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Volumn 288, Issue 31, 2013, Pages 22248-22256

Brain-specific angiogenesis inhibitor-1 signaling, regulation, and enrichment in the postsynaptic density

Author keywords

[No Author keywords available]

Indexed keywords

ADHESION RECEPTORS; ANGIOGENESIS; G PROTEIN; POSTSYNAPTIC DENSITIES; SCAFFOLD PROTEIN; SYNAPTIC RECEPTORS;

EID: 84881244040     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.489757     Document Type: Article
Times cited : (87)

References (64)
  • 1
    • 35248884458 scopus 로고    scopus 로고
    • The adhesion GPCRs: A unique family ofGprotein-coupled receptors with important roles in both central and peripheral tissues
    • Bjarnadóttir, T. K., Fredriksson, R., and Schiöth, H. B. (2007) The adhesion GPCRs: a unique family ofGprotein-coupled receptors with important roles in both central and peripheral tissues. Cell Mol. Life Sci. 64, 2104-2119
    • (2007) Cell Mol. Life Sci. , vol.64 , pp. 2104-2119
    • Bjarnadóttir, T.K.1    Fredriksson, R.2    Schiöth, H.B.3
  • 2
    • 84867772612 scopus 로고    scopus 로고
    • Adhesion G protein-coupled receptors: Signaling, pharmacology, and mechanisms of activation
    • Paavola, K. J., and Hall, R. A. (2012) Adhesion G protein-coupled receptors: signaling, pharmacology, and mechanisms of activation. Mol. Pharmacol. 82, 777-783
    • (2012) Mol. Pharmacol. , vol.82 , pp. 777-783
    • Paavola, K.J.1    Hall, R.A.2
  • 4
  • 5
    • 85027956431 scopus 로고    scopus 로고
    • Emerging roles for the BAI1 protein family in the regulation of phagocytosis, synaptogenesis, neurovasculature, and tumor development
    • Cork, S. M., and Van Meir, E. G. (2011) Emerging roles for the BAI1 protein family in the regulation of phagocytosis, synaptogenesis, neurovasculature, and tumor development. J. Mol. Med. 89, 743-752
    • (2011) J. Mol. Med. , vol.89 , pp. 743-752
    • Cork, S.M.1    Van Meir, E.G.2
  • 7
    • 0037219173 scopus 로고    scopus 로고
    • Brain angiogenesis inhibitor 1 is differentially expressed in normal brain and glioblastoma independently of p53 expression
    • Kaur, B., Brat, D. J., Calkins, C. C., and Van Meir, E. G. (2003) Brain angiogenesis inhibitor 1 is differentially expressed in normal brain and glioblastoma independently of p53 expression. Am. J. Pathol. 162, 19-27
    • (2003) Am. J. Pathol. , vol.162 , pp. 19-27
    • Kaur, B.1    Brat, D.J.2    Calkins, C.C.3    Van Meir, E.G.4
  • 8
    • 80052193218 scopus 로고    scopus 로고
    • Overexpression of MBD2 in glioblastoma maintains epigenetic silencing and inhibits the antiangiogenic function of the tumor suppressor gene BAI1
    • Zhu, D., Hunter, S. B., Vertino, P. M., and Van Meir, E. G. (2011) Overexpression of MBD2 in glioblastoma maintains epigenetic silencing and inhibits the antiangiogenic function of the tumor suppressor gene BAI1. Cancer Res. 71, 5859-5870
    • (2011) Cancer Res. , vol.71 , pp. 5859-5870
    • Zhu, D.1    Hunter, S.B.2    Vertino, P.M.3    Van Meir, E.G.4
  • 11
    • 79957912374 scopus 로고    scopus 로고
    • Brain-specific angiogenesis inhibitor-1 expression in astrocytes and neurons: Implications for its dual function as an apoptotic engulfment receptor
