메뉴 건너뛰기




Volumn 123, Issue 8, 2010, Pages 1320-1328

Dimerization of adiponectin receptor 1 is inhibited by adiponectin

Author keywords

Adiponectin; Adiponectin receptor; Bimolecular fluorescence complementation; Receptor dimerization

Indexed keywords

ADIPONECTIN RECEPTOR 1;

EID: 77951201291     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.057919     Document Type: Article
Times cited : (34)

References (51)
  • 1
    • 0036511213 scopus 로고    scopus 로고
    • ACRP30/adiponectin: An adipokine regulating glucose and lipid metabolism
    • Berg, A. H., Combs, T. P. and Scherer, P. E. (2002). ACRP30/adiponectin: an adipokine regulating glucose and lipid metabolism. Trends Endocrinol. Metab. 13, 84-89.
    • (2002) Trends Endocrinol. Metab. , vol.13 , pp. 84-89
    • Berg, A.H.1    Combs, T.P.2    Scherer, P.E.3
  • 2
    • 0016723939 scopus 로고
    • Percutaneous needle biopsy of skeletal muscle in physiological and clinical research
    • Bergstrom, J. (1975). Percutaneous needle biopsy of skeletal muscle in physiological and clinical research. Scand. J. Clin. Lab. Invest. 35, 609-616.
    • (1975) Scand. J. Clin. Lab. Invest. , vol.35 , pp. 609-616
    • Bergstrom, J.1
  • 5
    • 33644962142 scopus 로고    scopus 로고
    • Visualization of APP dimerization and APP-Notch2 heterodimerization in living cells using bimolecular fluorescence complementation
    • Chen, C. D., Oh, S. Y., Hinman, J. D. and Abraham, C. R. (2006). Visualization of APP dimerization and APP-Notch2 heterodimerization in living cells using bimolecular fluorescence complementation. J. Neurochem. 97, 30-43.
    • (2006) J. Neurochem. , vol.97 , pp. 30-43
    • Chen, C.D.1    Oh, S.Y.2    Hinman, J.D.3    Abraham, C.R.4
  • 7
    • 0038237527 scopus 로고    scopus 로고
    • Homodimerization of neuropeptide y receptors investigated by fluorescence resonance energy transfer in living cells
    • Dinger, M. C., Bader, J. E., Kobor, A. D., Kretzschmar, A. K. and Beck-Sickinger, A. G. (2003). Homodimerization of neuropeptide y receptors investigated by fluorescence resonance energy transfer in living cells. J. Biol. Chem. 278, 10562-10571.
    • (2003) J. Biol. Chem. , vol.278 , pp. 10562-10571
    • Dinger, M.C.1    Bader, J.E.2    Kobor, A.D.3    Kretzschmar, A.K.4    Beck-Sickinger, A.G.5
  • 8
    • 10044263319 scopus 로고    scopus 로고
    • Adiponectin, obesity, and cardiovascular disease
    • Fasshauer, M., Paschke, R. and Stumvoll, M. (2004). Adiponectin, obesity, and cardiovascular disease. Biochimie 86, 779-784.
    • (2004) Biochimie , vol.86 , pp. 779-784
    • Fasshauer, M.1    Paschke, R.2    Stumvoll, M.3
  • 9
    • 4344571483 scopus 로고    scopus 로고
    • Agonist-dependent dissociation of human somatostatin receptor 2 dimers: A role in receptor trafficking
    • Grant, M., Collier, B. and Kumar, U. (2004). Agonist-dependent dissociation of human somatostatin receptor 2 dimers: a role in receptor trafficking. J. Biol. Chem. 279, 36179-36183.
    • (2004) J. Biol. Chem. , vol.279 , pp. 36179-36183
    • Grant, M.1    Collier, B.2    Kumar, U.3
  • 10
    • 12544250874 scopus 로고    scopus 로고
    • Phospholipase Cbeta2 binds to and inhibits phospholipase Cdelta1
    • Guo, Y., Rebecchi, M. and Scarlata, S. (2005). Phospholipase Cbeta2 binds to and inhibits phospholipase Cdelta1. J. Biol. Chem. 280, 1438-1447.
