메뉴 건너뛰기




Volumn 288, Issue 5, 2013, Pages 3112-3125

Adiponectin receptors form homomers and heteromers exhibiting distinct ligand binding and intracellular signaling properties

Author keywords

[No Author keywords available]

Indexed keywords

ADIPONECTIN; AMP-ACTIVATED PROTEIN KINASE; C TERMINUS; CO-TRANSFECTIONS; COLOCALIZE; CYTOSOLIC; ENDOPLASMIC RETICULUM; EXPRESSION LEVELS; EXTRACELLULAR; G-PROTEIN COUPLED RECEPTORS; HETEROMERIC COMPLEXES; IMMUNOPRECIPITATIONS; INTERACTION BEHAVIOR; INTRACELLULAR SIGNALING; ISOFORMS; LIGAND BINDING; OLIGOMERIZATION PATTERNS; PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR; TRANS-MEMBRANE DOMAINS;

EID: 84873324067     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.404624     Document Type: Article
Times cited : (57)

References (56)
  • 1
    • 0042330251 scopus 로고    scopus 로고
    • Minireview. The adipocyte. At the crossroads of energy homeostasis, inflammation, and atherosclerosis
    • Rajala, M. W., and Scherer, P. E. (2003) Minireview. The adipocyte. At the crossroads of energy homeostasis, inflammation, and atherosclerosis. Endocrinology 144, 3765-3773
    • (2003) Endocrinology , vol.144 , pp. 3765-3773
    • Rajala, M.W.1    Scherer, P.E.2
  • 2
    • 0028787490 scopus 로고
    • A novel serum protein similar to C1q, produced exclusively in adipocytes
    • Scherer, P. E., Williams, S., Fogliano, M., Baldini, G., and Lodish, H. F. (1995) A novel serum protein similar to C1q, produced exclusively in adipocytes. J. Biol. Chem. 270, 26746-26749
    • (1995) J. Biol. Chem. , vol.270 , pp. 26746-26749
    • Scherer, P.E.1    Williams, S.2    Fogliano, M.3    Baldini, G.4    Lodish, H.F.5
  • 3
    • 17544382289 scopus 로고    scopus 로고
    • AdipoQ is a novel adiposespecific gene dysregulated in obesity
    • Hu, E., Liang, P., and Spiegelman, B. M. (1996) AdipoQ is a novel adiposespecific gene dysregulated in obesity. J. Biol. Chem. 271, 10697-10703
    • (1996) J. Biol. Chem. , vol.271 , pp. 10697-10703
    • Hu, E.1    Liang, P.2    Spiegelman, B.M.3
  • 4
    • 0029980285 scopus 로고    scopus 로고
    • CDNA cloning and expression of a novel adipose specific collagen-like factor, apM1 (AdiPose most abundant gene transcript 1)
    • Maeda, K., Okubo, K., Shimomura, I., Funahashi, T., Matsuzawa, Y., and Matsubara, K. (1996) cDNA cloning and expression of a novel adipose specific collagen-like factor, apM1 (AdiPose most abundant gene transcript 1). Biochem. Biophys. Res. Commun. 221, 286-289
    • (1996) Biochem. Biophys. Res. Commun. , vol.221 , pp. 286-289
    • Maeda, K.1    Okubo, K.2    Shimomura, I.3    Funahashi, T.4    Matsuzawa, Y.5    Matsubara, K.6
  • 5
    • 0029836585 scopus 로고    scopus 로고
    • Isolation and characterization of GBP28, a novel gelatin-binding protein purified from human plasma
    • Nakano, Y., Tobe, T., Choi-Miura, N. H., Mazda, T., and Tomita, M. (1996) Isolation and characterization of GBP28, a novel gelatin-binding protein purified from human plasma. J. Biochem. 120, 803-812
    • (1996) J. Biochem. , vol.120 , pp. 803-812
    • Nakano, Y.1    Tobe, T.2    Choi-Miura, N.H.3    Mazda, T.4    Tomita, M.5
  • 6
    • 18844432308 scopus 로고    scopus 로고
    • Adiponectin and adiponectin receptors
    • Kadowaki, T., and Yamauchi, T. (2005) Adiponectin and adiponectin receptors. Endocr. Rev. 26, 439-451
    • (2005) Endocr. Rev. , vol.26 , pp. 439-451
    • Kadowaki, T.1    Yamauchi, T.2
  • 7
    • 81855177709 scopus 로고    scopus 로고
