메뉴 건너뛰기




Volumn 13, Issue 8, 2003, Pages 638-646

14-3-3 Dimers probe the assembly status of multimeric membrane proteins

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0037447231     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(03)00208-2     Document Type: Article
Times cited : (177)

References (49)
  • 1
    • 0035424237 scopus 로고    scopus 로고
    • ER quality control: Towards an understanding at the molecular level
    • Ellgaard, L., and Helenius, A. (2001). ER quality control: towards an understanding at the molecular level. Curr. Opin. Cell Biol. 13, 431-437.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 431-437
    • Ellgaard, L.1    Helenius, A.2
  • 2
    • 0033667466 scopus 로고    scopus 로고
    • A trafficking checkpoint controls GABA(B) receptor heterodimerization
    • Margeta-Mitrovic, M., Jan, Y.N., and Jan, L.Y. (2000). A trafficking checkpoint controls GABA(B) receptor heterodimerization, Neuron 27, 97-106.
    • (2000) Neuron , vol.27 , pp. 97-106
    • Margeta-Mitrovic, M.1    Jan, Y.N.2    Jan, L.Y.3
  • 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., 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
  • 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., and Goldstein, S.A. (2002). Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals. Cell 111, 577-588.
    • (2002) Cell , vol.111 , pp. 577-588
    • O'Kelly, I.1    Butler, M.H.2    Zilberberg, N.3    Goldstein, S.A.4
  • 6
    • 0034520590 scopus 로고    scopus 로고
    • PDZ domain suppression of an ER retention signal in NMDA receptor NR1 splice variants
    • Standley, S., Roche, K.W., McCallum, J., Sans, N., and Wenthold, R.J. (2000). PDZ domain suppression of an ER retention signal in NMDA receptor NR1 splice variants. Neuron 28, 887-898.
    • (2000) Neuron , vol.28 , pp. 887-898
    • Standley, S.1    Roche, K.W.2    McCallum, J.3    Sans, N.4    Wenthold, R.J.5
  • 7
    • 0034788270 scopus 로고    scopus 로고
    • An ER retention signal explains differences in surface expression of NMDA and AMPA receptor subunits
    • Xia, H., Hornby, Z.D., and Malenka, R.C. (2001). An ER retention signal explains differences in surface expression of NMDA and AMPA receptor subunits. Neuropharmacology 41, 714-723.
    • (2001) Neuropharmacology , vol.41 , pp. 714-723
    • Xia, H.1    Hornby, Z.D.2    Malenka, R.C.3
  • 9
    • 0035066063 scopus 로고    scopus 로고
    • Molecular determinants of metabotropic glutamate receptor 1B trafficking
    • Chan, W.Y., Soloviev, M.M., Ciruela, F., and Mcllhinney, R.A. (2001). Molecular determinants of metabotropic glutamate receptor 1B trafficking. Mol. Cell. Neurosci. 17, 577-588.
    • (2001) Mol. Cell. Neurosci. , vol.17 , pp. 577-588
    • Chan, W.Y.1    Soloviev, M.M.2    Ciruela, F.3    Mcllhinney, R.A.4
  • 10
    • 0033166350 scopus 로고    scopus 로고
    • Removal of multiple arginine-framed trafficking signals overcomes misprocessing of delta F508 CFTR present in most patients with cystic fibrosis
    • Chang, X.B., Cui, L., Hou, Y.X., Jensen, T.J., Aleksandrov, A.A., Mengos, A., and Riordan, J.R. (1999). Removal of multiple arginine-framed trafficking signals overcomes misprocessing of delta F508 CFTR present in most patients with cystic fibrosis. Mol. Cell 4, 137-142.
