메뉴 건너뛰기




Volumn 566, Issue , 2014, Pages 231-235

Role of FK506 binding protein 12 in morphine-induced μ-opioid receptor internalization and desensitization

Author keywords

Opioid receptor; Desensitization; FK506 binding protein 12; Internalization; Morphine

Indexed keywords

ADENYLATE CYCLASE; CIS TRANS ISOMERASE; FK 506 BINDING PROTEIN; FK 506 BINDING PROTEIN 12; GUANINE NUCLEOTIDE BINDING PROTEIN; MORPHINE; MU OPIATE RECEPTOR; PROTEIN KINASE C; SMALL INTERFERING RNA; TACROLIMUS; UNCLASSIFIED DRUG;

EID: 84897885475     PISSN: 03043940     EISSN: 18727972     Source Type: Journal    
DOI: 10.1016/j.neulet.2014.02.059     Document Type: Article
Times cited : (9)

References (33)
  • 1
    • 0033013383 scopus 로고    scopus 로고
    • Opioids: first lessons from knockout mice
    • Kieffer B.L. Opioids: first lessons from knockout mice. Trends Pharmacol. Sci. 1999, 20:19-26.
    • (1999) Trends Pharmacol. Sci. , vol.20 , pp. 19-26
    • Kieffer, B.L.1
  • 2
    • 0035101820 scopus 로고    scopus 로고
    • Evolving concepts in G protein-coupled receptor endocytosis: the role in receptor desensitization and signaling
    • Ferguson S.S. Evolving concepts in G protein-coupled receptor endocytosis: the role in receptor desensitization and signaling. Pharmacol. Rev. 2001, 53:1-24.
    • (2001) Pharmacol. Rev. , vol.53 , pp. 1-24
    • Ferguson, S.S.1
  • 3
    • 0036895747 scopus 로고    scopus 로고
    • Differential mechanisms of morphine antinociceptive tolerance revealed in beta arrestin-2 knock-out mice
    • Bohn L.M., Lefkowitz R.J., Caron M.G. Differential mechanisms of morphine antinociceptive tolerance revealed in beta arrestin-2 knock-out mice. J. Neurosci. 2002, 22:10494-10500.
    • (2002) J. Neurosci. , vol.22 , pp. 10494-10500
    • Bohn, L.M.1    Lefkowitz, R.J.2    Caron, M.G.3
  • 4
    • 37349090553 scopus 로고    scopus 로고
    • Arrestin-dependent {μ}-opioid receptor-activated extracellular signal-regulated kinases (ERKs) translocate to nucleus in contrast to G protein-dependent ERK activation
    • Zheng H., Loh H.H., Law P.-Y. Arrestin-dependent {μ}-opioid receptor-activated extracellular signal-regulated kinases (ERKs) translocate to nucleus in contrast to G protein-dependent ERK activation. Mol. Pharmacol. 2008, 73:178-190.
    • (2008) Mol. Pharmacol. , vol.73 , pp. 178-190
    • Zheng, H.1    Loh, H.H.2    Law, P.-Y.3
  • 5
    • 0037146929 scopus 로고    scopus 로고
    • Prolonged reversal of morphine tolerance with no reversal of dependence by protein kinase C inhibitors
    • Smith F.L., Javed R., Elzey M.J., Welch S.P., Selley D., Sim-Selley L., Dewey W.L. Prolonged reversal of morphine tolerance with no reversal of dependence by protein kinase C inhibitors. Brain Res. 2002, 958:28-35.
    • (2002) Brain Res. , vol.958 , pp. 28-35
    • Smith, F.L.1    Javed, R.2    Elzey, M.J.3    Welch, S.P.4    Selley, D.5    Sim-Selley, L.6    Dewey, W.L.7
  • 6
    • 58449100187 scopus 로고    scopus 로고
    • Role of protein kinase C and μ-opioid receptor (MOPr) desensitization in tolerance to morphine in rat locus coeruleus neurons
    • Bailey C.P., Llorente J., Gabra B.H., Smith F.L., Dewey W.L., Kelly E., Henderson G. Role of protein kinase C and μ-opioid receptor (MOPr) desensitization in tolerance to morphine in rat locus coeruleus neurons. Eur. J. Neurosci. 2009, 29:307-318.
    • (2009) Eur. J. Neurosci. , vol.29 , pp. 307-318
    • Bailey, C.P.1    Llorente, J.2    Gabra, B.H.3    Smith, F.L.4    Dewey, W.L.5    Kelly, E.6    Henderson, G.7
  • 7
    • 0141814986 scopus 로고    scopus 로고
    • Mu-opioid receptor desensitization: role of receptor phosphorylation, internalization, and representation
    • Qiu Y., Law P.Y., Loh H.H. Mu-opioid receptor desensitization: role of receptor phosphorylation, internalization, and representation. J. Biol. Chem. 2003, 278:36733-36739.