    • Adiponectin and cardiovascular health. An update
    • Hui, X., Lam, K. S., Vanhoutte, P. M., and Xu, A. (2012) Adiponectin and cardiovascular health. An update. Br. J. Pharmacol. 165, 574-590
    • (2012) Br. J. Pharmacol. , vol.165 , pp. 574-590
    • Hui, X.1    Lam, K.S.2    Vanhoutte, P.M.3    Xu, A.4
  • 8
    • 79952709927 scopus 로고    scopus 로고
    • Regulation ofvascular tone by adipocytes
    • Maenhaut, N., and Van De Voorde, J. (2011) Regulation ofvascular tone by adipocytes. BMC Med. 9, 25
    • (2011) BMC Med. , vol.9 , pp. 25
    • Maenhaut, N.1    Van De Voorde, J.2
  • 10
    • 84858268902 scopus 로고    scopus 로고
    • Adiponectin and adipocyte fatty acid binding protein in the pathogenesis of cardiovascular disease
    • Xu, A., and Vanhoutte, P. M. (2012) Adiponectin and adipocyte fatty acid binding protein in the pathogenesis of cardiovascular disease. Am. J. Physiol. Heart Circ. Physiol. 302, H1231-H1240
    • (2012) Am. J. Physiol. Heart Circ. Physiol. , vol.302
    • Xu, A.1    Vanhoutte, P.M.2
  • 12
    • 84655175093 scopus 로고    scopus 로고
    • Adiponectin and breast cancer
    • Chen, X., and Wang, Y. (2011) Adiponectin and breast cancer. Med. Oncol. 28, 1288-1295
    • (2011) Med. Oncol. , vol.28 , pp. 1288-1295
    • Chen, X.1    Wang, Y.2
  • 13
    • 84866079242 scopus 로고    scopus 로고
    • The role of adiponectin in cancer. A review of current evidence
    • Dalamaga, M., Diakopoulos, K. N., and Mantzoros, C. S. (2012) The role of adiponectin in cancer. A review of current evidence. Endocr. Rev. 33, 547-594
    • (2012) Endocr. Rev. , vol.33 , pp. 547-594
    • Dalamaga, M.1    Diakopoulos, K.N.2    Mantzoros, C.S.3
  • 14
    • 0347379841 scopus 로고    scopus 로고
    • Role of disulfide bonds in Acrp30/adiponectin structure and signaling specificity. Different oligomers activate different signal transduction pathways
    • Tsao, T. S., Tomas, E., Murrey, H. E., Hug, C., Lee, D. H., Ruderman, N. B., Heuser, J. E., and Lodish, H. F. (2003) Role of disulfide bonds in Acrp30/adiponectin structure and signaling specificity. Different oligomers activate different signal transduction pathways. J. Biol. Chem. 278, 50810-50817
    • (2003) J. Biol. Chem. , vol.278 , pp. 50810-50817
    • Tsao, T.S.1    Tomas, E.2    Murrey, H.E.3    Hug, C.4    Lee, D.H.5    Ruderman, N.B.6    Heuser, J.E.7    Lodish, H.F.8
  • 17
    • 77957769313 scopus 로고    scopus 로고
    • Adiponectin receptor binding proteins. Recent advances in elucidating adiponectin signalling pathways
    • Buechler, C, Wanninger, J., and Neumeier, M. (2010) Adiponectin receptor binding proteins. Recent advances in elucidating adiponectin signalling pathways. FEBS Lett. 584, 4280-4286
    • (2010) FEBS Lett. , vol.584 , pp. 4280-4286
    • Buechler, C.1    Wanninger, J.2    Neumeier, M.3
  • 19
    • 55249090400 scopus 로고    scopus 로고
    • The adiponectin receptors AdipoR1 and AdipoR2 activate ERK1/2 through a Src/Ras-dependent pathway and stimulate cell growth
    • Lee, M. H., Klein, R. L., El-Shewy, H. M., Luttrell, D. K., and Luttrell, L. M. (2008) The adiponectin receptors AdipoR1 and AdipoR2 activate ERK1/2 through a Src/Ras-dependent pathway and stimulate cell growth. Biochemistry 47, 11682-11692
    • (2008) Biochemistry , vol.47 , pp. 11682-11692
    • Lee, M.H.1    Klein, R.L.2    El-Shewy, H.M.3    Luttrell, D.K.4    Luttrell, L.M.5
  • 22
    • 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