    • (1999) Mol. Cell , vol.4 , pp. 137-142
    • Chang, X.B.1    Cui, L.2    Hou, Y.X.3    Jensen, T.J.4    Aleksandrov, A.A.5    Mengos, A.6    Riordan, J.R.7
  • 11
    • 0035341508 scopus 로고    scopus 로고
    • An NMDA receptor ER retention signal regulated by phosphorylation and alternative splicing
    • Scott, D.B., Blanpied, T.A., Swanson, G.T., Zhang, C., and Ehlers, M.D. (2001). An NMDA receptor ER retention signal regulated by phosphorylation and alternative splicing. J. Neurosci. 21, 3063-3072.
    • (2001) J. Neurosci. , vol.21 , pp. 3063-3072
    • Scott, D.B.1    Blanpied, T.A.2    Swanson, G.T.3    Zhang, C.4    Ehlers, M.D.5
  • 12
    • 0032101992 scopus 로고    scopus 로고
    • A touching case of channel regulation: The ATP-sensitive K+ channel
    • Tucker, S.J., and Ashcroft, F.M. (1998). A touching case of channel regulation: the ATP-sensitive K+ channel. Curr. Opin. Neurobiol. 8, 316-320.
    • (1998) Curr. Opin. Neurobiol. , vol.8 , pp. 316-320
    • Tucker, S.J.1    Ashcroft, F.M.2
  • 13
    • 0033037098 scopus 로고    scopus 로고
    • ATP-sensitive potassium channels: A model of heteromultimeric potassium channel/receptor assemblies
    • Seino, S. (1999). ATP-sensitive potassium channels: a model of heteromultimeric potassium channel/receptor assemblies. Annu. Rev. Physiol. 61, 337-362.
    • (1999) Annu. Rev. Physiol. , vol.61 , pp. 337-362
    • Seino, S.1
  • 14
    • 0032788372 scopus 로고    scopus 로고
    • Molecular biology of adenosine triphosphate-sensitive potassium channels
    • Aguilar-Bryan, L., and Bryan, J. (1999). Molecular biology of adenosine triphosphate-sensitive potassium channels. Endocr. Rev. 20, 101-135.
    • (1999) Endocr. Rev. , vol.20 , pp. 101-135
    • Aguilar-Bryan, L.1    Bryan, J.2
  • 15
    • 0027756896 scopus 로고
    • A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants
    • Harbury, P.B., Zhang, T., Kim, P.S., and Alber, T. (1993). A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants. Science 262, 1401-1407.
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 16
    • 0028214450 scopus 로고
    • Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis
    • Schagger, H., Cramer, W.A., and von Jagow, G. (1994). Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis. Anal. Biochem. 217, 220-230.
    • (1994) Anal. Biochem. , vol.217 , pp. 220-230
    • Schagger, H.1    Cramer, W.A.2    Von Jagow, G.3
  • 17
    • 0033592326 scopus 로고    scopus 로고
    • Isolation of high-affinity peptide antagonists of 14-3-3 proteins by phage display
    • Wang, B., Yang, H., Liu, Y.C., Jelinek, T., Zhang, L., Ruoslahti, E., and Fu, H. (1999). Isolation of high-affinity peptide antagonists of 14-3-3 proteins by phage display. Biochemistry 38, 12499-12504.
    • (1999) Biochemistry , vol.38 , pp. 12499-12504
    • Wang, B.1    Yang, H.2    Liu, Y.C.3    Jelinek, T.4    Zhang, L.5    Ruoslahti, E.6    Fu, H.7
  • 19
    • 0032568665 scopus 로고    scopus 로고
    • 14-3-3Zeta binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove
    • Petosa, C., Masters, S.C., Bankston, L.A., Pohl, J., Wang, B., Fu, H., and Liddington, R.C. (1998). 14-3-3zeta binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove. J. Biol. Chem. 273, 16305-16310.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16305-16310
    • Petosa, C.1    Masters, S.C.2    Bankston, L.A.3    Pohl, J.4    Wang, B.5    Fu, H.6    Liddington, R.C.7
  • 20
    • 0036382829 scopus 로고    scopus 로고
    • Assembly-dependent trafficking assays in the detection of receptor- receptor interactions
    • Margeta-Mitrovic, M. (2002). Assembly-dependent trafficking assays in the detection of receptor- receptor interactions. Methods 27, 311-317.
