메뉴 건너뛰기




Volumn 392, Issue 2, 2010, Pages 234-239

ERp46 binds to AdipoR1, but not AdipoR2, and modulates adiponectin signalling

Author keywords

Adiponectin; AdipoR1; AMPK; ERp46; p38MAPK

Indexed keywords

ADENYLATE KINASE; ADIPONECTIN; ADIPONECTIN RECEPTOR 1; ADIPONECTIN RECEPTOR 2; CALNEXIN; FIBROBLAST GROWTH FACTOR RECEPTOR 3; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE P38; PROTEIN APPL1; PROTEIN CK2B; PROTEIN P46; RECEPTOR FOR ACTIVATED C KINASE 1; UNCLASSIFIED DRUG;

EID: 75749115950     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.01.029     Document Type: Article
Times cited : (59)

References (29)
  • 1
    • 33747356154 scopus 로고    scopus 로고
    • Adipose tissue: from lipid storage compartment to endocrine organ
    • Scherer P.E. Adipose tissue: from lipid storage compartment to endocrine organ. Diabetes 55 (2006) 1537-1545
    • (2006) Diabetes , vol.55 , pp. 1537-1545
    • Scherer, P.E.1
  • 3
    • 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. Physiological and pathophysiological roles of adiponectin and adiponectin receptors in the integrated regulation of metabolic and cardiovascular diseases. Int. J. Obes. 32 (2008) S13-S18
    • (2008) Int. J. Obes. , vol.32
    • Yamauchi, T.1    Kadowaki, T.2
  • 9
    • 34248147538 scopus 로고    scopus 로고
    • Adiponectin-induced eNOS activation and nitric oxide production are mediated by APPL1 in endothelial cells
    • Cheng K.K., Lam K.S., Wang Y., Yu H., Carling D., Wu D., Wong C., and Xu A. Adiponectin-induced eNOS activation and nitric oxide production are mediated by APPL1 in endothelial cells. Diabetes 56 (2007) 1387-1394
    • (2007) Diabetes , vol.56 , pp. 1387-1394
    • Cheng, K.K.1    Lam, K.S.2    Wang, Y.3    Yu, H.4    Carling, D.5    Wu, D.6    Wong, C.7    Xu, A.8
  • 11
    • 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. Receptor for activated C-kinase 1, a novel binding partner of adiponectin receptor 1. Biochem. Biophys. Res. Commun. 378 (2009) 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
  • 12
    • 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. Protein kinase CK2 interacts with adiponectin receptor 1 and participates in adiponectin signaling. Cell Signal. 21 (2009) 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
  • 14
    • 0344443678 scopus 로고    scopus 로고
    • EndoPDI, a novel protein-disulfide isomerase-like protein that is preferentially expressed in endothelial cells acts as a stress survival factor
    • Sullivan D.C., Huminiecki L., Moore J.W., Boyle J.J., Poulsom R., Creamer D., Barker J., and Bicknell R. EndoPDI, a novel protein-disulfide isomerase-like protein that is preferentially expressed in endothelial cells acts as a stress survival factor. J. Biol. Chem. 278 (2003) 47079-47088
    • (2003) J. Biol. Chem. , vol.278 , pp. 47079-47088
    • Sullivan, D.C.1    Huminiecki, L.2    Moore, J.W.3    Boyle, J.J.4    Poulsom, R.5    Creamer, D.6    Barker, J.7    Bicknell, R.8
  • 15
    • 1642473164 scopus 로고    scopus 로고
    • Identification of a novel thioredoxin-related protein, PC-TRP, which is preferentially expressed in plasma cells
    • Wrammert J., Källberg E., and Leanderson T. Identification of a novel thioredoxin-related protein, PC-TRP, which is preferentially expressed in plasma cells. Eur. J. Immunol. 34 (2004) 137-146
    • (2004) Eur. J. Immunol. , vol.34 , pp. 137-146
    • Wrammert, J.1    Källberg, E.2    Leanderson, T.3
  • 17
    • 33745365666 scopus 로고    scopus 로고
    • The subcellular fractionation properties and function of insulin receptor substrate-1 (IRS-1) are independent of cytoskeletal integrity
    • Thomas E.C., Zhe Y., Molero J.C., Schmitz-Peiffer C., Ramm G., James D.E., and Whitehead J.P. The subcellular fractionation properties and function of insulin receptor substrate-1 (IRS-1) are independent of cytoskeletal integrity. Int. J. Biochem. Cell Biol. 38 (2006) 1686-1699
    • (2006) Int. J. Biochem. Cell Biol. , vol.38 , pp. 1686-1699
    • Thomas, E.C.1    Zhe, Y.2    Molero, J.C.3    Schmitz-Peiffer, C.4    Ramm, G.5    James, D.E.6    Whitehead, J.P.7
