메뉴 건너뛰기




Volumn 22, Issue 7, 2008, Pages 2521-2533

B56β, a regulatory subunit of protein phosphatase 2A, interacts with CALEB/NGC and inhibits CALEB/NGC-mediated dendritic branching

Author keywords

Akt signaling; Dendritic tree elaboration; Mass spectrometry; Neuronal differentiation; Spine morphogenesis

Indexed keywords

EPIDERMAL GROWTH FACTOR; NEUROGLYCAN C; PHOSPHOPROTEIN PHOSPHATASE 2A; PROTEIN B56BETA; PROTEIN CALEB; PROTEIN KINASE B; PROTEIN SUBUNIT; REGULATOR PROTEIN; GLUTATHIONE TRANSFERASE; MEMBRANE PROTEIN; PEPTIDE FRAGMENT; PHOSPHOPROTEIN PHOSPHATASE 2; PPP2R5B PROTEIN, HUMAN;

EID: 46749152149     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fj.07-096115     Document Type: Article
Times cited : (11)

References (32)
  • 1
    • 0141918787 scopus 로고    scopus 로고
    • The control of dendrite development
    • Jan, Y. N., and Jan, L. Y. (2003) The control of dendrite development. Neuron 40, 229-242
    • (2003) Neuron , vol.40 , pp. 229-242
    • Jan, Y.N.1    Jan, L.Y.2
  • 2
    • 0346024190 scopus 로고    scopus 로고
    • Genesis of dendritic spines: Insights from ultrastructural and imaging studies
    • Yuste, R., and Bonhoeffer, T. (2004) Genesis of dendritic spines: insights from ultrastructural and imaging studies. Nat. Rev. Neurosci. 5, 24-34
    • (2004) Nat. Rev. Neurosci , vol.5 , pp. 24-34
    • Yuste, R.1    Bonhoeffer, T.2
  • 3
    • 9644276929 scopus 로고    scopus 로고
    • Dynamics and pathology of dendritic spines
    • Halpain, S., Spencer, K., and Graber, S. (2005) Dynamics and pathology of dendritic spines. Prog. Brain. Res. 147, 29-37
    • (2005) Prog. Brain. Res , vol.147 , pp. 29-37
    • Halpain, S.1    Spencer, K.2    Graber, S.3
  • 4
    • 20544447033 scopus 로고    scopus 로고
    • Rho GTPases, dendritic structure, and mental retardation
    • Newey, S. E., Velamoor, V., Govek, E. E., and Van Aelst, L. (2005) Rho GTPases, dendritic structure, and mental retardation. J. Neurobiol. 64, 58-74
    • (2005) J. Neurobiol , vol.64 , pp. 58-74
    • Newey, S.E.1    Velamoor, V.2    Govek, E.E.3    Van Aelst, L.4
  • 6
    • 0035654078 scopus 로고    scopus 로고
    • Dendritic spines: Structure, dynamics and regulation
    • Hering, H., and Sheng, M. (2001) Dendritic spines: structure, dynamics and regulation. Nat. Rev. Neurosci. 2, 880-888
    • (2001) Nat. Rev. Neurosci , vol.2 , pp. 880-888
    • Hering, H.1    Sheng, M.2
  • 7
    • 18844403842 scopus 로고    scopus 로고
    • Molecular mechanisms of dendritic spine development and remodeling
    • Ethell, I. M., and Pasquale, E. B. (2005) Molecular mechanisms of dendritic spine development and remodeling. Prog. Neurobiol. 75, 161-205
    • (2005) Prog. Neurobiol , vol.75 , pp. 161-205
    • Ethell, I.M.1    Pasquale, E.B.2
  • 9
    • 0035831530 scopus 로고    scopus 로고
    • CALEB binds via its acidic stretch to the fibrinogen-like domain of tenascin-C or tenascin-R and its expression is dynamically regulated after optic nerve lesion
    • Schumacher, S., Jung, M., Norenberg, U., Dorner, A., Chiquet-Ehrismann, R., Stuermer, C. A., and Rathjen, F. G. (2001) CALEB binds via its acidic stretch to the fibrinogen-like domain of tenascin-C or tenascin-R and its expression is dynamically regulated after optic nerve lesion. J. Biol. Chem. 276, 7337-7345
    • (2001) J. Biol. Chem , vol.276 , pp. 7337-7345
    • Schumacher, S.1    Jung, M.2    Norenberg, U.3    Dorner, A.4    Chiquet-Ehrismann, R.5    Stuermer, C.A.6    Rathjen, F.G.7
  • 10
    • 0344011635 scopus 로고    scopus 로고
    • Regulated binding of the fibrinogen-like domains of tenascin-R and tenascin-C to the neural EGF family member CALEB