    • (2005) J. Biol. Chem. , vol.280 , pp. 1438-1447
    • Guo, Y.1    Rebecchi, M.2    Scarlata, S.3
  • 11
    • 62749096761 scopus 로고    scopus 로고
    • Protein kinase CK2 interacts with adiponectin receptor 1 and participates in adiponectin signaling
    • Heiker, J. T., Wottawah, C. M., Juhl, C., Kosel, D., Morl, K. and Beck-Sickinger, A. G. (2009). Protein kinase CK2 interacts with adiponectin receptor 1 and participates in adiponectin signaling. Cell Signal. 21, 936-942.
    • (2009) Cell Signal. , vol.21 , pp. 936-942
    • Heiker, J.T.1    Wottawah, C.M.2    Juhl, C.3    Kosel, D.4    Morl, K.5    Beck-Sickinger, A.G.6
  • 12
    • 35748982441 scopus 로고    scopus 로고
    • Functional calcitonin gene-related peptide receptors are formed by the asymmetric assembly of a calcitonin receptor-like receptor homo-oligomer and a monomer of receptor activity-modifying protein-1
    • Heroux, M., Hogue, M., Lemieux, S. and Bouvier, M. (2007). Functional calcitonin gene-related peptide receptors are formed by the asymmetric assembly of a calcitonin receptor-like receptor homo-oligomer and a monomer of receptor activity-modifying protein-1. J. Biol. Chem. 282, 31610-31620.
    • (2007) J. Biol. Chem. , vol.282 , pp. 31610-31620
    • Heroux, M.1    Hogue, M.2    Lemieux, S.3    Bouvier, M.4
  • 13
    • 33748751347 scopus 로고    scopus 로고
    • Serotonin 5-HT2C receptor homodimer biogenesis in the endoplasmic reticulum: Real-time visualization with confocal fluorescence resonance energy transfer
    • Herrick-Davis, K., Weaver, B. A., Grinde, E. and Mazurkiewicz, J. E. (2006). Serotonin 5-HT2C receptor homodimer biogenesis in the endoplasmic reticulum: real-time visualization with confocal fluorescence resonance energy transfer. J. Biol. Chem. 281, 27109-27116.
    • (2006) J. Biol. Chem. , vol.281 , pp. 27109-27116
    • Herrick-Davis, K.1    Weaver, B.A.2    Grinde, E.3    Mazurkiewicz, J.E.4
  • 14
    • 38349117500 scopus 로고    scopus 로고
    • Glycine residues G338 and G342 are important determinants for serotonin transporter dimerisation and cell surface expression
    • Horschitz, S., Lau, T. and Schloss, P. (2008). Glycine residues G338 and G342 are important determinants for serotonin transporter dimerisation and cell surface expression. Neurochem. Int. 52, 770-775.
    • (2008) Neurochem. Int. , vol.52 , pp. 770-775
    • Horschitz, S.1    Lau, T.2    Schloss, P.3
  • 15
    • 0036241055 scopus 로고    scopus 로고
    • Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation
    • Hu, C.-D., Chinenov, Y. and Kerppola, T. K. (2002). Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation. Mol. Cell 9, 789-798.
    • (2002) Mol. Cell , vol.9 , pp. 789-798
    • Hu, C.-D.1    Chinenov, Y.2    Kerppola, T.K.3
  • 16
    • 34547857813 scopus 로고    scopus 로고
    • Aromatic and cation-pi interactions enhance helix-helix association in a membrane environment
    • Johnson, R. M., Hecht, K. and Deber, C. M. (2007). Aromatic and cation-pi interactions enhance helix-helix association in a membrane environment. Biochemistry 46, 9208-9214.