  • 23
    • 3142761477 scopus 로고    scopus 로고
    • T-cadherin is a receptor for hexameric and high molecular weight forms of Acrp30/adiponectin
    • Hug, C, Wang, J., Ahmad, N. S., Bogan, J. S., Tsao, T. S., and Lodish, H. F. (2004) T-cadherin is a receptor for hexameric and high molecular weight forms of Acrp30/adiponectin. Proc. Natl. Acad. Sci. U. S. A. 101, 10308-10313
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 10308-10313
    • Hug, C.1    Wang, J.2    Ahmad, N.S.3    Bogan, J.S.4    Tsao, T.S.5    Lodish, H.F.6
  • 24
    • 48149095486 scopus 로고    scopus 로고
    • The insulin receptor. A prototype for dimeric, allosteric membrane receptors?
    • De Meyts, P. (2008) The insulin receptor. A prototype for dimeric, allosteric membrane receptors? Trends Biochem. Sci. 33, 376-384
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 376-384
    • De Meyts, P.1
  • 25
  • 27
    • 33748459957 scopus 로고    scopus 로고
    • Measurement of FRET efficiency and ratio of donor to acceptor concentration in living cells
    • Chen, H., Puhl, H. L., 3rd, Koushik, S. V., Vogel, S. S., and Ikeda, S. R. (2006) Measurement of FRET efficiency and ratio of donor to acceptor concentration in living cells. Biophys. J. 91, L39-L41
    • (2006) Biophys. J. , vol.91
    • Chen, H.1    Puhl III, H.L.2    Koushik, S.V.3    Vogel, S.S.4    Ikeda, S.R.5
  • 28
    • 26844569694 scopus 로고    scopus 로고
    • PixFRET, an ImageJ plug-in for FRET calculation that can accommodate variations in spectral bleed-throughs
    • Feige, J. N, Sage, D., Wahli, W., Desvergne, B., and Gelman, L. (2005) PixFRET, an ImageJ plug-in for FRET calculation that can accommodate variations in spectral bleed-throughs. Microsc. Res. Tech. 68, 51-58
    • (2005) Microsc. Res. Tech. , vol.68 , pp. 51-58
    • Feige, J.N.1    Sage, D.2    Wahli, W.3    Desvergne, B.4    Gelman, L.5
  • 29
    • 0031956092 scopus 로고    scopus 로고
    • Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy
    • Gordon, G. W., Berry, G., Liang, X. H., Levine, B., and Herman, B. (1998) Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy. Biophys. J. 74, 2702-2713
    • (1998) Biophys. J. , vol.74 , pp. 2702-2713
    • Gordon, G.W.1    Berry, G.2    Liang, X.H.3    Levine, B.4    Herman, B.5
  • 30
    • 0034810232 scopus 로고    scopus 로고
    • Reliable and global measurement of fluorescence resonance energy transfer using fluorescence microscopes
    • Xia, Z., and Liu, Y. (2001) Reliable and global measurement of fluorescence resonance energy transfer using fluorescence microscopes. Biophys. J. 81, 2395-2402
    • (2001) Biophys. J. , vol.81 , pp. 2395-2402
    • Xia, Z.1    Liu, Y.2
  • 31
    • 0038729670 scopus 로고    scopus 로고
    • Measurement of the millisecond activation switch of G proteincoupled receptors in living cells
    • Vilardaga, J. P., Bünemann, M., Krasel, C, Castro, M., and Lohse, M. J. (2003) Measurement of the millisecond activation switch of G proteincoupled receptors in living cells. Nat. Biotechnol. 21, 807-812
    • (2003) Nat. Biotechnol. , vol.21 , pp. 807-812
    • Vilardaga, J.P.1    Bünemann, M.2    Krasel, C.3    Castro, M.4    Lohse, M.J.5
  • 32
    • 0036669824 scopus 로고    scopus 로고
    • Measuring protein conformational changes by FRET/LRET
    • Heyduk, T. (2002) Measuring protein conformational changes by FRET/LRET. Curr. Opin. Biotechnol. 13, 292-296
    • (2002) Curr. Opin. Biotechnol. , vol.13 , pp. 292-296
