zonula occludens-1. Mol Biol Cell 22, 1516-1528.
    • (2011) Mol Biol Cell , vol.22 , pp. 1516-1528
    • Rhett, J.M.1    Jourdan, J.2    Gourdie, R.G.3
  • 56
    • 0037035519 scopus 로고    scopus 로고
    • Connexin family members target to lipid raft domains and interact with caveolin-1
    • DOI 10.1021/bi0121656
    • Schubert AL, Schubert W, Spray DC, Lisanti MP (2002). Connexin family members target to lipid raft domains and interact with caveolin-1. Biochemistry 41, 5754-5764. (Pubitemid 34462696)
    • (2002) Biochemistry , vol.41 , Issue.18 , pp. 5754-5764
    • Schubert, A.-L.1    Schubert, W.2    Spray, D.C.3    Lisanti, M.P.4
  • 58
    • 20444411484 scopus 로고    scopus 로고
    • Connexin phosphorylation as a regulatory event linked to gap junction channel assembly
    • DOI 10.1016/j.bbamem.2004.09.013, PII S0005273604002445
    • Solan JL, Lampe PD (2005). Connexin phosphorylation as a regulatory event linked to gap junction channel assembly. Biochim Biophys Acta 1711, 154-163. (Pubitemid 40799290)
    • (2005) Biochimica et Biophysica Acta - Biomembranes , vol.1711 , Issue.2 , pp. 154-163
    • Solan, J.L.1    Lampe, P.D.2
  • 59
    • 48449089173 scopus 로고    scopus 로고
    • Connexin 43 in LA-25 cells with active v-src is phosphorylated on Y247, Y265, S262, S279/282, and S368 via multiple signaling pathways
    • Solan JL, Lampe PD (2008). Connexin 43 in LA-25 cells with active v-src is phosphorylated on Y247, Y265, S262, S279/282, and S368 via multiple signaling pathways. Cell Commun Adhes 15, 75-84.
    • (2008) Cell Commun Adhes , vol.15 , pp. 75-84
    • Solan, J.L.1    Lampe, P.D.2
  • 61
    • 0037672616 scopus 로고    scopus 로고
    • A tyrosine-based sorting signal is involved in connexin43 stability and gap junction turnover
    • DOI 10.1242/jcs.00440
    • Thomas MA, Zosso N, Scerri I, Demaurex N, Chanson M, Staub O (2003). A tyrosine-based sorting signal is involved in connexin43 stability and gap junction turnover. J Cell Sci 116, 2213-2222. (Pubitemid 36722368)
    • (2003) Journal of Cell Science , vol.116 , Issue.11 , pp. 2213-2222
    • Thomas, M.A.1    Zosso, N.2    Scerri, I.3    Demaurex, N.4    Chanson, M.5    Staub, O.6
  • 62
    • 0242330147 scopus 로고    scopus 로고
    • Sorting it out: AP-2 and alternate clathrin adaptors in endocytic cargo selection
    • DOI 10.1083/jcb.200309175
    • Traub LM (2003). Sorting it out: AP-2 and alternate clathrin adaptors in endocytic cargo selection. J Cell Biol 163, 203-208. (Pubitemid 37363120)
    • (2003) Journal of Cell Biology , vol.163 , Issue.2 , pp. 203-208
    • Traub, L.M.1
  • 63
    • 20544465126 scopus 로고    scopus 로고
    • Common principles in clathrin-mediated sorting at the Golgi and the plasma membrane
    • DOI 10.1016/j.bbamcr.2005.04.005, PII S0167488905000765
    • Traub LM (2005). Common principles in clathrin-mediated sorting at the Golgi and the plasma membrane. Biochim Biophys Acta 1744, 415-437. (Pubitemid 40848259)
    • (2005) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1744 , Issue.3 , pp. 415-437
    • Traub, L.M.1
  • 65
    • 0032476578 scopus 로고    scopus 로고
    • Targeted ablation of connexin50 in mice results in microphthalmia and zonular pulverulent cataracts
    • DOI 10.1083/jcb.143.3.815
    • White TW, Goodenough DA, Paul DL (1998). Targeted ablation of connexin50 in mice results in microphthalmia and zonular pulverulent cataracts. J Cell Biol 143, 815-825. (Pubitemid 28512573)
    • (1998) Journal of Cell Biology , vol.143 , Issue.3 , pp. 815-825
    • White, T.W.1    Goodenough, D.A.2    Paul, D.L.3
  • 66
    • 34247383616 scopus 로고    scopus 로고
    • Clathrin-dependent mechanisms of G protein-coupled receptor endocytosis
    • DOI 10.1111/j.1600-0854.2007.00551.x
    • Wolfe BL, Trejo J (2007). Clathrin-dependent mechanisms of G protein-coupled receptor endocytosis. Traffic 8, 462-470. (Pubitemid 46638559)
    • (2007) Traffic , vol.8 , Issue.5 , pp. 462-470
    • Wolfe, B.L.1    Trejo, J.2
  • 67
    • 84870064725 scopus 로고    scopus 로고
    • The role of connexins in ear and skin physiology-functional insights from disease-associated mutations
    • Xu J, Nicholson BJ (2013). The role of connexins in ear and skin physiology-functional insights from disease-associated mutations. Biochim Biophys Acta 1828, 167-178.
    • (2013) Biochim Biophys Acta , vol.1828 , pp. 167-178
    • Xu, J.1    Nicholson, B.J.2
  • 68
    • 0036231656 scopus 로고    scopus 로고
    • The size of lipid rafts: An atomic force microscopy study of ganglioside GM1 domains in sphingomyelin/DOPC/cholesterol membranes
    • Yuan C, Furlong J, Burgos P, Johnston LJ (2002). The size of lipid rafts: an atomic force microscopy study of ganglioside GM1 domains in sphingomyelin/DOPC/cholesterol membranes. Biophys J 82, 2526-2535. (Pubitemid 34441292)
    • (2002) Biophysical Journal , vol.82 , Issue.5 , pp. 2526-2535
    • Yuan, C.1    Furlong, J.2    Burgos, P.3    Johnston, L.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.