    • Sokolowski, J. D., Nobles, S. L., Heffron, D. S., Park, D., Ravichandran, K. S., and Mandell, J. W. (2011) Brain-specific angiogenesis inhibitor-1 expression in astrocytes and neurons: Implications for its dual function as an apoptotic engulfment receptor. Brain Behav. Immun. 25, 915-921
    • (2011) Brain Behav. Immun. , vol.25 , pp. 915-921
    • Sokolowski, J.D.1    Nobles, S.L.2    Heffron, D.S.3    Park, D.4    Ravichandran, K.S.5    Mandell, J.W.6
  • 12
    • 0035809779 scopus 로고    scopus 로고
    • Characterization of mouse brain-specific angiogenesis inhibitor 1 (BAI1) and phytanoyl-CoA alpha-hydroxylase-associated protein 1, a novel BAI1-binding protein
    • Koh, J. T., Lee, Z. H., Ahn, K. Y., Kim, J. K., Bae, C. S., Kim, H. H., Kee, H. J., and Kim, K. K. (2001) Characterization of mouse brain-specific angiogenesis inhibitor 1 (BAI1) and phytanoyl-CoA alpha-hydroxylase-associated protein 1, a novel BAI1-binding protein. Brain Res. Mol. Brain. Res. 87, 223-237
    • (2001) Brain Res. Mol. Brain. Res. , vol.87 , pp. 223-237
    • Koh, J.T.1    Lee, Z.H.2    Ahn, K.Y.3    Kim, J.K.4    Bae, C.S.5    Kim, H.H.6    Kee, H.J.7    Kim, K.K.8
  • 13
    • 19944379133 scopus 로고    scopus 로고
    • Vasculostatin, a proteolytic fragment of brain angiogenesis inhibitor 1, is an antiangiogenic and antitumorigenic factor
    • Kaur, B., Brat, D. J., Devi, N. S., and Van Meir, E. G. (2005) Vasculostatin, a proteolytic fragment of brain angiogenesis inhibitor 1, is an antiangiogenic and antitumorigenic factor. Oncogene 24, 3632-3642
    • (2005) Oncogene , vol.24 , pp. 3632-3642
    • Kaur, B.1    Brat, D.J.2    Devi, N.S.3    Van Meir, E.G.4
  • 14
    • 33747034191 scopus 로고    scopus 로고
    • Therapeutic effect of brain-specific angiogenesis inhibitor 1 on glioblastoma: An animal experiment
    • Xiao, X. R., Kang, X. X., and Zhao, J. Z. (2006) [Therapeutic effect of brain-specific angiogenesis inhibitor 1 on glioblastoma: an animal experiment]. Zhonghua Yi Xue Za Zhi 86, 1342-1346
    • (2006) Zhonghua Yi Xue Za Zhi , vol.86 , pp. 1342-1346
    • Xiao, X.R.1    Kang, X.X.2    Zhao, J.Z.3
  • 15
    • 38449116226 scopus 로고    scopus 로고
    • Inhibition of tumor growth through suppression of angiogenesis by brain-specific angiogenesis inhibitor 1 gene transfer in murine renal cell carcinoma
    • Kudo, S., Konda, R., Obara, W., Kudo, D., Tani, K., Nakamura, Y., and Fujioka, T. (2007) Inhibition of tumor growth through suppression of angiogenesis by brain-specific angiogenesis inhibitor 1 gene transfer in murine renal cell carcinoma. Oncol. Rep. 18, 785-791
    • (2007) Oncol. Rep. , vol.18 , pp. 785-791
    • Kudo, S.1    Konda, R.2    Obara, W.3    Kudo, D.4    Tani, K.5    Nakamura, Y.6    Fujioka, T.7
  • 16
    • 16344374686 scopus 로고    scopus 로고
    • Lipid-mediated delivery of brain-specific angiogenesis inhibitor 1 gene reduces corneal neovascularization in an in vivo rabbit model
    • Yoon, K. C., Ahn, K. Y., Lee, J. H., Chun, B. J., Park, S. W., Seo, M. S., Park, Y. G., and Kim, K. K. (2005) Lipid-mediated delivery of brain-specific angiogenesis inhibitor 1 gene reduces corneal neovascularization in an in vivo rabbit model. Gene Ther. 12, 617-624