    • (2002) Methods , vol.27 , pp. 311-317
    • Margeta-Mitrovic, M.1
  • 21
    • 0027538121 scopus 로고
    • Retrieval of transmembrane proteins to the endoplasmic reticulum
    • Jackson, M.R., Nilsson, T., and Peterson, P.A. (1993). Retrieval of transmembrane proteins to the endoplasmic reticulum. J. Cell Biol. 121, 317-333.
    • (1993) J. Cell Biol. , vol.121 , pp. 317-333
    • Jackson, M.R.1    Nilsson, T.2    Peterson, P.A.3
  • 22
    • 0347154149 scopus 로고    scopus 로고
    • An artificial tetramerization domain restores efficient assembly of functional Shaker channels lacking T1
    • Zerangue, N., Jan, Y.N., and Jan, L.Y. (2000). An artificial tetramerization domain restores efficient assembly of functional Shaker channels lacking T1. Proc. Natl. Acad. Sci. USA 97, 3591-3595.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3591-3595
    • Zerangue, N.1    Jan, Y.N.2    Jan, L.Y.3
  • 23
    • 0035473486 scopus 로고    scopus 로고
    • 14-3-3 Proteins; bringing new definitions to scaffolding
    • Tzivion, G., Shen, Y.H., and Zhu, J. (2001). 14-3-3 proteins; bringing new definitions to scaffolding. Oncogene 20, 6331-6338.
    • (2001) Oncogene , vol.20 , pp. 6331-6338
    • Tzivion, G.1    Shen, Y.H.2    Zhu, J.3
  • 24
    • 0036479325 scopus 로고    scopus 로고
    • 14-3-3 Proteins: Active cofactors in cellular regulation by serine/threonine phosphorylation
    • Tzivion, G., and Avruch, J. (2002). 14-3-3 proteins: active cofactors in cellular regulation by serine/threonine phosphorylation. J. Biol. Chem, 277, 3061-3064.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3061-3064
    • Tzivion, G.1    Avruch, J.2
  • 25
    • 0034788964 scopus 로고    scopus 로고
    • 14-3-3 Proteins: Key regulators of cell division, signalling and apoptosis
    • van Hemert, M.J., Steensma, H.Y., and van Heusden, G.P. (2001). 14-3-3 proteins: key regulators of cell division, signalling and apoptosis. Bioessays 23, 936-946.
    • (2001) Bioessays , vol.23 , pp. 936-946
    • Van Hemert, M.J.1    Steensma, H.Y.2    Van Heusden, G.P.3
  • 27
    • 0028349810 scopus 로고
    • An N-terminal double-arginine motif maintains type II membrane proteins in the endoplasmic reticulum
    • Schutze, M.P., Peterson, P.A., and Jackson, M.R. (1994). An N-terminal double-arginine motif maintains type II membrane proteins in the endoplasmic reticulum. EMBO J. 13, 1696-1705.
    • (1994) EMBO J. , vol.13 , pp. 1696-1705
    • Schutze, M.P.1    Peterson, P.A.2    Jackson, M.R.3
  • 28
    • 0032477869 scopus 로고    scopus 로고
    • Exit of major histocompatibility complex class II-invariant chain p35 complexes from the endoplasmic reticulum is modulated by phosphorylation
    • Kuwana, T., Peterson, P.A., and Karlsson, L. (1998). Exit of major histocompatibility complex class II-invariant chain p35 complexes from the endoplasmic reticulum is modulated by phosphorylation. Proc. Natl. Acad. Sci. USA 95, 1056-1061.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1056-1061
    • Kuwana, T.1    Peterson, P.A.2    Karlsson, L.3
  • 29
    • 0032525027 scopus 로고    scopus 로고
    • Phosphorylation regulates the delivery of MHC class II invariant chain complexes to antigen processing compartments
    • Anderson, H.A., and Roche, P.A. (1998). Phosphorylation regulates the delivery of MHC class II invariant chain complexes to antigen processing compartments. J. Immunol. 160, 4850-4858.