    • Heyduk, T.1
  • 33
    • 0035930602 scopus 로고    scopus 로고
    • Agonist-dependent dissociation of oligomeric complexes of G protein-coupled cholecystokinin receptors demonstrated in living cells using bioluminescence resonance energy transfer
    • Cheng, Z. J., and Miller, L. J. (2001) Agonist-dependent dissociation of oligomeric complexes of G protein-coupled cholecystokinin receptors demonstrated in living cells using bioluminescence resonance energy transfer. J. Biol. Chem. 276, 48040-48047
    • (2001) J. Biol. Chem. , vol.276 , pp. 48040-48047
    • Cheng, Z.J.1    Miller, L.J.2
  • 34
    • 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
  • 36
    • 69249206623 scopus 로고    scopus 로고
    • G protein-coupled receptor hetero-dimerization. Contribution to pharmacology and function
    • Milligan, G. (2009) G protein-coupled receptor hetero-dimerization. Contribution to pharmacology and function. Br J. Pharmacol. 158, 5-14
    • (2009) Br J. Pharmacol. , vol.158 , pp. 5-14
    • Milligan, G.1
  • 37
    • 73049085563 scopus 로고    scopus 로고
    • The asymmetric/symmetric activation of GPCR dimers as a possible mechanistic rationale for multiple signalling pathways
    • Rovira, X., Pin, J. P., and Giraldo, J. (2010) The asymmetric/symmetric activation of GPCR dimers as a possible mechanistic rationale for multiple signalling pathways. Trends Pharmacol. Sci. 31, 15-21
    • (2010) Trends Pharmacol. Sci. , vol.31 , pp. 15-21
    • Rovira, X.1    Pin, J.P.2    Giraldo, J.3
  • 38
    • 0242572132 scopus 로고    scopus 로고
    • Dimerization of G-protein-coupled receptors: Roles in signal transduction
    • Bai, M. (2004) Dimerization of G-protein-coupled receptors: roles in signal transduction. Cell. Signal. 16, 175-186
    • (2004) Cell. Signal. , vol.16 , pp. 175-186
    • Bai, M.1
  • 39
    • 84868547684 scopus 로고    scopus 로고
    • Quantitative intensity-based FRET approaches. A comparative snapshot
    • Zeug, A., Woehler, A., Neher, E., and Ponimaskin, E. G. (2012) Quantitative intensity-based FRET approaches. A comparative snapshot. Biophys. J. 103, 1821-1827
    • (2012) Biophys. J. , vol.103 , pp. 1821-1827
    • Zeug, A.1    Woehler, A.2    Neher, E.3    Ponimaskin, E.G.4
  • 41
    • 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
  • 42
    • 4043125390 scopus 로고    scopus 로고
    • Homodimerization of the β2-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 β2-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
  • 43
    • 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
  • 44
    • 0030760634 scopus 로고    scopus 로고
    • Dimerization of the delta opioid receptor. Implication for a role in receptor internalization
    • Cvejic, S., and Devi, L. A. (1997) Dimerization of the delta opioid receptor. Implication for a role in receptor internalization. J. Biol. Chem. 272, 26959-26964
    • (1997) J. Biol. Chem. , vol.272 , pp. 26959-26964
    • Cvejic, S.1    Devi, L.A.2
  • 45
    • 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
  • 46
    • 43749115484 scopus 로고    scopus 로고
    • Dimerization of G protein-coupled receptors: New avenues for somatostatin receptor signalling, control, and functioning
    • Duran-Prado, M., Malagon, M. M., Gracia-Navarro, F., and Castano, J. P. (2008) Dimerization of G protein-coupled receptors: new avenues for somatostatin receptor signalling, control, and functioning. Mol. Cell. Endocrinol. 286, 63-68
    • (2008) Mol. Cell. Endocrinol. , vol.286 , pp. 63-68