    • (2005) Gene Ther. , vol.12 , pp. 617-624
    • Yoon, K.C.1    Ahn, K.Y.2    Lee, J.H.3    Chun, B.J.4    Park, S.W.5    Seo, M.S.6    Park, Y.G.7    Kim, K.K.8
  • 18
    • 84871234437 scopus 로고    scopus 로고
    • A proprotein convertase/MMP-14 proteolytic cascade releases a novel 40 kDa vasculostatin from tumor suppressor BAI1
    • Cork, S. M., Kaur, B., Devi, N. S., Cooper, L., Saltz, J. H., Sandberg, E. M., Kaluz, S., and Van Meir, E. G. (2012) A proprotein convertase/MMP-14 proteolytic cascade releases a novel 40 kDa vasculostatin from tumor suppressor BAI1. Oncogene 31, 5144-5152
    • (2012) Oncogene , vol.31 , pp. 5144-5152
    • Cork, S.M.1    Kaur, B.2    Devi, N.S.3    Cooper, L.4    Saltz, J.H.5    Sandberg, E.M.6    Kaluz, S.7    Van Meir, E.G.8
  • 20
    • 0037077301 scopus 로고    scopus 로고
    • Selectivity and promiscuity of the first and second PDZ domains of PSD-95 and synapse-associated protein 2002
    • Lim, I. A., Hall, D. D., and Hell, J. W. (2002) Selectivity and promiscuity of the first and second PDZ domains of PSD-95 and synapse-associated protein 2002. J. Biol. Chem. 277, 21697-21711
    • (2002) J. Biol. Chem. , vol.277 , pp. 21697-21711
    • Lim, I.A.1    Hall, D.D.2    Hell, J.W.3
  • 21
    • 0032577870 scopus 로고    scopus 로고
    • Cloning and characterization of BAI-associated protein 1: A PDZ domain-containing protein that interacts with BAI1
    • Shiratsuchi, T., Futamura, M., Oda, K., Nishimori, H., Nakamura, Y., and Tokino, T. (1998) Cloning and characterization of BAI-associated protein 1: a PDZ domain-containing protein that interacts with BAI1. Biochem. Biophys. Res. Commun. 247, 597-604
    • (1998) Biochem. Biophys. Res. Commun. , vol.247 , pp. 597-604
    • Shiratsuchi, T.1    Futamura, M.2    Oda, K.3    Nishimori, H.4    Nakamura, Y.5    Tokino, T.6
  • 22
    • 80051703577 scopus 로고    scopus 로고
    • TheNterminus of the adhesionGprotein-coupled receptor GPR56 controls receptor signaling activity
    • Paavola, K. J., Stephenson, J. R., Ritter, S. L., Alter, S. P., and Hall, R. A. (2011) TheNterminus of the adhesionGprotein-coupled receptor GPR56 controls receptor signaling activity. J. Biol. Chem. 286, 28914-28921
    • (2011) J. Biol. Chem. , vol.286 , pp. 28914-28921
    • Paavola, K.J.1    Stephenson, J.R.2    Ritter, S.L.3    Alter, S.P.4    Hall, R.A.5
  • 25
    • 58749107499 scopus 로고    scopus 로고
    • A rapid Percoll gradient procedure for preparation of synaptosomes
    • Dunkley, P. R., Jarvie, P. E., and Robinson, P. J. (2008) A rapid Percoll gradient procedure for preparation of synaptosomes. Nat. Protoc. 3, 1718-1728
    • (2008) Nat. Protoc. , vol.3 , pp. 1718-1728
    • Dunkley, P.R.1    Jarvie, P.E.2    Robinson, P.J.3
  • 26
    • 79960817178 scopus 로고    scopus 로고
    • Emerging roles of brain-specific angiogenesis inhibitor 1
    • Park, D., and Ravichandran, K. S. (2010) Emerging roles of brain-specific angiogenesis inhibitor 1. Adv. Exp. Med. Biol. 706, 167-178
    • (2010) Adv. Exp. Med. Biol. , vol.706 , pp. 167-178
    • Park, D.1    Ravichandran, K.S.2
  • 27
    • 47249103800 scopus 로고    scopus 로고
    • Orphan G protein-coupled receptor GPR56 regulates neural progenitor cell migration via a Gβ12/13 and rho pathway