  • 18
    • 0025779079 scopus 로고
    • Protein synthesis inhibitors activate glucose transport without increasing plasma membrane glucose transporters in 3T3-L1 adipocytes
    • Clancy B.M., Harrison S.A., Buxton J.M., and Czech M.P. Protein synthesis inhibitors activate glucose transport without increasing plasma membrane glucose transporters in 3T3-L1 adipocytes. J. Biol. Chem. 266 (1991) 10122-10130
    • (1991) J. Biol. Chem. , vol.266 , pp. 10122-10130
    • Clancy, B.M.1    Harrison, S.A.2    Buxton, J.M.3    Czech, M.P.4
  • 19
    • 33745664785 scopus 로고    scopus 로고
    • Adiponectin multimerisation is dependent on conserved lysines in the collagenous domain: Evidence for regulation of multimerisation by alterations in post-translational modifications
    • Richards A.A., Stephens T., Charlton H.K., Jones A., Macdonald G.A., Prins J.B., and Whitehead J.P. Adiponectin multimerisation is dependent on conserved lysines in the collagenous domain: Evidence for regulation of multimerisation by alterations in post-translational modifications. Mol. Endocrinol. 20 (2006) 1673-1687
    • (2006) Mol. Endocrinol. , vol.20 , pp. 1673-1687
    • Richards, A.A.1    Stephens, T.2    Charlton, H.K.3    Jones, A.4    Macdonald, G.A.5    Prins, J.B.6    Whitehead, J.P.7
  • 21
    • 0036836665 scopus 로고    scopus 로고
    • Proteins of the PDI family: unpredicted non-ER locations and functions
    • Turano C., Coppari S., Altieri F., and Ferraro A. Proteins of the PDI family: unpredicted non-ER locations and functions. J Cell. Physiol. 193 (2002) 154-163
    • (2002) J Cell. Physiol. , vol.193 , pp. 154-163
    • Turano, C.1    Coppari, S.2    Altieri, F.3    Ferraro, A.4
  • 22
    • 34247265428 scopus 로고    scopus 로고
    • Adiponectin sensitizes insulin signaling by reducing p70 S6 kinase-mediated serine phosphorylation of IRS-1
    • Wang C., Mao X., Wang L., Liu M., Wetzel M.D., Guan K.-L., Dong L.Q., and Liu F. Adiponectin sensitizes insulin signaling by reducing p70 S6 kinase-mediated serine phosphorylation of IRS-1. J. Biol. Chem. 282 (2007) 7991-7996
    • (2007) J. Biol. Chem. , vol.282 , pp. 7991-7996
    • Wang, C.1    Mao, X.2    Wang, L.3    Liu, M.4    Wetzel, M.D.5    Guan, K.-L.6    Dong, L.Q.7    Liu, F.8
  • 24
    • 24044453711 scopus 로고    scopus 로고
    • Proteomic profiling of hepatic endoplasmic reticulum-associated proteins in an animal model of insulin resistance and metabolic dyslipidemia
    • Morand J.P., Macri J., and Adeli K. Proteomic profiling of hepatic endoplasmic reticulum-associated proteins in an animal model of insulin resistance and metabolic dyslipidemia. J. Biol. Chem. 280 (2005) 17626-17633
    • (2005) J. Biol. Chem. , vol.280 , pp. 17626-17633
    • Morand, J.P.1    Macri, J.2    Adeli, K.3
  • 25
    • 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. The adiponectin receptors AdipoR1 and AdipoR2 activate ERK1/2 through a Src/Ras-dependent pathway and stimulate cell growth. Biochemistry 47 (2008) 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
  • 26
    • 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. 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 (2006) 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
  • 27
    • 70350452142 scopus 로고    scopus 로고
    • Adiponectin increases motility of human prostate cancer cells via adipoR, p38
    • Tang C.H., and Lu M.E. Adiponectin increases motility of human prostate cancer cells via adipoR, p38. AMPK, and NF-kappaB pathways. Prostate 69 (2009) 1781-17879
    • (2009) AMPK, and NF-kappaB pathways. Prostate , vol.69 , pp. 1781-17879
    • Tang, C.H.1    Lu, M.E.2
  • 29
    • 61849184242 scopus 로고    scopus 로고
    • Endocytosis of adiponectin receptor 1 through a clathrin- and Rab5-dependent pathway
    • Ding Q., Wang Z., and Chen Y. Endocytosis of adiponectin receptor 1 through a clathrin- and Rab5-dependent pathway. Cell Res. 19 (2009) 317-327
    • (2009) Cell Res. , vol.19 , pp. 317-327
    • Ding, Q.1    Wang, Z.2    Chen, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.