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Volumn 288, Issue 13, 2013, Pages 9189-9199

Role of C-terminal Membrane-proximal basic residues in cell surface trafficking of HIV coreceptor GPR15 protein

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; CYTOLOGY;

EID: 84876000606     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.445817     Document Type: Article
Times cited : (9)

References (37)
  • 1
    • 68749105852 scopus 로고    scopus 로고
    • Enhancement of the surface expression of G protein-coupled receptors
    • Dunham, J. H., and Hall, R. A. (2009) Enhancement of the surface expression of G protein-coupled receptors. Trends Biotechnol. 27, 541-545
    • (2009) Trends Biotechnol. , vol.27 , pp. 541-545
    • Dunham, J.H.1    Hall, R.A.2
  • 2
    • 33748751670 scopus 로고    scopus 로고
    • Trafficking of G protein-coupled receptors
    • Drake, M. T., Shenoy, S. K., and Lefkowitz, R. J. (2006) Trafficking of G protein-coupled receptors. Circ. Res. 99, 570-582
    • (2006) Circ. Res. , vol.99 , pp. 570-582
    • Drake, M.T.1    Shenoy, S.K.2    Lefkowitz, R.J.3
  • 3
    • 34247383616 scopus 로고    scopus 로고
    • Clathrin-dependent mechanisms of G protein-coupled receptor endocytosis
    • Wolfe, B. L., and Trejo, J. (2007) Clathrin-dependent mechanisms of G protein-coupled receptor endocytosis. Traffic 8, 462-470
    • (2007) Traffic , vol.8 , pp. 462-470
    • Wolfe, B.L.1    Trejo, J.2
  • 4
    • 39149104024 scopus 로고    scopus 로고
    • GPCR monomers and oligomers. It takes all kinds
    • Gurevich, V. V., and Gurevich, E. V. (2008) GPCR monomers and oligomers. It takes all kinds. Trends Neurosci. 31, 74-81
    • (2008) Trends Neurosci. , Issue.31 , pp. 74-81
    • Gurevich, V.V.1    Gurevich, E.V.2
  • 5
    • 41149090339 scopus 로고    scopus 로고
    • Regulation of GPCRs by endocytic membrane trafficking and its potential implications
    • Hanyaloglu, A. C., and von Zastrow, M. (2008) Regulation of GPCRs by endocytic membrane trafficking and its potential implications. Annu. Rev. Pharmacol. Toxicol. 48, 537-568
    • (2008) Annu. Rev. Pharmacol. Toxicol. , vol.48 , pp. 537-568
    • Hanyaloglu, A.C.1    Von Zastrow, M.2
  • 6
    • 0032516855 scopus 로고    scopus 로고
    • COPII and selective export from the endoplasmic reticulum
    • Barlowe, C. (1998) COPII and selective export from the endoplasmic reticulum. Biochim. Biophys. Acta 1404, 67-76
    • (1998) Biochim. Biophys. Acta , vol.1404 , pp. 67-76
    • Barlowe, C.1
  • 7
    • 0035339285 scopus 로고    scopus 로고
    • ER export. More than one way out
    • Glick, B. S. (2001) ER export. More than one way out. Curr. Biol. 11, R361-363
    • (2001) Curr. Biol. , vol.11
    • Glick, B.S.1
  • 8
    • 0442292206 scopus 로고    scopus 로고
    • Biogenesis of ER-to-Golgi transport carriers. Complex roles of COPII in ER export
    • Palmer, K. J., and Stephens, D. J. (2004) Biogenesis of ER-to-Golgi transport carriers. Complex roles of COPII in ER export. Trends Cell Biol. 14, 57-61
    • (2004) Trends Cell Biol. , vol.14 , pp. 57-61
    • Palmer, K.J.1    Stephens, D.J.2
  • 10
    • 0037683407 scopus 로고    scopus 로고
    • Signals for COPII-dependent export from the ER. What's the ticket out?