    • Iguchi, T., Sakata, K., Yoshizaki, K., Tago, K., Mizuno, N., and Itoh, H. (2008) Orphan G protein-coupled receptor GPR56 regulates neural progenitor cell migration via a Gβ12/13 and rho pathway. J. Biol. Chem. 283, 14469-14478
    • (2008) J. Biol. Chem. , vol.283 , pp. 14469-14478
    • Iguchi, T.1    Sakata, K.2    Yoshizaki, K.3    Tago, K.4    Mizuno, N.5    Itoh, H.6
  • 28
    • 82655171586 scopus 로고    scopus 로고
    • LPA receptor heterodimerizes with CD97 to amplify LPA-initiated RHO-dependent signaling and invasion in prostate cancer cells
    • Ward, Y., Lake, R., Yin, J. J., Heger, C. D., Raffeld, M., Goldsmith, P. K., Merino, M., and Kelly, K. (2011) LPA receptor heterodimerizes with CD97 to amplify LPA-initiated RHO-dependent signaling and invasion in prostate cancer cells. Cancer Res. 71, 7301-7311
    • (2011) Cancer Res. , vol.71 , pp. 7301-7311
    • Ward, Y.1    Lake, R.2    Yin, J.J.3    Heger, C.D.4    Raffeld, M.5    Goldsmith, P.K.6    Merino, M.7    Kelly, K.8
  • 30
    • 77952958326 scopus 로고    scopus 로고
    • α-2 adrenergic receptor mediated ERK activation is regulated by interaction with MAGI-3
    • Yang, X., Zheng, J., Xiong, Y., Shen, H., Sun, L., Huang, Y., Sun, C., Li, Y., and He, J. (2010) α-2 adrenergic receptor mediated ERK activation is regulated by interaction with MAGI-3. FEBS Lett. 584, 2207-2212
    • (2010) FEBS Lett. , vol.584 , pp. 2207-2212
    • Yang, X.1    Zheng, J.2    Xiong, Y.3    Shen, H.4    Sun, L.5    Huang, Y.6    Sun, C.7    Li, Y.8    He, J.9
  • 31
    • 33845788234 scopus 로고    scopus 로고
    • MAGI-3 regulates LPA-induced activation of Erk and RhoA
    • Zhang, H., Wang, D., Sun, H., Hall, R. A., and Yun, C. C. (2007) MAGI-3 regulates LPA-induced activation of Erk and RhoA. Cell Signal 19, 261-268
    • (2007) Cell Signal , vol.19 , pp. 261-268
    • Zhang, H.1    Wang, D.2    Sun, H.3    Hall, R.A.4    Yun, C.C.5
  • 32
    • 4444262013 scopus 로고    scopus 로고
    • MAGI-3 is involved in the regulation of the JNK signaling pathway as a scaffold protein for frizzled and Ltap
    • Yao, R., Natsume, Y., and Noda, T. (2004) MAGI-3 is involved in the regulation of the JNK signaling pathway as a scaffold protein for frizzled and Ltap. Oncogene 23, 6023-6030
    • (2004) Oncogene , vol.23 , pp. 6023-6030
    • Yao, R.1    Natsume, Y.2    Noda, T.3
  • 33
    • 0035137316 scopus 로고    scopus 로고
    • Cellular distribution of constitutively active mutant parathyroid hormone (PTH)/PTH-related protein receptors and regulation of cyclic adenosine 3', 5'-monophosphate signaling by-arrestin2
    • Ferrari, S. L., and Bisello, A. (2001) Cellular distribution of constitutively active mutant parathyroid hormone (PTH)/PTH-related protein receptors and regulation of cyclic adenosine 3', 5'-monophosphate signaling by-arrestin2. Mol. Endocrinol. 15, 149-163
    • (2001) Mol. Endocrinol. , vol.15 , pp. 149-163
    • Ferrari, S.L.1    Bisello, A.2
  • 34
    • 0033049565 scopus 로고    scopus 로고
    • Constitutively active β-1b adrenergic receptor mutants display different phosphorylation and internalization features