    • (1998) J. Immunol. , vol.160 , pp. 4850-4858
    • Anderson, H.A.1    Roche, P.A.2
  • 30
    • 0033571092 scopus 로고    scopus 로고
    • Phosphorylation of the invariant chain by protein kinase C regulates MHC class II trafficking to antigen-processing compartments
    • Anderson, H.A., Bergstralh, D.T., Kawamura, T., Blauvelt, A., and Roche, P.A. (1999). Phosphorylation of the invariant chain by protein kinase C regulates MHC class II trafficking to antigen-processing compartments. J. Immunol. 163, 5435-5443.
    • (1999) J. Immunol. , vol.163 , pp. 5435-5443
    • Anderson, H.A.1    Bergstralh, D.T.2    Kawamura, T.3    Blauvelt, A.4    Roche, P.A.5
  • 31
    • 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
  • 32
    • 0029988456 scopus 로고    scopus 로고
    • Delta-and zeta-COP, two coatomer subunits homologous to clathrin-associated proteins, are involved in ER retrieval
    • Cosson, P., Démollière, C., Hennecke, S., Duden, R., and Letourneur, F. (1996). Delta-and zeta-COP, two coatomer subunits homologous to clathrin-associated proteins, are involved in ER retrieval. EMBO J. 15, 1792-1798.
    • (1996) EMBO J. , vol.15 , pp. 1792-1798
    • Cosson, P.1    Démollière, C.2    Hennecke, S.3    Duden, R.4    Letourneur, F.5
  • 33
    • 0028029829 scopus 로고
    • Signal-mediated retrieval of a membrane protein from the Golgi to the ER in yeast
    • Gaynor, E.C., te Heesen, S., Graham, T.R., Aebi, M., and Emr, S.D. (1994). Signal-mediated retrieval of a membrane protein from the Golgi to the ER in yeast. J. Cell Biol, 127, 653-665.
    • (1994) J. Cell Biol. , vol.127 , pp. 653-665
    • Gaynor, E.C.1    Te Heesen, S.2    Graham, T.R.3    Aebi, M.4    Emr, S.D.5
  • 34
    • 0029874257 scopus 로고    scopus 로고
    • Nonclathrin coat protein gamma, a subunit of coatomer, binds to the cytoplasmic dilysine motif of membrane proteins of the early secretory pathway
    • Harter, C., Pavel, J., Coccia, F., Draken, E., Wegehingel, S., Tschochner, H., and Wieland, F. (1996). Nonclathrin coat protein gamma, a subunit of coatomer, binds to the cytoplasmic dilysine motif of membrane proteins of the early secretory pathway. Proc. Natl. Acad. Sci. USA 93, 1902-1906.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1902-1906
    • Harter, C.1    Pavel, J.2    Coccia, F.3    Draken, E.4    Wegehingel, S.5    Tschochner, H.6    Wieland, F.7
  • 35
    • 0024314706 scopus 로고
    • Short cytoplasmic sequences serve as retention signals for transmembrane proteins in the endoplasmic reticulum
    • Nilsson, T., Jackson, M., and Peterson, P.A. (1989). Short cytoplasmic sequences serve as retention signals for transmembrane proteins in the endoplasmic reticulum. Cell 58, 707-718.
    • (1989) Cell , vol.58 , pp. 707-718
    • Nilsson, T.1    Jackson, M.2    Peterson, P.A.3
  • 36
    • 0028361767 scopus 로고
    • The KKXX signal mediates retrieval of membrane proteins from the Golgi to the ER in yeast
    • Townsley, F.M., and Pelham, H.R. (1994). The KKXX signal mediates retrieval of membrane proteins from the Golgi to the ER in yeast. Eur. J. Cell Biol. 64, 211-216.