    • (2007) Biochemistry , vol.46 , pp. 9208-9214
    • Johnson, R.M.1    Hecht, K.2    Deber, C.M.3
  • 17
    • 33745834319 scopus 로고    scopus 로고
    • Adiponectin and adiponectin receptors in insulin resistance, diabetes, and the metabolic syndrome
    • Kadowaki, T., Yamauchi, T., Kubota, N., Hara, K., Ueki, K. and Tobe, K. (2006). Adiponectin and adiponectin receptors in insulin resistance, diabetes, and the metabolic syndrome. J. Clin. Invest. 116, 1784-1792.
    • (2006) J. Clin. Invest. , vol.116 , pp. 1784-1792
    • Kadowaki, T.1    Yamauchi, T.2    Kubota, N.3    Hara, K.4    Ueki, K.5    Tobe, K.6
  • 18
    • 34347222583 scopus 로고    scopus 로고
    • Design and implementation of bimolecular fluorescence complementation (BiFC) assays for the visualization of protein interactions in living cells
    • Kerppola, T. K. (2006). Design and implementation of bimolecular fluorescence complementation (BiFC) assays for the visualization of protein interactions in living cells. Nat. Protoc. 1, 1278-1286.
    • (2006) Nat. Protoc. , vol.1 , pp. 1278-1286
    • Kerppola, T.K.1
  • 19
    • 43149088724 scopus 로고    scopus 로고
    • Amyloidogenic processing but not amyloid precursor protein (APP) intracellular C-terminal domain production requires a precisely oriented APP dimer assembled by transmembrane GXXXG motifs
    • Kienlen-Campard, P., Tasiaux, B., Van Hees, J., Li, M., Huysseune, S., Sato, T., Fei, J. Z., Aimoto, S., Courtoy, P. J., Smith, S. O. et al. (2008). Amyloidogenic processing but not amyloid precursor protein (APP) intracellular C-terminal domain production requires a precisely oriented APP dimer assembled by transmembrane GXXXG motifs. J. Biol. Chem. 283, 7733-7744.
    • (2008) J. Biol. Chem. , vol.283 , pp. 7733-7744
    • Kienlen-Campard, P.1    Tasiaux, B.2    Van Hees, J.3    Li, M.4    Huysseune, S.5    Sato, T.6    Fei, J.Z.7    Aimoto, S.8    Courtoy, P.J.9    Smith, S.O.10
  • 20
    • 0037160035 scopus 로고    scopus 로고
    • Ligand-dependent inhibition of oligomerization at the human thyrotropin receptor
    • Latif, R., Graves, P. and Davies, T. F. (2002). Ligand-dependent inhibition of oligomerization at the human thyrotropin receptor. J. Biol. Chem. 277, 45059-45067.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45059-45067
    • Latif, R.1    Graves, P.2    Davies, T.F.3
  • 21
    • 0027050182 scopus 로고
    • Sequence specificity in the dimerization of transmembrane alpha-helices
    • Lemmon, M. A., Flanagan, J. M., Treutlein, H. R., Zhang, J. and Engelman, D. M. (1992). Sequence specificity in the dimerization of transmembrane alpha-helices. Biochemistry 31, 12719-12725.
    • (1992) Biochemistry , vol.31 , pp. 12719-12725
    • Lemmon, M.A.1    Flanagan, J.M.2    Treutlein, H.R.3    Zhang, J.4    Engelman, D.M.5
  • 22
    • 35748954385 scopus 로고    scopus 로고
    • Heterodimerization, trafficking and membrane topology of the two proteins, Ost alpha and Ost beta, that constitute the organic solute and steroid transporter
    • Li, N., Cui, Z., Fang, F., Lee, J. Y. and Ballatori, N. (2007). Heterodimerization, trafficking and membrane topology of the two proteins, Ost alpha and Ost beta, that constitute the organic solute and steroid transporter. Biochem. J. 407, 363-372.