    • Mhaouty-Kodja, S., Barak, L. S., Scheer, A., Abuin, L., Diviani, D., Caron, M. G., and Cotecchia, S. (1999) Constitutively active β-1b adrenergic receptor mutants display different phosphorylation and internalization features. Mol. Pharmacol. 55, 339-347
    • (1999) Mol. Pharmacol. , vol.55 , pp. 339-347
    • Mhaouty-Kodja, S.1    Barak, L.S.2    Scheer, A.3    Abuin, L.4    Diviani, D.5    Caron, M.G.6    Cotecchia, S.7
  • 35
    • 0035834428 scopus 로고    scopus 로고
    • Regulation of receptor fate by ubiquitination of activated δ(2)-adrenergic receptor and α-arrestin
    • Shenoy, S. K., McDonald, P. H., Kohout, T. A., and Lefkowitz, R. J. (2001) Regulation of receptor fate by ubiquitination of activated δ(2)-adrenergic receptor and α-arrestin. Science 294, 1307-1313
    • (2001) Science , vol.294 , pp. 1307-1313
    • Shenoy, S.K.1    McDonald, P.H.2    Kohout, T.A.3    Lefkowitz, R.J.4
  • 36
    • 34247573976 scopus 로고    scopus 로고
    • Seven-transmembrane receptors and ubiquitination
    • Shenoy, S. K. (2007) Seven-transmembrane receptors and ubiquitination. Circ. Res. 100, 1142-1154
    • (2007) Circ. Res. , vol.100 , pp. 1142-1154
    • Shenoy, S.K.1
  • 37
    • 0030856051 scopus 로고    scopus 로고
    • α-Latrotoxin receptor, latrophilin, is a novel member of the secretin family of G protein-coupled receptors
    • Lelianova, V. G., Davletov, B. A., Sterling, A., Rahman, M. A., Grishin, E. V., Totty, N. F., and Ushkaryov, Y. A. (1997) α-Latrotoxin receptor, latrophilin, is a novel member of the secretin family of G protein-coupled receptors. J. Biol. Chem. 272, 21504-21508
    • (1997) J. Biol. Chem. , vol.272 , pp. 21504-21508
    • Lelianova, V.G.1    Davletov, B.A.2    Sterling, A.3    Rahman, M.A.4    Grishin, E.V.5    Totty, N.F.6    Ushkaryov, Y.A.7
  • 38
    • 0033611669 scopus 로고    scopus 로고
    • Norepinephrine exocytosis stimulated by α-latrotoxin requires both external and stored Ca2+ and is mediated by latrophilin. G proteins and phospholipase C
    • Rahman, M. A., Ashton, A. C., Meunier, F. A., Davletov, B. A., Dolly, J. O., and Ushkaryov, Y. A. (1999) Norepinephrine exocytosis stimulated by α-latrotoxin requires both external and stored Ca2+ and is mediated by latrophilin, G proteins and phospholipase C. Philos. Trans. R. Soc. Lond. B Biol. Sci. 354, 379-386
    • (1999) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.354 , pp. 379-386
    • Rahman, M.A.1    Ashton, A.C.2    Meunier, F.A.3    Davletov, B.A.4    Dolly, J.O.5    Ushkaryov, Y.A.6
  • 39
    • 82755167752 scopus 로고    scopus 로고
    • Cell adhesion receptor GPR133 couples to G(s) protein
    • Bohnekamp, J., and Schöneberg, T. (2011) Cell adhesion receptor GPR133 couples to G(s) protein. J. Biol. Chem. 286, 41912-41916
    • (2011) J. Biol. Chem. , vol.286 , pp. 41912-41916
    • Bohnekamp, J.1    Schöneberg, T.2
  • 40
    • 84859888903 scopus 로고    scopus 로고
    • Signaling property study of adhesion G-protein-coupled receptors
    • Gupte, J., Swaminath, G., Danao, J., Tian, H., Li, Y., and Wu, X. (2012) Signaling property study of adhesion G-protein-coupled receptors. FEBS Lett. 586, 1214-1219
    • (2012) FEBS Lett. , vol.586 , pp. 1214-1219
    • Gupte, J.1    Swaminath, G.2    Danao, J.3    Tian, H.4    Li, Y.5    Wu, X.6
  • 41
    • 77951639349 scopus 로고    scopus 로고