    • Barlowe, C. (2003) Signals for COPII-dependent export from the ER. What's the ticket out? Trends Cell Biol. 13, 295-300
    • (2003) Trends Cell Biol. , vol.13 , pp. 295-300
    • Barlowe, C.1
  • 11
    • 0035955633 scopus 로고    scopus 로고
    • A membrane-proximal basic domain and cysteine cluster in the C-terminal tail of CCR5 constitute a bipartite motif critical for cell surface expression
    • Venkatesan, S., Petrovic, A., Locati, M., Kim, Y. O., Weissman, D., and Murphy, P. M. (2001) A membrane-proximal basic domain and cysteine cluster in the C-terminal tail of CCR5 constitute a bipartite motif critical for cell surface expression. J. Biol. Chem. 276, 40133-40145
    • (2001) J. Biol. Chem. , vol.276 , pp. 40133-40145
    • Venkatesan, S.1    Petrovic, A.2    Locati, M.3    Kim, Y.O.4    Weissman, D.5    Murphy, P.M.6
  • 12
    • 3843070933 scopus 로고    scopus 로고
    • The basic residues in the membrane-proximal C-terminal tail of the rat melanin-concentrating hormone receptor 1 are required for receptor function
    • Tetsuka, M., Saito, Y., Imai, K., Doi, H., and Maruyama, K. (2004) The basic residues in the membrane-proximal C-terminal tail of the rat melanin-concentrating hormone receptor 1 are required for receptor function. Endocrinology 145, 3712-3723
    • (2004) Endocrinology , vol.145 , pp. 3712-3723
    • Tetsuka, M.1    Saito, Y.2    Imai, K.3    Doi, H.4    Maruyama, K.5
  • 13
    • 0141521617 scopus 로고    scopus 로고
    • Endoplasmic reticulum export of glycosyltransferases depends on interaction of a cytoplasmic dibasic motif with Sar1
    • Giraudo, C. G., and Maccioni, H. J. (2003) Endoplasmic reticulum export of glycosyltransferases depends on interaction of a cytoplasmic dibasic motif with Sar1. Mol. Biol. Cell 14, 3753-3766
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3753-3766
    • Giraudo, C.G.1    Maccioni, H.J.2
  • 14
    • 84860920761 scopus 로고    scopus 로고
    • A triple Arg motif mediates α(2B)-adrenergic receptor interaction with Sec24C/D and export
    • Dong, C., Nichols, C. D., Guo, J., Huang, W., Lambert, N. A., and Wu, G. (2012) A triple Arg motif mediates α(2B)-adrenergic receptor interaction with Sec24C/D and export. Traffic 13, 857-868
    • (2012) Traffic , vol.13 , pp. 857-868
    • Dong, C.1    Nichols, C.D.2    Guo, J.3    Huang, W.4    Lambert, N.A.5    Wu, G.6
  • 15
    • 79953192176 scopus 로고    scopus 로고
    • Phosphorylation-dependent C-terminal binding of 14-3-3 proteins promotes cell surface expression of HIV co-receptor GPR15
    • Okamoto, Y., and Shikano, S. (2011) Phosphorylation-dependent C-terminal binding of 14-3-3 proteins promotes cell surface expression of HIV co-receptor GPR15. J. Biol. Chem. 286, 7171-7181
    • (2011) J. Biol. Chem. , vol.286 , pp. 7171-7181
    • Okamoto, Y.1    Shikano, S.2
  • 16
    • 4944228608 scopus 로고    scopus 로고
    • Topogenesis of membrane proteins at the endoplasmic reticulum
    • Higy, M., Junne, T., and Spiess, M. (2004) Topogenesis of membrane proteins at the endoplasmic reticulum. Biochemistry 43, 12716-12722
    • (2004) Biochemistry , vol.43 , pp. 12716-12722
    • Higy, M.1    Junne, T.2    Spiess, M.3
  • 17
    • 67650732710 scopus 로고    scopus 로고
    • Lipid-dependent membrane protein topogenesis
    • Dowhan, W., and Bogdanov, M. (2009) Lipid-dependent membrane protein topogenesis. Annu. Rev. Biochem. 78, 515-540
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 515-540
    • Dowhan, W.1    Bogdanov, M.2
