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Volumn 7, Issue 10, 2005, Pages 985-992

Genetic isolation of transport signals directing cell surface expression

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE PROTEIN; POTASSIUM CHANNEL;

EID: 27144526643     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb1297     Document Type: Article
Times cited : (57)

References (32)
  • 1
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin, E. & von Heijne, G. Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci. 7, 1029-1038 (1998).
    • (1998) Protein Sci. , vol.7 , pp. 1029-1038
    • Wallin, E.1    von Heijne, G.2
  • 2
    • 0842324801 scopus 로고    scopus 로고
    • The mechanisms of vesicle budding and fusion
    • Bonifacino, J. S. & Glick, B. S. The mechanisms of vesicle budding and fusion. Cell 116, 153-166 (2004).
    • (2004) Cell , vol.116 , pp. 153-166
    • Bonifacino, J.S.1    Glick, B.S.2
  • 3
    • 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. & Jan, L. Y. A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels. Neuron 22, 537-548 (1999).
    • (1999) Neuron , vol.22 , pp. 537-548
    • Zerangue, N.1    Schwappach, B.2    Jan, Y.N.3    Jan, L.Y.4
  • 4
    • 4344662040 scopus 로고    scopus 로고
    • PI3K promotes voltage-dependent calcium channel trafficking to the plasma membrane
    • Viard, P. et al. PI3K promotes voltage-dependent calcium channel trafficking to the plasma membrane. Nature Neurosci. 7, 939-946 (2004).
    • (2004) Nature Neurosci. , vol.7 , pp. 939-946
    • Viard, P.1
  • 5
    • 0037112329 scopus 로고    scopus 로고
    • Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals
    • O'Kelly, I., Butler, M. H., Zilberberg, N. & Goldstein, S. A. Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals. Cell 111, 577-588 (2002).
    • (2002) Cell , vol.111 , pp. 577-588
    • O'Kelly, I.1    Butler, M.H.2    Zilberberg, N.3    Goldstein, S.A.4
  • 6
    • 0033710346 scopus 로고    scopus 로고
    • Molecular basis for K(ATP) assembly: Transmembrane interactions mediate association of a K+ channel with an ABC transporter
    • Schwappach, B., Zerangue, N., Jan, Y. N. & Jan, L. Y. Molecular basis for K(ATP) assembly: Transmembrane interactions mediate association of a K+ channel with an ABC transporter. Neuron 26, 155-167 (2000).
    • (2000) Neuron , vol.26 , pp. 155-167
    • Schwappach, B.1    Zerangue, N.2    Jan, Y.N.3    Jan, L.Y.4
  • 7
    • 0038285159 scopus 로고    scopus 로고
    • Membrane receptor trafficking: Evidence of proximal and distal zones conferred by two independent endoplasmic reticulum localization signals
    • Shikano, S. & Li, M. Membrane receptor trafficking: Evidence of proximal and distal zones conferred by two independent endoplasmic reticulum localization signals. Proc. Natl Acad. Sci. USA 100, 5783-5788 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5783-5788
    • Shikano, S.1    Li, M.2
  • 8
    • 0030812940 scopus 로고    scopus 로고
    • A di-acidic signal required for selective export from the endoplasmic reticulum
    • Nishimura, N. & Balch, W. E. A di-acidic signal required for selective export from the endoplasmic reticulum. Science 277, 556-558 (1997).
    • (1997) Science , vol.277 , pp. 556-558
    • Nishimura, N.1    Balch, W.E.2
  • 9
    • 0033959784 scopus 로고    scopus 로고
    • Efficient export of the vesicular stomatitis virus G protein from the endoplasmic reticulum requires a signal in the cytoplasmic tail that includes both tyrosine-based and di-acidic motifs
    • Sevier, C. S., Weisz, O. A., Davis, M. & Machamer, C. E. Efficient export of the vesicular stomatitis virus G protein from the endoplasmic reticulum requires a signal in the cytoplasmic tail that includes both tyrosine-based and di-acidic motifs. Mol. Biol. Cell 11, 13-22 (2000).
    • (2000) Mol. Biol. Cell , vol.11 , pp. 13-22
    • Sevier, C.S.1    Weisz, O.A.2    Davis, M.3    Machamer, C.E.4
  • 10
    • 0035846990 scopus 로고    scopus 로고