    • (2003) J. Biol. Chem. , vol.278 , pp. 36733-36739
    • Qiu, Y.1    Law, P.Y.2    Loh, H.H.3
  • 9
    • 0033179904 scopus 로고    scopus 로고
    • Functional dissociation of μ opioid receptor signaling and endocytosis: implications for the biology of opiate tolerance and addiction
    • Whistler J.L., Chuang H.H., Chu P., Jan L.Y., von Zastrow M. Functional dissociation of μ opioid receptor signaling and endocytosis: implications for the biology of opiate tolerance and addiction. Neuron 1999, 23:737-746.
    • (1999) Neuron , vol.23 , pp. 737-746
    • Whistler, J.L.1    Chuang, H.H.2    Chu, P.3    Jan, L.Y.4    von Zastrow, M.5
  • 10
    • 0037169345 scopus 로고    scopus 로고
    • Regulation of opioid receptor trafficking and morphine tolerance by receptor oligomerization
    • He L., Fong J., von Zastrow M., Whistler J.L. Regulation of opioid receptor trafficking and morphine tolerance by receptor oligomerization. Cell 2002, 108:271-282.
    • (2002) Cell , vol.108 , pp. 271-282
    • He, L.1    Fong, J.2    von Zastrow, M.3    Whistler, J.L.4
  • 11
    • 33845913776 scopus 로고    scopus 로고
    • Interaction of the μ-opioid receptor with synaptophysin influences receptor trafficking and signaling
    • Liang Y.J., Wu D.F., Yang L.Q., Hollt V., Koch T. Interaction of the μ-opioid receptor with synaptophysin influences receptor trafficking and signaling. Mol. Pharmacol. 2007, 71:123-131.
    • (2007) Mol. Pharmacol. , vol.71 , pp. 123-131
    • Liang, Y.J.1    Wu, D.F.2    Yang, L.Q.3    Hollt, V.4    Koch, T.5
  • 12
    • 0038322031 scopus 로고    scopus 로고
    • ADP-ribosylation factor-dependent phospholipase D2 activation is required for agonist-induced μ-opioid receptor endocytosis
    • Koch T., Brandenburg L.O., Schulz S., Liang Y., Klein J., Hollt V. ADP-ribosylation factor-dependent phospholipase D2 activation is required for agonist-induced μ-opioid receptor endocytosis. J. Biol. Chem. 2003, 278:9979-9985.
    • (2003) J. Biol. Chem. , vol.278 , pp. 9979-9985
    • Koch, T.1    Brandenburg, L.O.2    Schulz, S.3    Liang, Y.4    Klein, J.5    Hollt, V.6
  • 13
    • 34547581105 scopus 로고    scopus 로고
    • Membrane glycoprotein M6a interacts with the μ-opioid receptor and facilitates receptor endocytosis and recycling
    • Wu D.F., Koch T., Liang Y.J., Stumm R., Schulz S., Schroder H., Hollt V. Membrane glycoprotein M6a interacts with the μ-opioid receptor and facilitates receptor endocytosis and recycling. J. Biol. Chem. 2007, 282:22239-22247.
    • (2007) J. Biol. Chem. , vol.282 , pp. 22239-22247
    • Wu, D.F.1    Koch, T.2    Liang, Y.J.3    Stumm, R.4    Schulz, S.5    Schroder, H.6    Hollt, V.7
  • 14
    • 73649133635 scopus 로고    scopus 로고
    • GRIN1 regulates μ-opioid receptor activities by tethering the receptor and G protein in the lipid raft
    • Ge X., Qiu Y., Loh H.H., Law P.Y. GRIN1 regulates μ-opioid receptor activities by tethering the receptor and G protein in the lipid raft. J. Biol. Chem. 2009, 284:36521-36534.
    • (2009) J. Biol. Chem. , vol.284 , pp. 36521-36534
    • Ge, X.1    Qiu, Y.2    Loh, H.H.3    Law, P.Y.4
  • 15
    • 84890597813 scopus 로고    scopus 로고
    • FK506-binding protein 12 modulates μ-opioid receptor phosphorylation and protein kinase C{varepsilon}-dependent signaling by its direct interaction with the receptor
    • Qiu Y., Zhao W., Wang Y., Xu J.R., Huie E., Jiang S., Yan Y.H., Loh H.H., Chen H.Z., Law P.Y. FK506-binding protein 12 modulates μ-opioid receptor phosphorylation and protein kinase C{varepsilon}-dependent signaling by its direct interaction with the receptor. Mol. Pharmacol. 2014, 85:37-49.
    • (2014) Mol. Pharmacol. , vol.85 , pp. 37-49