    • (2007) Biochem. J. , vol.407 , pp. 363-372
    • Li, N.1    Cui, Z.2    Fang, F.3    Lee, J.Y.4    Ballatori, N.5
  • 23
    • 33947362780 scopus 로고    scopus 로고
    • The {alpha}1b-adrenoceptor exists as a higher-order oligomer: Effective oligomerization is required for receptor maturation, surface delivery, and function
    • Lopez-Gimenez, J. F., Canals, M., Pediani, J. D. and Milligan, G. (2007). The {alpha}1b-adrenoceptor exists as a higher-order oligomer: effective oligomerization is required for receptor maturation, surface delivery, and function. Mol. Pharmacol. 71, 1015-1029.
    • (2007) Mol. Pharmacol. , vol.71 , pp. 1015-1029
    • Lopez-Gimenez, J.F.1    Canals, M.2    Pediani, J.D.3    Milligan, G.4
  • 24
    • 9944264993 scopus 로고    scopus 로고
    • Melanocortin receptors form constitutive homo- and heterodimers
    • Mandrika, I., Petrovska, R. and Wikberg, J. (2005). Melanocortin receptors form constitutive homo- and heterodimers. Biochem. Biophys. Res. Commun. 326, 349-354.
    • (2005) Biochem. Biophys. Res. Commun. , vol.326 , pp. 349-354
    • Mandrika, I.1    Petrovska, R.2    Wikberg, J.3
  • 26
    • 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
  • 27
    • 0032546782 scopus 로고    scopus 로고
    • pi-Stacking interactions. Alive and well in proteins
    • McGaughey, G. B., Gagne, M. and Rappe, A. K. (1998). pi-Stacking interactions. Alive and well in proteins. J. Biol. Chem. 273, 15458-15463.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15458-15463
    • McGaughey, G.B.1    Gagne, M.2    Rappe, A.K.3
  • 28
    • 40349085622 scopus 로고    scopus 로고
    • A day in the life of a G protein-coupled receptor: The contribution to function of G protein-coupled receptor dimerization
    • Milligan, G. (2008). A day in the life of a G protein-coupled receptor: the contribution to function of G protein-coupled receptor dimerization. Br. J. Pharmacol. 153, Suppl. 1, S216-S229.
    • (2008) Br. J. Pharmacol. , vol.153 , Issue.SUPPL. 1
    • Milligan, G.1
  • 29
    • 34247525991 scopus 로고    scopus 로고
    • Detection of transient protein-protein interactions by bimolecular fluorescence complementation: The Abl-SH3 case
    • Morell, M., Espargaro, A., Aviles, F. X. and Ventura, S. (2007). Detection of transient protein-protein interactions by bimolecular fluorescence complementation: the Abl-SH3 case. Proteomics 7, 1023-1036.
    • (2007) Proteomics , vol.7 , pp. 1023-1036
    • Morell, M.1    Espargaro, A.2    Aviles, F.X.3    Ventura, S.4
  • 30
    • 0036138908 scopus 로고    scopus 로고
    • A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications
    • Nagai, T., Ibata, K., Park, E. S., Kubota, M., Mikoshiba, K. and Miyawaki, A. (2002). A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nat. Biotechnol. 20, 87-90.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 87-90
    • Nagai, T.1    Ibata, K.2    Park, E.S.3    Kubota, M.4    Mikoshiba, K.5    Miyawaki, A.6
  • 31
    • 0031056665 scopus 로고    scopus 로고
    • Leptin receptor (OB-R) oligomerizes with itself but not with its closely related cytokine signal transducer gp130
    • DOI 10.1016/S0014-5793(97)00013-6, PII S0014579397000136
    • Nakashima, K., Narazaki, M. and Taga, T. (1997). Leptin receptor (OB-R) oligomerizes with itself but not with its closely related cytokine signal transducer gp130. FEBS Lett. 403, 79-82. (Pubitemid 27079813)
    • (1997) FEBS Letters , vol.403 , Issue.1 , pp. 79-82
    • Nakashima, K.1    Narazaki, M.2    Taga, T.3
  • 32
    • 33746334169 scopus 로고    scopus 로고
    • Altered fiber distribution and fiber-specific glycolytic and oxidative enzyme activity in skeletal muscle of patients with type 2 diabetes
    • Oberbach, A., Bossenz, Y., Lehmann, S., Niebauer, J., Adams, V., Paschke, R., Schon, M. R., Bluher, M. and Punkt, K. (2006). Altered fiber distribution and fiber-specific glycolytic and oxidative enzyme activity in skeletal muscle of patients with type 2 diabetes. Diabetes Care 29, 895-900.