    • Schumacher, S., and Stube, E. M. (2003) Regulated binding of the fibrinogen-like domains of tenascin-R and tenascin-C to the neural EGF family member CALEB. J. Neurochem. 87, 1213-1223
    • (2003) J. Neurochem , vol.87 , pp. 1213-1223
    • Schumacher, S.1    Stube, E.M.2
  • 11
    • 0141891100 scopus 로고    scopus 로고
    • CALEB/NGC interacts with the Golgi-associated protein PIST
    • Hassel, B., Schreff, M., Stube, E. M., Blaich, U., and Schumacher, S. (2003) CALEB/NGC interacts with the Golgi-associated protein PIST. J. Biol. Chem. 278, 40136-40143
    • (2003) J. Biol. Chem , vol.278 , pp. 40136-40143
    • Hassel, B.1    Schreff, M.2    Stube, E.M.3    Blaich, U.4    Schumacher, S.5
  • 12
    • 0035252894 scopus 로고    scopus 로고
    • Protein phosphatase 2A: A highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling
    • Janssens, V., and Goris, J. (2001) Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling. Biochem. J. 353, 417-439
    • (2001) Biochem. J , vol.353 , pp. 417-439
    • Janssens, V.1    Goris, J.2
  • 13
    • 0028832251 scopus 로고
    • Identification of a new family of protein phosphatase 2A regulatory subunits
    • McCright, B., and Virshup, D. M. (1995) Identification of a new family of protein phosphatase 2A regulatory subunits. J. Biol. Chem. 270, 26123-26128
    • (1995) J. Biol. Chem , vol.270 , pp. 26123-26128
    • McCright, B.1    Virshup, D.M.2
  • 14
    • 0029834655 scopus 로고    scopus 로고
    • The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm
    • McCright, B., Rivers, A. M., Audlin, S., and Virshup, D. M. (1996) The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm. J. Biol. Chem. 271, 22081-22089
    • (1996) J. Biol. Chem , vol.271 , pp. 22081-22089
    • McCright, B.1    Rivers, A.M.2    Audlin, S.3    Virshup, D.M.4
  • 15
    • 0029893086 scopus 로고    scopus 로고
    • The variable subunit associated with protein phosphatase 2A0 defines a novel multimember family of regulatory subunits
    • Zolnierowicz, S., Van Hoof, C., Andjelkovic, N., Cron, P., Stevens, I., Merlevede, W., Goris, J., and Hemmings, B. A. (1996) The variable subunit associated with protein phosphatase 2A0 defines a novel multimember family of regulatory subunits. Biochem. J. 317, 187-194
    • (1996) Biochem. J , vol.317 , pp. 187-194
    • Zolnierowicz, S.1    Van Hoof, C.2    Andjelkovic, N.3    Cron, P.4    Stevens, I.5    Merlevede, W.6    Goris, J.7    Hemmings, B.A.8
  • 16
    • 0033605639 scopus 로고    scopus 로고
    • Regulation of beta-catenin signaling by the B56 subunit of protein phosphatase 2A
    • Seeling, J. M., Miller, J. R., Gil, R., Moon, R. T., White, R., and Virshup, D. M. (1999) Regulation of beta-catenin signaling by the B56 subunit of protein phosphatase 2A. Science 283, 2089-2091
    • (1999) Science , vol.283 , pp. 2089-2091
    • Seeling, J.M.1    Miller, J.R.2    Gil, R.3    Moon, R.T.4    White, R.5    Virshup, D.M.6
  • 17
    • 0035423033 scopus 로고    scopus 로고
    • Protein phosphatase 2A and its B56 regulatory subunit inhibit Wnt signaling in Xenopus
    • Li, X., Yost, H. J., Virshup, D. M., and Seeling, J. M. (2001) Protein phosphatase 2A and its B56 regulatory subunit inhibit Wnt signaling in Xenopus. EMBO J. 20, 4122-4131
    • (2001) EMBO J , vol.20 , pp. 4122-4131
    • Li, X.1    Yost, H.J.2    Virshup, D.M.3    Seeling, J.M.4
  • 19
    • 0036096778 scopus 로고    scopus 로고
    • B56-associated protein phosphatase 2A is required for survival and protects from apoptosis in Drosophila melanogaster