    • Brain-specific angiogenesis inhibitor 2 (BAI2) may be activated by proteolytic processing
    • Okajima, D., Kudo, G., and Yokota, H. (2010) Brain-specific angiogenesis inhibitor 2 (BAI2) may be activated by proteolytic processing. J. Recept. Signal Transduct. Res. 30, 143-153
    • (2010) J. Recept. Signal Transduct. Res. , vol.30 , pp. 143-153
    • Okajima, D.1    Kudo, G.2    Yokota, H.3
  • 43
    • 84878318013 scopus 로고    scopus 로고
    • Sticky signaling-adhesion class g protein-coupled receptors take the stage
    • Langenhan, T., Aust, G., and Hamann, J. (2013) Sticky signaling-adhesion class g protein-coupled receptors take the stage. Sci. Signal. 6, re3
    • (2013) Sci. Signal. , pp. 6
    • Langenhan, T.1    Aust, G.2    Hamann, J.3
  • 44
    • 84861315728 scopus 로고    scopus 로고
    • Activation of myeloid cell-specific adhesion class G protein-coupled receptor EMR2 via ligation-induced translocation and interaction of receptor subunits in lipid raft microdomains
    • Huang, Y. S., Chiang, N. Y., Hu, C. H., Hsiao, C. C., Cheng, K. F., Tsai, W. P., Yona, S., Stacey, M., Gordon, S., Chang, G. W., and Lin, H. H. (2012) Activation of myeloid cell-specific adhesion class G protein-coupled receptor EMR2 via ligation-induced translocation and interaction of receptor subunits in lipid raft microdomains. Mol. Cell. Biol. 32, 1408-1420
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 1408-1420
    • Huang, Y.S.1    Chiang, N.Y.2    Hu, C.H.3    Hsiao, C.C.4    Cheng, K.F.5    Tsai, W.P.6    Yona, S.7    Stacey, M.8    Gordon, S.9    Chang, G.W.10    Lin, H.H.11
  • 45
    • 10244236521 scopus 로고    scopus 로고
    • Characterization of densin-180, a new brain-specific synaptic protein of the O-sialoglycoprotein family
    • Apperson, M. L., Moon, I. S., and Kennedy, M. B. (1996) Characterization of densin-180, a new brain-specific synaptic protein of the O-sialoglycoprotein family. J. Neurosci. 16, 6839-6852
    • (1996) J. Neurosci. , vol.16 , pp. 6839-6852
    • Apperson, M.L.1    Moon, I.S.2    Kennedy, M.B.3
  • 46
    • 0026492629 scopus 로고
    • The rat-brain postsynaptic density fraction contains a homolog of the Drosophila Disks-Large tumor suppressor protein
    • Cho, K. O., Hunt, C. A., and Kennedy, M. B. (1992) The rat-brain postsynaptic density fraction contains a homolog of the Drosophila Disks-Large tumor suppressor protein. Neuron 9, 929-942
    • (1992) Neuron , vol.9 , pp. 929-942
    • Cho, K.O.1    Hunt, C.A.2    Kennedy, M.B.3
  • 48
    • 0036560492 scopus 로고    scopus 로고
    • Syntrophins and dystrobrevins: Defining the dystrophin scaffold at synapses
    • Albrecht, D. E., and Froehner, S. C. (2002) Syntrophins and dystrobrevins: Defining the dystrophin scaffold at synapses. Neurosignals 11, 123-129
    • (2002) Neurosignals , vol.11 , pp. 123-129
    • Albrecht, D.E.1    Froehner, S.C.2
  • 50
    • 84861121293 scopus 로고    scopus 로고
    • S-SCAM/MAGI-2 is an essential synaptic scaffolding molecule for the GluA2-containing maintenance pool of AMPA receptors
    • Danielson, E., Zhang, N., Metallo, J., Kaleka, K., Shin, S. M., Gerges, N., and Lee, S. H. (2012) S-SCAM/MAGI-2 is an essential synaptic scaffolding molecule for the GluA2-containing maintenance pool of AMPA receptors. J. Neurosci. 32, 6967-6980