    • (2006) Diabetes Care , vol.29 , pp. 895-900
    • Oberbach, A.1    Bossenz, Y.2    Lehmann, S.3    Niebauer, J.4    Adams, V.5    Paschke, R.6    Schon, M.R.7    Bluher, M.8    Punkt, K.9
  • 33
    • 1542467519 scopus 로고    scopus 로고
    • Oligomerization, biogenesis, and signaling is promoted by a glycophorin A-like dimerization motif in transmembrane domain 1 of a yeast G protein -coupled receptor
    • Overton, M. C., Chinault, S. L. and Blumer, K. J. (2003). Oligomerization, biogenesis, and signaling is promoted by a glycophorin A-like dimerization motif in transmembrane domain 1 of a yeast G protein -coupled receptor. J. Biol. Chem. 279, 49369-49377.
    • (2003) J. Biol. Chem. , vol.279 , pp. 49369-49377
    • Overton, M.C.1    Chinault, S.L.2    Blumer, K.J.3
  • 34
    • 34247476788 scopus 로고    scopus 로고
    • Peptides as transmembrane segments: Decrypting the determinants for helix-helix interactions in membrane proteins
    • Rath, A., Johnson, R. M. and Deber, C. M. (2007). Peptides as transmembrane segments: decrypting the determinants for helix-helix interactions in membrane proteins. Biopolymers 88, 217-232.
    • (2007) Biopolymers , vol.88 , pp. 217-232
    • Rath, A.1    Johnson, R.M.2    Deber, C.M.3
  • 35
    • 4043125390 scopus 로고    scopus 로고
    • Homodimerization of the beta2-adrenergic receptor as a prerequisite for cell surface targeting
    • Salahpour, A., Angers, S., Mercier, J. F., Lagace, M., Marullo, S. and Bouvier, M. (2004). Homodimerization of the beta2-adrenergic receptor as a prerequisite for cell surface targeting. J. Biol. Chem. 279, 33390-33397.
    • (2004) J. Biol. Chem. , vol.279 , pp. 33390-33397
    • Salahpour, A.1    Angers, S.2    Mercier, J.F.3    Lagace, M.4    Marullo, S.5    Bouvier, M.6
  • 37
    • 4143085058 scopus 로고    scopus 로고
    • Folding of helical membrane proteins: The role of polar, GxxxG-like and proline motifs
    • Senes, A., Engel, D. E. and DeGrado, W. F. (2004). Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs. Curr. Opin. Struct. Biol. 14, 465-479.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 465-479
    • Senes, A.1    Engel, D.E.2    DeGrado, W.F.3
  • 38
    • 33645219173 scopus 로고    scopus 로고
    • BAP31 is involved in the retention of cytochrome P450 2C2 in the endoplasmic reticulum
    • Szczesna-Skorupa, E. and Kemper, B. (2006). BAP31 is involved in the retention of cytochrome P450 2C2 in the endoplasmic reticulum. J. Biol. Chem. 281, 4142-4148.
    • (2006) J. Biol. Chem. , vol.281 , pp. 4142-4148
    • Szczesna-Skorupa, E.1    Kemper, B.2
  • 39
    • 1242276192 scopus 로고    scopus 로고
    • Roles of G-protein-coupled receptor dimerization
    • Terrillon, S. and Bouvier, M. (2004). Roles of G-protein-coupled receptor dimerization. EMBO Rep. 5, 30-34.