  • 18
    • 24644490119 scopus 로고    scopus 로고
    • Comparative analysis of amino acid distributions in integral membrane proteins from 107 genomes
    • Nilsson, J., Persson, B., and von Heijne, G. (2005) Comparative analysis of amino acid distributions in integral membrane proteins from 107 genomes. Proteins 60, 606-616
    • (2005) Proteins , vol.60 , pp. 606-616
    • Nilsson, J.1    Persson, B.2    Von Heijne, G.3
  • 19
    • 70350038016 scopus 로고    scopus 로고
    • Mapping the human membrane proteome. A majority of the human membrane proteins can be classified according to function and evolutionary origin
    • Almén, M. S., Nordström, K. J., Fredriksson, R., and Schiöth, H. B. (2009) Mapping the human membrane proteome. A majority of the human membrane proteins can be classified according to function and evolutionary origin. BMC Biol. 7, 50
    • (2009) BMC Biol. , vol.7 , pp. 50
    • Almén, M.S.1    Nordström, K.J.2    Fredriksson, R.3    Schiöth, H.B.4
  • 20
    • 0033103174 scopus 로고    scopus 로고
    • A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels
    • Zerangue, N., Schwappach, B., Jan, Y. N., and Jan, L. Y. (1999) A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels. Neuron 22, 537-548
    • (1999) Neuron , vol.22 , pp. 537-548
    • Zerangue, N.1    Schwappach, B.2    Jan, Y.N.3    Jan, L.Y.4
  • 21
    • 0037447231 scopus 로고    scopus 로고
    • 14-3-3 dimers probe the assembly status of multimeric membrane proteins
    • Yuan, H., Michelsen, K., and Schwappach, B. (2003) 14-3-3 dimers probe the assembly status of multimeric membrane proteins. Curr. Biol. 13, 638-646
    • (2003) Curr. Biol. , vol.13 , pp. 638-646
    • Yuan, H.1    Michelsen, K.2    Schwappach, B.3
  • 22
    • 0028181745 scopus 로고
    • Coatomer interaction with di-lysine endoplasmic reticulum retention motifs
    • Cosson, P., and Letourneur, F. (1994) Coatomer interaction with di-lysine endoplasmic reticulum retention motifs. Science 263, 1629-1631
    • (1994) Science , vol.263 , pp. 1629-1631
    • Cosson, P.1    Letourneur, F.2
  • 23
    • 0025184422 scopus 로고
    • Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum
    • Jackson, M. R., Nilsson, T., and Peterson, P. A. (1990) Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum. EMBO J. 9, 3153-3162
    • (1990) EMBO J. , vol.9 , pp. 3153-3162
    • Jackson, M.R.1    Nilsson, T.2    Peterson, P.A.3
  • 24
    • 0032489878 scopus 로고    scopus 로고
    • Cargo selection by the COPII budding machinery during export from the ER
    • Aridor, M., Weissman, J., Bannykh, S., Nuoffer, C., and Balch, W. E. (1998) Cargo selection by the COPII budding machinery during export from the ER. J. Cell Biol. 141, 61-70
    • (1998) J. Cell Biol. , vol.141 , pp. 61-70
    • Aridor, M.1    Weissman, J.2    Bannykh, S.3    Nuoffer, C.4    Balch, W.E.5
  • 25
    • 33847357796 scopus 로고    scopus 로고
    • Role of Sec24 isoforms in selective export of membrane proteins from the endoplasmic reticulum
    • Wendeler, M. W., Paccaud, J. P., and Hauri, H. P. (2007) Role of Sec24 isoforms in selective export of membrane proteins from the endoplasmic reticulum. EMBO Rep. 8, 258-264
    • (2007) EMBO Rep. , vol.8 , pp. 258-264
    • Wendeler, M.W.1    Paccaud, J.P.2    Hauri, H.P.3
  • 26
    • 79952475401 scopus 로고    scopus 로고
    • Selective protein export from the ER mediated by COPIIcoated vesicles
    • Sato, K. (2010) Selective protein export from the ER mediated by COPIIcoated vesicles. Seikagaku 82, 1011-1020