    • (1994) Eur. J. Cell Biol. , vol.64 , pp. 211-216
    • Townsley, F.M.1    Pelham, H.R.2
  • 37
    • 0242467078 scopus 로고    scopus 로고
    • PKA-mediated phosphorylation of the human K(ATP) channel: Separate roles of Kir6.2 and SUR1 subunit phosphorylation
    • Beguin, P., Nagashima, K., Nishimura, M., Gonoi, T., and Seino, S. (1999). PKA-mediated phosphorylation of the human K(ATP) channel: separate roles of Kir6.2 and SUR1 subunit phosphorylation. EMBO J, 18, 4722-4732.
    • (1999) EMBO J. , vol.18 , pp. 4722-4732
    • Beguin, P.1    Nagashima, K.2    Nishimura, M.3    Gonoi, T.4    Seino, S.5
  • 38
    • 0034161609 scopus 로고    scopus 로고
    • Regulation of ATP-sensitive potassium channel function by protein kinase A-mediated phosphorylation in transfected HEK293 cells
    • Lin, Y.F., Jan, Y.N., and Jan, L.Y. (2000). Regulation of ATP-sensitive potassium channel function by protein kinase A-mediated phosphorylation in transfected HEK293 cells. EMBO J. 19, 942-955.
    • (2000) EMBO J. , vol.19 , pp. 942-955
    • Lin, Y.F.1    Jan, Y.N.2    Jan, L.Y.3
  • 41
    • 0033118606 scopus 로고    scopus 로고
    • A dynamically regulated 14-3-3, Slob, and Slowpoke potassium channel complex in Drosophila presynaptic nerve terminals
    • Zhou, Y., Schopperle, W.M., Murrey, H., Jaramillo, A., Dagan, D., Griffith, L.C., and Levitan, I.B. (1999). A dynamically regulated 14-3-3, Slob, and Slowpoke potassium channel complex in Drosophila presynaptic nerve terminals. Neuron 22, 809-818.
    • (1999) Neuron , vol.22 , pp. 809-818
    • Zhou, Y.1    Schopperle, W.M.2    Murrey, H.3    Jaramillo, A.4    Dagan, D.5    Griffith, L.C.6    Levitan, I.B.7
  • 42
    • 0035781086 scopus 로고    scopus 로고
    • Plant plasma membrane H+-ATPases: Powerhouses for nutrient uptake
    • Palmgren, M.G. (2001). Plant plasma membrane H+-ATPases: powerhouses for nutrient uptake. Annu. Rev. Plant Physiol. Plant Mol. Biol. 52, 817-845.
    • (2001) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.52 , pp. 817-845
    • Palmgren, M.G.1
  • 43
    • 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., and McDonald, T.V. (2002). 14-3-3 amplifies and prolongs adrenergic stimulation of HERG K+ channel activity. EMBO J. 21, 1889-1898.
    • (2002) EMBO J. , vol.21 , pp. 1889-1898
    • Kagan, A.1    Melman, Y.F.2    Krumerman, A.3    McDonald, T.V.4
  • 47
    • 0020994721 scopus 로고
    • Preparation of microsomal membranes for cotranslational protein translocation
    • Walter, P., and Blobel, G. (1983). Preparation of microsomal membranes for cotranslational protein translocation. Methods Enzymol. 96, 84-93.
    • (1983) Methods Enzymol. , vol.96 , pp. 84-93
    • Walter, P.1    Blobel, G.2
  • 49
    • 0029162515 scopus 로고
    • Protein insertion into the endoplasmic reticulum of permeabilized cells
    • Jadot, M., Hofmann, M.W., Graf, R., Quader, H., and Martoglio, B. (1995). Protein insertion into the endoplasmic reticulum of permeabilized cells. FEBS Lett. 371, 145-148.
    • (1995) FEBS Lett. , vol.371 , pp. 145-148
    • Jadot, M.1    Hofmann, M.W.2    Graf, R.3    Quader, H.4    Martoglio, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.