    • (2004) EMBO Rep. , vol.5 , pp. 30-34
    • Terrillon, S.1    Bouvier, M.2
  • 40
    • 33748992313 scopus 로고    scopus 로고
    • Adipocytokines: Mediators linking adipose tissue, inflammation and immunity
    • Tilg, H. and Moschen, A. R. (2006). Adipocytokines: mediators linking adipose tissue, inflammation and immunity. Nat. Rev. Immunol. 6, 772-783.
    • (2006) Nat. Rev. Immunol. , vol.6 , pp. 772-783
    • Tilg, H.1    Moschen, A.R.2
  • 42
    • 33847619358 scopus 로고    scopus 로고
    • The insulin and EGF receptor structures: New insights into ligand-induced receptor activation
    • Ward, C. W., Lawrence, M. C., Streltsov, V. A., Adams, T. E. and McKern, N. M. (2007). The insulin and EGF receptor structures: new insights into ligand-induced receptor activation. Trends Biochem. Sci. 32, 129-137.
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 129-137
    • Ward, C.W.1    Lawrence, M.C.2    Streltsov, V.A.3    Adams, T.E.4    McKern, N.M.5
  • 43
    • 0031040793 scopus 로고    scopus 로고
    • Leptin receptor (OB-R) signaling. Cytoplasmic domain mutational analysis and evidence for receptor homo-oligomerization
    • White, D. W., Kuropatwinski, K. K., Devos, R., Baumann, H. and Tartaglia, L. A. (1997). Leptin receptor (OB-R) signaling. Cytoplasmic domain mutational analysis and evidence for receptor homo-oligomerization. J. Biol. Chem. 272, 4065-4071.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4065-4071
    • White, D.W.1    Kuropatwinski, K.K.2    Devos, R.3    Baumann, H.4    Tartaglia, L.A.5
  • 45
    • 56949089685 scopus 로고    scopus 로고
    • Receptor for activated C-kinase 1, a novel binding partner of adiponectin receptor 1
    • Xu, Y., Wang, N., Ling, F., Li, P. and Gao, Y. (2009). Receptor for activated C-kinase 1, a novel binding partner of adiponectin receptor 1. Biochem. Biophys. Res. Commun. 378, 95-98.
    • (2009) Biochem. Biophys. Res. Commun. , vol.378 , pp. 95-98
    • Xu, Y.1    Wang, N.2    Ling, F.3    Li, P.4    Gao, Y.5
  • 46
    • 0036851817 scopus 로고    scopus 로고
    • Adiponectin stimulates glucose utilization and fatty-acid oxidation by activating AMP-activated protein kinase
    • Yamauchi, T., Kamon, J., Minokoshi, Y., Ito, Y., Waki, H., Uchida, S., Yamashita, S., Noda, M., Kita, S., Ueki, K. et al. (2002). Adiponectin stimulates glucose utilization and fatty-acid oxidation by activating AMP-activated protein kinase. Nat. Med. 8, 1288-1295.
    • (2002) Nat. Med. , vol.8 , pp. 1288-1295
    • Yamauchi, T.1    Kamon, J.2    Minokoshi, Y.3    Ito, Y.4    Waki, H.5    Uchida, S.6    Yamashita, S.7    Noda, M.8    Kita, S.9    Ueki, K.10
  • 49
    • 33750578279 scopus 로고    scopus 로고
    • Adiponectin increases fatty acid oxidation in skeletal muscle cells by sequential activation of AMP-activated protein kinase, p38 mitogen-activated protein kinase, and peroxisome proliferator-activated receptor alpha
    • Yoon, M. J., Lee, G. Y., Chung, J. J., Ahn, Y. H., Hong, S. H. and Kim, J. B. (2006). Adiponectin increases fatty acid oxidation in skeletal muscle cells by sequential activation of AMP-activated protein kinase, p38 mitogen-activated protein kinase, and peroxisome proliferator-activated receptor alpha. Diabetes 55, 2562-2570.
    • (2006) Diabetes , vol.55 , pp. 2562-2570
    • Yoon, M.J.1    Lee, G.Y.2    Chung, J.J.3    Ahn, Y.H.4    Hong, S.H.5    Kim, J.B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.