    • (2010) Seikagaku , vol.82 , pp. 1011-1020
    • Sato, K.1
  • 27
    • 79959668938 scopus 로고    scopus 로고
    • Golgi export of the Kir2.1 channel is driven by a trafficking signal located within its tertiary structure
    • Ma, D., Taneja, T. K., Hagen, B. M., Kim, B. Y., Ortega, B., Lederer, W. J., and Welling, P. A. (2011) Golgi export of the Kir2.1 channel is driven by a trafficking signal located within its tertiary structure. Cell 145, 1102-1115
    • (2011) Cell , vol.145 , pp. 1102-1115
    • Ma, D.1    Taneja, T.K.2    Hagen, B.M.3    Kim, B.Y.4    Ortega, B.5    Lederer, W.J.6    Welling, P.A.7
  • 28
    • 67649306770 scopus 로고    scopus 로고
    • G-protein-coupled receptors, cholesterol and palmitoylation. Facts about fats
    • Chini, B., and Parenti, M. (2009) G-protein-coupled receptors, cholesterol and palmitoylation. Facts about fats. J. Mol. Endocrinol. 42, 371-379
    • (2009) J. Mol. Endocrinol. , vol.42 , pp. 371-379
    • Chini, B.1    Parenti, M.2
  • 31
    • 0028872763 scopus 로고
    • The lutropin/choriogonadotropin receptor is palmitoylated at intracellular cysteine residues
    • Zhu, H., Wang, H., and Ascoli, M. (1995) The lutropin/choriogonadotropin receptor is palmitoylated at intracellular cysteine residues. Mol. Endocrinol. 9, 141-150
    • (1995) Mol. Endocrinol. , vol.9 , pp. 141-150
    • Zhu, H.1    Wang, H.2    Ascoli, M.3
  • 33
    • 0037112783 scopus 로고    scopus 로고
    • The Erv41p-Erv46p complex. Multiple export signals are required in trans for COPII-dependent transport from the ER
    • Otte, S., and Barlowe, C. (2002) The Erv41p-Erv46p complex. Multiple export signals are required in trans for COPII-dependent transport from the ER. EMBO J. 21, 6095-6104
    • (2002) EMBO J. , vol.21 , pp. 6095-6104
    • Otte, S.1    Barlowe, C.2
  • 34
    • 0038285159 scopus 로고    scopus 로고
    • Membrane receptor trafficking. Evidence of proximal and distal zones conferred by two independent endoplasmic reticulum localization signals
    • Shikano, S., and Li, M. (2003) Membrane receptor trafficking. Evidence of proximal and distal zones conferred by two independent endoplasmic reticulum localization signals. Proc. Natl. Acad. Sci. U.S.A. 100, 5783-5788
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 5783-5788
    • Shikano, S.1    Li, M.2
  • 35
    • 27844528834 scopus 로고    scopus 로고
    • A three-amino-acid-long HLA-DRβ cytoplasmic tail is sufficient to overcome ER retention of invariant-chain p35
    • Khalil, H., Brunet, A., and Thibodeau, J. (2005) A three-amino-acid-long HLA-DRβ cytoplasmic tail is sufficient to overcome ER retention of invariant-chain p35. J. Cell Sci. 118, 4679-4687
    • (2005) J. Cell Sci. , vol.118 , pp. 4679-4687
    • Khalil, H.1    Brunet, A.2    Thibodeau, J.3
  • 36
    • 22344431603 scopus 로고    scopus 로고
    • The RXR-type endoplasmic reticulum-retention/retrieval signal of GABAB1 requires distant spacing from the membrane to function
    • Gassmann, M., Haller, C., Stoll, Y., Abdel Aziz, S., Biermann, B., Mosbacher, J., Kaupmann, K., and Bettler, B. (2005) The RXR-type endoplasmic reticulum-retention/retrieval signal of GABAB1 requires distant spacing from the membrane to function. Mol. Pharmacol. 68, 137-144
    • (2005) Mol. Pharmacol. , vol.68 , pp. 137-144
    • Gassmann, M.1    Haller, C.2    Stoll, Y.3    Abdel Aziz, S.4    Biermann, B.5    Mosbacher, J.6    Kaupmann, K.7    Bettler, B.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.