    • Qiu, Y.1    Zhao, W.2    Wang, Y.3    Xu, J.R.4    Huie, E.5    Jiang, S.6    Yan, Y.H.7    Loh, H.H.8    Chen, H.Z.9    Law, P.Y.10
  • 16
    • 0026649497 scopus 로고
    • PPIase catalysis by human FK506-binding protein proceeds through a conformational twist mechanism
    • Park S.T., Aldape R.A., Futer O., DeCenzo M.T., Livingston D.J. PPIase catalysis by human FK506-binding protein proceeds through a conformational twist mechanism. J. Biol. Chem. 1992, 267:3316-3324.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3316-3324
    • Park, S.T.1    Aldape, R.A.2    Futer, O.3    DeCenzo, M.T.4    Livingston, D.J.5
  • 18
    • 47249145512 scopus 로고    scopus 로고
    • Analysis of FK506-mediated protection in an organotypic model of spinal cord damage: heat shock protein 70 levels are modulated in microglial cells
    • Guzman-Lenis M.S., Vallejo C., Navarro X., Casas C. Analysis of FK506-mediated protection in an organotypic model of spinal cord damage: heat shock protein 70 levels are modulated in microglial cells. Neuroscience 2008, 155:104-113.
    • (2008) Neuroscience , vol.155 , pp. 104-113
    • Guzman-Lenis, M.S.1    Vallejo, C.2    Navarro, X.3    Casas, C.4
  • 20
    • 45249118270 scopus 로고    scopus 로고
    • FK506 binding protein 12 differentially accelerates fibril formation of wild type alpha-synuclein and its clinical mutants A30P or A53T
    • Gerard M., Debyser Z., Desender L., Baert J., Brandt I., Baekelandt V., Engelborghs Y. FK506 binding protein 12 differentially accelerates fibril formation of wild type alpha-synuclein and its clinical mutants A30P or A53T. J. Neurochem. 2008, 106:121-133.
    • (2008) J. Neurochem. , vol.106 , pp. 121-133
    • Gerard, M.1    Debyser, Z.2    Desender, L.3    Baert, J.4    Brandt, I.5    Baekelandt, V.6    Engelborghs, Y.7
  • 21
    • 0027563367 scopus 로고
    • Expression and characterization of two beta-adrenergic receptor kinase isoforms using the baculovirus expression system
    • Kim C.M., Dion S.B., Onorato J.J., Benovic J.L. Expression and characterization of two beta-adrenergic receptor kinase isoforms using the baculovirus expression system. Receptor 1993, 3:39-55.
    • (1993) Receptor , vol.3 , pp. 39-55
    • Kim, C.M.1    Dion, S.B.2    Onorato, J.J.3    Benovic, J.L.4
  • 23
    • 0031042365 scopus 로고    scopus 로고
    • An internal FK506-binding domain is the catalytic core of the prolyl isomerase activity associated with the Bacillus subtilis trigger factor
    • Gothel S.F., Schmid R., Wipat A., Carter N.M., Emmerson P.T., Harwood C.R., Marahiel M.A. An internal FK506-binding domain is the catalytic core of the prolyl isomerase activity associated with the Bacillus subtilis trigger factor. Eur. J. Biochem. 1997, 244:59-65.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 59-65
    • Gothel, S.F.1    Schmid, R.2    Wipat, A.3    Carter, N.M.4    Emmerson, P.T.5    Harwood, C.R.6    Marahiel, M.A.7
  • 24
    • 0028818439 scopus 로고
    • Agonist-dependent phosphorylation and desensitization of the rat A3 adenosine receptor. Evidence for a G-protein-coupled receptor kinase-mediated mechanism
    • Palmer T.M., Benovic J.L., Stiles G.L. Agonist-dependent phosphorylation and desensitization of the rat A3 adenosine receptor. Evidence for a G-protein-coupled receptor kinase-mediated mechanism. J. Biol. Chem. 1995, 270:29607-29613.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29607-29613
    • Palmer, T.M.1    Benovic, J.L.2    Stiles, G.L.3
  • 25
    • 15744388079 scopus 로고    scopus 로고
    • Antagonist efficacy in MORS196L mutant is affected by the interaction between transmembrane domains of the opioid receptor