    • (2012) J. Neurosci. , vol.32 , pp. 6967-6980
    • Danielson, E.1    Zhang, N.2    Metallo, J.3    Kaleka, K.4    Shin, S.M.5    Gerges, N.6    Lee, S.H.7
  • 51
    • 0033151584 scopus 로고    scopus 로고
    • Characterization of MALS/Velis-1,-2, and-3: A family of mammalian LIN-7 homologs enriched at brain synapses in association with the postsynaptic density-95/NMDA receptor postsynaptic complex
    • Jo, K., Derin, R., Li, M., and Bredt, D. S. (1999) Characterization of MALS/Velis-1,-2, and-3: a family of mammalian LIN-7 homologs enriched at brain synapses in association with the postsynaptic density-95/NMDA receptor postsynaptic complex. J. Neurosci. 19, 4189-4199
    • (1999) J. Neurosci. , vol.19 , pp. 4189-4199
    • Jo, K.1    Derin, R.2    Li, M.3    Bredt, D.S.4
  • 52
    • 33646162635 scopus 로고    scopus 로고
    • GRKs and α-arrestins: Roles in receptor silencing, trafficking and signaling
    • Reiter, E., and Lefkowitz, R. J. (2006) GRKs and α-arrestins: roles in receptor silencing, trafficking and signaling. Trends Endocrinol. Metab. 17, 159-165
    • (2006) Trends Endocrinol. Metab. , vol.17 , pp. 159-165
    • Reiter, E.1    Lefkowitz, R.J.2
  • 54
    • 79955789504 scopus 로고    scopus 로고
    • Control of synapse development and plasticity by Rho GTPase regulatory proteins
    • Tolias, K. F., Duman, J. G., and Um, K. (2011) Control of synapse development and plasticity by Rho GTPase regulatory proteins. Prog. Neurobiol. 94, 133-148
    • (2011) Prog. Neurobiol. , vol.94 , pp. 133-148
    • Tolias, K.F.1    Duman, J.G.2    Um, K.3
  • 55
    • 67650490390 scopus 로고    scopus 로고
    • Different Rho GTPase-dependent signaling pathways initiate sequential steps in the consolidation of long-term potentiation
    • Rex, C. S., Chen, L. Y., Sharma, A., Liu, J., Babayan, A. H., Gall, C. M., and Lynch, G. (2009) Different Rho GTPase-dependent signaling pathways initiate sequential steps in the consolidation of long-term potentiation. J. Cell Biol. 186, 85-97
    • (2009) J. Cell Biol. , vol.186 , pp. 85-97
    • Rex, C.S.1    Chen, L.Y.2    Sharma, A.3    Liu, J.4    Babayan, A.H.5    Gall, C.M.6    Lynch, G.7
  • 56
    • 0038008186 scopus 로고    scopus 로고
    • Protein kinase C and ERK involvement in dendritic spine plasticity in cultured rodent hippocampal neurons
    • Goldin, M., and Segal, M. (2003) Protein kinase C and ERK involvement in dendritic spine plasticity in cultured rodent hippocampal neurons. Eur. J. Neurosci. 17, 2529-2539
    • (2003) Eur. J. Neurosci. , vol.17 , pp. 2529-2539
    • Goldin, M.1    Segal, M.2
  • 57
    • 33846437825 scopus 로고    scopus 로고
    • The role of the extracellular signal-regulated kinase pathway in memory encoding
    • Giovannini, M. G. (2006) The role of the extracellular signal-regulated kinase pathway in memory encoding. Rev. Neurosci. 17, 619-634
    • (2006) Rev. Neurosci. , vol.17 , pp. 619-634
    • Giovannini, M.G.1
  • 58
    • 2942550646 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases in synaptic plasticity and memory
    • Sweatt, J. D. (2004) Mitogen-activated protein kinases in synaptic plasticity and memory. Curr. Opin. Neurobiol. 14, 311-317