    • Duran-Prado, M.1    Malagon, M.M.2    Gracia-Navarro, F.3    Castano, J.P.4
  • 47
    • 79953802623 scopus 로고    scopus 로고
    • Separation and reformation of cell surface dopamine receptor oligomers visualized in cells
    • O'Dowd, B. F., Ji, X., Alijaniaram, M., Nguyen, T., and George, S. R. (2011) Separation and reformation of cell surface dopamine receptor oligomers visualized in cells. Eur. J. Pharmacol. 658, 74-83
    • (2011) Eur. J. Pharmacol. , vol.658 , pp. 74-83
    • O'Dowd, B.F.1    Ji, X.2    Alijaniaram, M.3    Nguyen, T.4    George, S.R.5
  • 48
    • 0032101983 scopus 로고    scopus 로고
    • G-protein-coupled receptors. Turn-ons and turn-offs
    • Carman, C. V., and Benovic, J. L. (1998) G-protein-coupled receptors. Turn-ons and turn-offs. Curr. Opin. Neurobiol. 8, 335-344
    • (1998) Curr. Opin. Neurobiol. , vol.8 , pp. 335-344
    • Carman, C.V.1    Benovic, J.L.2
  • 49
    • 0035252096 scopus 로고    scopus 로고
    • Role of endocytosis in mediating down-regulation of G-protein-coupled receptors
    • Tsao, P., Cao, T., and Von Zastrow, M. (2001) Role of endocytosis in mediating down-regulation of G-protein-coupled receptors. Trends Pharmacol. Sci. 22, 91-96
    • (2001) Trends Pharmacol. Sci. , vol.22 , pp. 91-96
    • Tsao, P.1    Cao, T.2    Von Zastrow, M.3
  • 50
    • 0034646719 scopus 로고    scopus 로고
    • Type-specific sorting of G proteincoupled receptors after endocytosis
    • Tsao, P. I., and Von Zastrow, M. (2000) Type-specific sorting of G proteincoupled receptors after endocytosis. J. Biol. Chem. 275, 11130-11140
    • (2000) J. Biol. Chem. , vol.275 , pp. 11130-11140
    • Tsao, P.I.1    Von Zastrow, M.2
  • 51
    • 36749011973 scopus 로고    scopus 로고
    • Circulating adiponectin and adiponectin receptor expression in skeletal muscle. Effects of exercise
    • Vu, V., Riddell, M. C, and Sweeney, G. (2007) Circulating adiponectin and adiponectin receptor expression in skeletal muscle. effects of exercise. Diabetes Metab. Res. Rev. 23, 600-611
    • (2007) Diabetes Metab. Res. Rev. , vol.23 , pp. 600-611
    • Vu, V.1    Riddell, M.C.2    Sweeney, G.3
  • 53
    • 58149499174 scopus 로고    scopus 로고
    • Physiological and pathophysiological roles of adiponectin and adiponectin receptors in the integrated regulation of metabolic and cardiovascular diseases
    • Yamauchi, T., and Kadowaki, T. (2008) Physiological and pathophysiological roles of adiponectin and adiponectin receptors in the integrated regulation of metabolic and cardiovascular diseases. Int. J. Obes. 32, S13-S18
    • (2008) Int. J. Obes. , vol.32
    • Yamauchi, T.1    Kadowaki, T.2
  • 55
    • 33644664433 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor PPARa activation increases adiponectin receptors and reduces obesity-related inflammation in adipose tissue. Comparison of activation of PPARa, PPAR7, and their combination
    • Tsuchida, An., Yamauchi, T., Takekawa, S., Hada, Y., Ito, Y., Maki, T., and Kadowaki, T. (2005) Peroxisome proliferator-activated receptor PPARa activation increases adiponectin receptors and reduces obesity-related inflammation in adipose tissue. Comparison of activation of PPARa, PPAR7, and their combination. Diabetes 54, 3358-3370
    • (2005) Diabetes , vol.54 , pp. 3358-3370
    • Tsuchida, A.1    Yamauchi, T.2    Takekawa, S.3    Hada, Y.4    Ito, Y.5    Maki, T.6    Kadowaki, T.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.