    • Li, X., Scuderi, A., Letsou, A., and Virshup, D. M. (2002) B56-associated protein phosphatase 2A is required for survival and protects from apoptosis in Drosophila melanogaster. Mol. Cell. Biol. 22, 3674-3684
    • (2002) Mol. Cell. Biol , vol.22 , pp. 3674-3684
    • Li, X.1    Scuderi, A.2    Letsou, A.3    Virshup, D.M.4
  • 20
    • 0037151038 scopus 로고    scopus 로고
    • A functional role for the B56 alpha-subunit of protein phosphatase 2A in ceramide-mediated regulation of Bcl2 phosphorylation status and function
    • Ruvolo, P. P., Clark, W., Mumby, M., Gao, F., and May, W. S. (2002) A functional role for the B56 alpha-subunit of protein phosphatase 2A in ceramide-mediated regulation of Bcl2 phosphorylation status and function. J. Biol. Chem. 277, 22847-22852
    • (2002) J. Biol. Chem , vol.277 , pp. 22847-22852
    • Ruvolo, P.P.1    Clark, W.2    Mumby, M.3    Gao, F.4    May, W.S.5
  • 21
    • 33644524383 scopus 로고    scopus 로고
    • B56-containing PP2A dephosphorylate ERK and their activity is controlled by the early gene IEX-1 and ERK
    • Letourneux, C., Rocher, G., and Porteu, F. (2006) B56-containing PP2A dephosphorylate ERK and their activity is controlled by the early gene IEX-1 and ERK. EMBO J. 25, 727-738
    • (2006) EMBO J , vol.25 , pp. 727-738
    • Letourneux, C.1    Rocher, G.2    Porteu, F.3
  • 22
    • 34247142858 scopus 로고    scopus 로고
    • Inhibition of B56-containing protein phosphatase 2As by the early response gene IEX-1 leads to control of Akt activity
    • Rocher, G., Letourneux, C., Lenormand, P., and Porteu, F. (2007) Inhibition of B56-containing protein phosphatase 2As by the early response gene IEX-1 leads to control of Akt activity. J. Biol. Chem. 282, 5468-5477
    • (2007) J. Biol. Chem , vol.282 , pp. 5468-5477
    • Rocher, G.1    Letourneux, C.2    Lenormand, P.3    Porteu, F.4
  • 23
    • 0031017324 scopus 로고    scopus 로고
    • Chicken acidic leucine-rich EGF-like domain containing brain protein (CALEB), a neural member of the EGF family of differentiation factors, is implicated in neurite formation
    • Schumacher, S., Volkmer, H., Buck, F., Otto, A., Tarnok, A., Roth, S., and Rathjen, F. G. (1997) Chicken acidic leucine-rich EGF-like domain containing brain protein (CALEB), a neural member of the EGF family of differentiation factors, is implicated in neurite formation. J. Cell Biol. 136, 895-906
    • (1997) J. Cell Biol , vol.136 , pp. 895-906
    • Schumacher, S.1    Volkmer, H.2    Buck, F.3    Otto, A.4    Tarnok, A.5    Roth, S.6    Rathjen, F.G.7
  • 24
    • 33747747658 scopus 로고    scopus 로고
    • Identification of neurite outgrowth-promoting domains of neuroglycan C, a brain-specific chondroitin sulfate proteoglycan, and involvement of phosphatidylinositol 3-kinase and protein kinase C signaling pathways in neuritogenesis
    • Nakanishi, K., Aono, S., Hirano, K., Kuroda, Y., Ida, M., Tokita, Y., Matsui, F., and Oohira, A. (2006) Identification of neurite outgrowth-promoting domains of neuroglycan C, a brain-specific chondroitin sulfate proteoglycan, and involvement of phosphatidylinositol 3-kinase and protein kinase C signaling pathways in neuritogenesis. J. Biol. Chem. 281, 24970-24978
    • (2006) J. Biol. Chem , vol.281 , pp. 24970-24978
    • Nakanishi, K.1    Aono, S.2    Hirano, K.3    Kuroda, Y.4    Ida, M.5    Tokita, Y.6    Matsui, F.7    Oohira, A.8
  • 25
    • 20244385297 scopus 로고    scopus 로고
    • Impaired synapse function during postnatal development in the absence of CALEB, an EGF-like protein processed by neuronal activity