    • (2004) Curr. Opin. Neurobiol. , vol.14 , pp. 311-317
    • Sweatt, J.D.1
  • 59
    • 84876271509 scopus 로고    scopus 로고
    • The adhesion-GPCR BAI1 regulates synaptogenesis by controlling the recruitment of the Par3/Tiam1 polarity complex to synaptic sites
    • Duman, J. G., Tzeng, C. P., Tu, Y. K., Munjal, T., Schwechter, B., Ho, T. S., and Tolias, K. F. (2013) The adhesion-GPCR BAI1 regulates synaptogenesis by controlling the recruitment of the Par3/Tiam1 polarity complex to synaptic sites. J. Neurosci. 33, 6964-6978
    • (2013) J. Neurosci. , vol.33 , pp. 6964-6978
    • Duman, J.G.1    Tzeng, C.P.2    Tu, Y.K.3    Munjal, T.4    Schwechter, B.5    Ho, T.S.6    Tolias, K.F.7
  • 60
    • 79251635430 scopus 로고    scopus 로고
    • Antidepressant-like behavior in brain-specific angiogenesis inhibitor 2-deficient mice
    • Okajima, D., Kudo, G., and Yokota, H. (2011) Antidepressant-like behavior in brain-specific angiogenesis inhibitor 2-deficient mice. J. Physiol. Sci. 61, 47-54
    • (2011) J. Physiol. Sci. , vol.61 , pp. 47-54
    • Okajima, D.1    Kudo, G.2    Yokota, H.3
  • 61
    • 79952291044 scopus 로고    scopus 로고
    • The cell-adhesion G protein-coupled receptor BAI3 is a high-affinity receptor for C1qlike proteins
    • Bolliger, M. F., Martinelli, D. C., and Südhof, T. C. (2011) The cell-adhesion G protein-coupled receptor BAI3 is a high-affinity receptor for C1qlike proteins. Proc. Natl. Acad. Sci. U.S.A. 108, 2534-2539
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 2534-2539
    • Bolliger, M.F.1    Martinelli, D.C.2    Südhof, T.C.3
  • 62
    • 84881165056 scopus 로고    scopus 로고
    • The adhesion-GPCR BAI3, a gene linked to psychiatric disorders, regulates dendrite morphogenesis in neurons
    • DOI 10.1038/mp.2013.46 [Epub ahead of print]
    • Lanoue, V., Usardi, A., Sigoillot, S. M., Talleur, M., Iyer, K., Mariani, J., Isope, P., Vodjdani, G., Heintz, N., and Selimi, F. (2013) The adhesion-GPCR BAI3, a gene linked to psychiatric disorders, regulates dendrite morphogenesis in neurons. Mol. Psych., DOI 10.1038/mp.2013.46 [Epub ahead of print]
    • (2013) Mol. Psych.
    • Lanoue, V.1    Usardi, A.2    Sigoillot, S.M.3    Talleur, M.4    Iyer, K.5    Mariani, J.6    Isope, P.7    Vodjdani, G.8    Heintz, N.9    Selimi, F.10
  • 63
    • 0036082812 scopus 로고    scopus 로고
    • Dendritic spine pathology: Cause or consequence of neurological disorders?
    • Fiala, J. C., Spacek, J., and Harris, K. M. (2002) Dendritic spine pathology: Cause or consequence of neurological disorders? Brain Res. Rev. 39, 29-54
    • (2002) Brain Res. Rev. , vol.39 , pp. 29-54
    • Fiala, J.C.1    Spacek, J.2    Harris, K.M.3
  • 64
    • 2942560575 scopus 로고    scopus 로고
    • Microanatomy of dendritic spines: Emerging principles of synaptic pathology in psychiatric and neurological disease
    • Blanpied, T. A., and Ehlers, M. D. (2004) Microanatomy of dendritic spines: Emerging principles of synaptic pathology in psychiatric and neurological disease. Biol. Psychiat. 55, 1121-1127
    • (2004) Biol. Psychiat. , vol.55 , pp. 1121-1127
    • Blanpied, T.A.1    Ehlers, M.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.