    • Role of ER export signals in controlling surface potassium channel numbers
    • Ma, D. et al. Role of ER export signals in controlling surface potassium channel numbers. Science 291, 316-319 (2001).
    • (2001) Science , vol.291 , pp. 316-319
    • Ma, D.1
  • 11
    • 0024314706 scopus 로고
    • Short cytoplasmic sequences serve as retention signals for transmembrane proteins in the endoplasmic reticulum
    • Nilsson, T., Jackson, M. & Peterson, P. A. Short cytoplasmic sequences serve as retention signals for transmembrane proteins in the endoplasmic reticulum. Cell 58, 707-718 (1989).
    • (1989) Cell , vol.58 , pp. 707-718
    • Nilsson, T.1    Jackson, M.2    Peterson, P.A.3
  • 12
    • 0029145135 scopus 로고
    • Functional expression of a vertebrate inwardly rectifying K+ channel in yeast
    • Tang, W. et al. Functional expression of a vertebrate inwardly rectifying K+ channel in yeast. Mol. Biol. Cell 6, 1231-1240 (1995).
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1231-1240
    • Tang, W.1
  • 13
    • 0036498862 scopus 로고    scopus 로고
    • Functional diversity of protein C-termini: More than zipcoding?
    • Chung, J. J., Shikano, S., Hanyu, Y. & Li, M. Functional diversity of protein C-termini: More than zipcoding? Trends Cell Biol. 12, 146-150 (2002).
    • (2002) Trends Cell Biol. , vol.12 , pp. 146-150
    • Chung, J.J.1    Shikano, S.2    Hanyu, Y.3    Li, M.4
  • 16
    • 0033592326 scopus 로고    scopus 로고
    • Isolation of high-affinity peptide antagonists of 14-3-3 proteins by phage display
    • Wang, B. et al. Isolation of high-affinity peptide antagonists of 14-3-3 proteins by phage display. Biochemistry 38, 12499-12504 (1999).
    • (1999) Biochemistry , vol.38 , pp. 12499-12504
    • Wang, B.1
  • 17
    • 10044230383 scopus 로고    scopus 로고
    • Function recovery after chemobleaching (FRAC): Evidence for activity silent membrane receptors on cell surface
    • Sun, H., Shikano, S., Xiong, Q. & Li, M. Function recovery after chemobleaching (FRAC): Evidence for activity silent membrane receptors on cell surface. Proc. Natl Acad. Sci. USA 101, 16964-16969 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 16964-16969
    • Sun, H.1    Shikano, S.2    Xiong, Q.3    Li, M.4
  • 19
    • 0037138389 scopus 로고    scopus 로고
    • How do 14-3-3 proteins work? - Gatekeeper phosphorylation and the molecular anvil hypothesis
    • Yaffe, M. B. How do 14-3-3 proteins work? - Gatekeeper phosphorylation and the molecular anvil hypothesis. FEBS Lett. 513, 53-57 (2002).
    • (2002) FEBS Lett. , vol.513 , pp. 53-57
    • Yaffe, M.B.1
  • 20
    • 12844265993 scopus 로고    scopus 로고
    • Melatonin synthesis: 14-3-3-dependent activation and inhibition of arylalkylamine N-acetyltransferase mediated by phosphoserine-205
    • Ganguly, S. et al. Melatonin synthesis: 14-3-3-dependent activation and inhibition of arylalkylamine N-acetyltransferase mediated by phosphoserine-205. Proc. Natl Acad. Sci. USA 102, 1222-1227 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 1222-1227
    • Ganguly, S.1
  • 21
    • 0034596067 scopus 로고    scopus 로고
    • Proton block and voltage gating are potassium-dependent in the cardiac leak channel Kcnk3
    • Lopes, C. M., Gallagher, P. G., Buck, M. E., Butler, M. H. & Goldstein, S. A. Proton block and voltage gating are potassium-dependent in the cardiac leak channel Kcnk3. J. Biol. Chem. 275, 16969-16978 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 16969-16978
    • Lopes, C.M.1    Gallagher, P.G.2    Buck, M.E.3    Butler, M.H.4    Goldstein, S.A.5
  • 22
    • 0037258717 scopus 로고    scopus 로고
    • The virotoxin model of HIV-1 enteropathy: Involvement of GPR15/Bob and galactosylceramide in the cytopathic effects induced by HIV-1 gp120 in the HT-29-D4 intestinal cell line
    • Maresca, M. et al. The virotoxin model of HIV-1 enteropathy: Involvement of GPR15/Bob and galactosylceramide in the cytopathic effects induced by HIV-1 gp120 in the HT-29-D4 intestinal cell line. J. Biomed. Sci. 10, 156-166 (2003).