    • Juttner, R., More, M. I., Das, D., Babich, A., Meier, J., Henning, M., Erdmann, B., Mu ller, E. C., Otto, A., Grantyn, R., and Rathjen, F. G. (2005) Impaired synapse function during postnatal development in the absence of CALEB, an EGF-like protein processed by neuronal activity. Neuron 46, 233-245
    • (2005) Neuron , vol.46 , pp. 233-245
    • Juttner, R.1    More, M.I.2    Das, D.3    Babich, A.4    Meier, J.5    Henning, M.6    Erdmann, B.7    Mu ller, E.C.8    Otto, A.9    Grantyn, R.10    Rathjen, F.G.11
  • 26
    • 30544449810 scopus 로고    scopus 로고
    • Control of dendritic arborization by the phosphoinositide-3′- kinase-Akt-mammalian target of rapamycin pathway
    • Jaworski, J., Spangler, S., Seeburg, D. P., Hoogenraad, C. C., and Sheng, M. (2005) Control of dendritic arborization by the phosphoinositide-3′- kinase-Akt-mammalian target of rapamycin pathway. J. Neurosci. 25, 11300-11312
    • (2005) J. Neurosci , vol.25 , pp. 11300-11312
    • Jaworski, J.1    Spangler, S.2    Seeburg, D.P.3    Hoogenraad, C.C.4    Sheng, M.5
  • 27
    • 30544442753 scopus 로고    scopus 로고
    • Regulation of dendritic morphogenesis by Ras-PI3K-Akt-mTOR and Ras-MAPK signaling pathways
    • Kumar, V., Zhang, M. X., Swank, M. W., Kunz, J., and Wu, G. Y. (2005) Regulation of dendritic morphogenesis by Ras-PI3K-Akt-mTOR and Ras-MAPK signaling pathways. J. Neurosci. 25, 11288-11299
    • (2005) J. Neurosci , vol.25 , pp. 11288-11299
    • Kumar, V.1    Zhang, M.X.2    Swank, M.W.3    Kunz, J.4    Wu, G.Y.5
  • 28
    • 0347052869 scopus 로고    scopus 로고
    • Leemhuis, J., Boutillier, S., Scale barth, H., Feuerstein, T. J., Brock, C., Nurnberg, B., Aktories, K., and Meyer, D. K. (2004) Rho GTPases and phosphoinositide 3-kinase organize formation of branched dendrites. J. Biol. Chem. 279, 585-596
    • Leemhuis, J., Boutillier, S., Scale barth, H., Feuerstein, T. J., Brock, C., Nurnberg, B., Aktories, K., and Meyer, D. K. (2004) Rho GTPases and phosphoinositide 3-kinase organize formation of branched dendrites. J. Biol. Chem. 279, 585-596
  • 29
    • 0242384747 scopus 로고    scopus 로고
    • Beta-catenin is critical for dendritic morphogenesis
    • Yu, X., and Malenka, R. C. (2003) Beta-catenin is critical for dendritic morphogenesis. Nat. Neurosci. 6, 1169-1177
    • (2003) Nat. Neurosci , vol.6 , pp. 1169-1177
    • Yu, X.1    Malenka, R.C.2
  • 30
    • 0023746492 scopus 로고
    • Characterization of the rat mas oncogene and its high-level expression in the hippocampus and cerebral cortex of rat brain
    • Young, D., O'Neill, K., Jessell, T., and Wigler, M. (1988) Characterization of the rat mas oncogene and its high-level expression in the hippocampus and cerebral cortex of rat brain. Proc. Natl. Acad. Sci. U. S. A. 85, 5339-5342
    • (1988) Proc. Natl. Acad. Sci. U. S. A , vol.85 , pp. 5339-5342
    • Young, D.1    O'Neill, K.2    Jessell, T.3    Wigler, M.4
  • 31
    • 0004285740 scopus 로고    scopus 로고
    • Banker, G, and Goslin, K, eds, MIT Press, Cambridge, MA, USA
    • Banker, G., and Goslin, K. (eds) (1998) Culturing Nerve Cells, MIT Press, Cambridge, MA, USA
    • (1998) Culturing Nerve Cells
  • 32
    • 0027226219 scopus 로고
    • Optimized survival of hippocampal neurons in B27-supplemented Neurobasal, a new serum-free medium combination
    • Brewer, G. J., Torricelli, J. R., Evege, E. K., and Price, P. J. (1993) Optimized survival of hippocampal neurons in B27-supplemented Neurobasal, a new serum-free medium combination. J. Neurosci. Res. 35, 567-576
    • (1993) J. Neurosci. Res , vol.35 , pp. 567-576
    • Brewer, G.J.1    Torricelli, J.R.2    Evege, E.K.3    Price, P.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.