    • Claude-Geppert P.A., Liu J., Solberg J., Erickson-Herbrandson L.J., Loh H.H., Law P.Y. Antagonist efficacy in MORS196L mutant is affected by the interaction between transmembrane domains of the opioid receptor. J. Pharmacol. Exp. Ther. 2005, 313:216-226.
    • (2005) J. Pharmacol. Exp. Ther. , vol.313 , pp. 216-226
    • Claude-Geppert, P.A.1    Liu, J.2    Solberg, J.3    Erickson-Herbrandson, L.J.4    Loh, H.H.5    Law, P.Y.6
  • 26
    • 0031589163 scopus 로고    scopus 로고
    • Comparative mutational analysis of peptidyl prolyl cis/trans isomerases: active sites of Escherichia coli trigger factor and human FKBP12
    • Tradler T., Stoller G., Rucknagel K.P., Schierhorn A., Rahfeld J.U., Fischer G. Comparative mutational analysis of peptidyl prolyl cis/trans isomerases: active sites of Escherichia coli trigger factor and human FKBP12. FEBS Lett. 1997, 407:184-190.
    • (1997) FEBS Lett. , vol.407 , pp. 184-190
    • Tradler, T.1    Stoller, G.2    Rucknagel, K.P.3    Schierhorn, A.4    Rahfeld, J.U.5    Fischer, G.6
  • 27
    • 0030875721 scopus 로고    scopus 로고
    • Agonist-induced desensitization of the μ opioid receptor is determined by threonine 394 preceded by acidic amino acids in the COOH-terminal tail
    • Pak Y., O'Dowd B.F., George S.R. Agonist-induced desensitization of the μ opioid receptor is determined by threonine 394 preceded by acidic amino acids in the COOH-terminal tail. J. Biol. Chem. 1997, 272:24961-24965.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24961-24965
    • Pak, Y.1    O'Dowd, B.F.2    George, S.R.3
  • 29
    • 46849091809 scopus 로고    scopus 로고
    • Morphine-induced μ-opioid receptor rapid desensitization is independent of receptor phosphorylation and beta-arrestins
    • Chu J., Zheng H., Loh H.H., Law P.Y. Morphine-induced μ-opioid receptor rapid desensitization is independent of receptor phosphorylation and beta-arrestins. Cell Signalling 2008, 20:1616-1624.
    • (2008) Cell Signalling , vol.20 , pp. 1616-1624
    • Chu, J.1    Zheng, H.2    Loh, H.H.3    Law, P.Y.4
  • 30
    • 74449092214 scopus 로고    scopus 로고
    • Agonist-dependent μ-opioid receptor signaling can lead to heterologous desensitization
    • Chu J., Zheng H., Zhang Y., Loh H.H., Law P.Y. Agonist-dependent μ-opioid receptor signaling can lead to heterologous desensitization. Cell Signalling 2010, 22:684-696.
    • (2010) Cell Signalling , vol.22 , pp. 684-696
    • Chu, J.1    Zheng, H.2    Zhang, Y.3    Loh, H.H.4    Law, P.Y.5
  • 31
    • 38349103412 scopus 로고    scopus 로고
    • Role of receptor internalization in opioid tolerance and dependence
    • Koch T., Hollt V. Role of receptor internalization in opioid tolerance and dependence. Pharmacol. Ther. 2008, 117:199-206.
    • (2008) Pharmacol. Ther. , vol.117 , pp. 199-206
    • Koch, T.1    Hollt, V.2
  • 32
    • 0037368572 scopus 로고    scopus 로고
    • The effects of FK506 on the development and expression of morphine tolerance and dependence in mice
    • Homayoun H., Khavandgar S., Mehr S.E., Namiranian K., Dehpour A.R. The effects of FK506 on the development and expression of morphine tolerance and dependence in mice. Behav. Pharmacol. 2003, 14:121-127.
    • (2003) Behav. Pharmacol. , vol.14 , pp. 121-127
    • Homayoun, H.1    Khavandgar, S.2    Mehr, S.E.3    Namiranian, K.4    Dehpour, A.R.5
  • 33
    • 21344468365 scopus 로고    scopus 로고
    • Regulation of gene expression by chronic morphine and morphine withdrawal in the locus ceruleus and ventral tegmental area
    • McClung C.A., Nestler E.J., Zachariou V. Regulation of gene expression by chronic morphine and morphine withdrawal in the locus ceruleus and ventral tegmental area. J. Neurosci. 2005, 25:6005-6015.
    • (2005) J. Neurosci. , vol.25 , pp. 6005-6015
    • McClung, C.A.1    Nestler, E.J.2    Zachariou, V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.