    • (2003) J. Biomed. Sci. , vol.10 , pp. 156-166
    • Maresca, M.1
  • 23
    • 0035283096 scopus 로고    scopus 로고
    • Cloning and sequencing of cynomolgus macaque CCR3, GPR15, and STRL33: Potential coreceptors for HIV type 1, HIV type 2, and SIV
    • Wade-Evans, A. M., Russell, J., Jenkins, A. & Javan, C. Cloning and sequencing of cynomolgus macaque CCR3, GPR15, and STRL33: Potential coreceptors for HIV type 1, HIV type 2, and SIV. AIDS Res. Hum. Retroviruses 17, 371-375 (2001).
    • (2001) AIDS Res. Hum. Retroviruses , vol.17 , pp. 371-375
    • Wade-Evans, A.M.1    Russell, J.2    Jenkins, A.3    Javan, C.4
  • 24
    • 0037447231 scopus 로고    scopus 로고
    • 14-3-3 dimers probe the assembly status of multimeric membrane proteins
    • Yuan, H., Michelsen, K. & Schwappach, B. 14-3-3 dimers probe the assembly status of multimeric membrane proteins. Curr. Biol. 13, 638-646 (2003).
    • (2003) Curr. Biol. , vol.13 , pp. 638-646
    • Yuan, H.1    Michelsen, K.2    Schwappach, B.3
  • 25
    • 0035072833 scopus 로고    scopus 로고
    • A motif-based profile scanning approach for genome-wide prediction of signaling pathways
    • Yaffe, M. B. et al. A motif-based profile scanning approach for genome-wide prediction of signaling pathways. Nature Biotechnol. 19, 348-353 (2001).
    • (2001) Nature Biotechnol. , vol.19 , pp. 348-353
    • Yaffe, M.B.1
  • 26
    • 2942552470 scopus 로고    scopus 로고
    • Unlocking the code of 14-3-3
    • Dougherty, M. K. & Morrison, D. K. Unlocking the code of 14-3-3. J. Cell Sci. 117, 1875-1884 (2004).
    • (2004) J. Cell Sci. , vol.117 , pp. 1875-1884
    • Dougherty, M.K.1    Morrison, D.K.2
  • 27
    • 0037090803 scopus 로고    scopus 로고
    • 14-3-3 amplifies and prolongs adrenergic stimulation of HERG K+ channel activity
    • Kagan, A., Melman, Y. F., Krumerman, A. & McDonald, T. V. 14-3-3 amplifies and prolongs adrenergic stimulation of HERG K+ channel activity. EMBO J. 21, 1889-1898 (2002).
    • (2002) EMBO J. , vol.21 , pp. 1889-1898
    • Kagan, A.1    Melman, Y.F.2    Krumerman, A.3    McDonald, T.V.4
  • 28
    • 0043029286 scopus 로고    scopus 로고
    • SNARE selectivity of the COPII coat
    • Mossessova, E., Bickford, L. C. & Goldberg, J. SNARE selectivity of the COPII coat. Cell 114, 483-495 (2003).
    • (2003) Cell , vol.114 , pp. 483-495
    • Mossessova, E.1    Bickford, L.C.2    Goldberg, J.3
  • 29
    • 0041526467 scopus 로고    scopus 로고
    • Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles
    • Miller, E. A. et al. Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles. Cell 114, 497-509 (2003).
    • (2003) Cell , vol.114 , pp. 497-509
    • Miller, E.A.1
  • 30
    • 27144474397 scopus 로고    scopus 로고
    • Genome-wide analyses of carboxyl-terminal sequences
    • Chung, J. J., Yang, H. & Li, M. Genome-wide analyses of carboxyl-terminal sequences. Mol. Cell. Proteomics 2, 173-181 (2003).
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 173-181
    • Chung, J.J.1    Yang, H.2    Li, M.3
  • 31
    • 27744523654 scopus 로고    scopus 로고
    • Carboxyl-terminal recognition by 14-3-3 proteins for surface expression of membrane receptors
    • (in the press)
    • Coblitz, B. et al. Carboxyl-terminal recognition by 14-3-3 proteins for surface expression of membrane receptors. J. Biol. Chem. (in the press).
    • J. Biol. Chem.
    • Coblitz, B.1
  • 32
    • 0037186091 scopus 로고    scopus 로고
    • Diverse trafficking patterns due to multiple traffic motifs in G protein-activated inwardly rectifying potassium channels from brain and heart
    • Ma, D. et al. Diverse trafficking patterns due to multiple traffic motifs in G protein-activated inwardly rectifying potassium channels from brain and heart. Neuron 33, 715-729 (2002).
    • (2002) Neuron , vol.33 , pp. 715-729
    • Ma, D.1


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