메뉴 건너뛰기




Volumn 92, Issue 3, 2005, Pages 647-659

BAALC 1-6-8 protein is targeted to postsynaptic lipid rafts by its N-terminal myristoylation and palmitoylation, and interacts with α, but not β, subunit of Ca2+/calmodulin-dependent protein kinase II

Author keywords

Brain and acute leukemia cytoplasmic protein; Ca2+ calmodulin dependent protein kinase II; Myristoylation; Palmitoylation; Postsynaptic density; Postsynaptic lipid raft

Indexed keywords

BRAIN PROTEIN; PROTEIN BAALC 1 6 8; PROTEIN KINASE (CALCIUM,CALMODULIN) II; UNCLASSIFIED DRUG;

EID: 13244252410     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2004.02902.x     Document Type: Article
Times cited : (24)

References (48)
  • 1
    • 0028301606 scopus 로고
    • Dual myristylation and palmitylation of Src family member p59fyn affects subcellular localization
    • Alland L., Peseckis S. M., Atherton R. E., Berthiaume L. and Resh M. D. (1994) Dual myristylation and palmitylation of Src family member p59fyn affects subcellular localization. J. Biol. Chem. 269, 16 701-16 705.
    • (1994) J. Biol. Chem. , vol.269
    • Alland, L.1    Peseckis, S.M.2    Atherton, R.E.3    Berthiaume, L.4    Resh, M.D.5
  • 3
    • 0016631494 scopus 로고
    • Cross-linking of the components of lactose synthetase with dimethylpimelimidate
    • Brew K., Shaper J. H., Olsen K. W., Trayer I. P. and Hill R. L. (1975) Cross-linking of the components of lactose synthetase with dimethylpimelimidate. J. Biol Chem. 250, 1434-1444.
    • (1975) J. Biol Chem. , vol.250 , pp. 1434-1444
    • Brew, K.1    Shaper, J.H.2    Olsen, K.W.3    Trayer, I.P.4    Hill, R.L.5
  • 4
    • 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
  • 5
    • 0026492629 scopus 로고
    • The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-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 discs-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
  • 6
    • 0036584774 scopus 로고    scopus 로고
    • Differential palmitoylation directs the AMPA receptor-binding protein ABP to spines or to intracellular clusters
    • DeSouza S., Fu J., States B. A. and Ziff E. B. (2002) Differential palmitoylation directs the AMPA receptor-binding protein ABP to spines or to intracellular clusters. J. Neurosci. 22, 3493-3503.
    • (2002) J. Neurosci. , vol.22 , pp. 3493-3503
    • DeSouza, S.1    Fu, J.2    States, B.A.3    Ziff, E.B.4
  • 7
    • 18344396972 scopus 로고    scopus 로고
    • Synaptic strength regulated by palmitate cycling on PSD-95
    • El-Husseini, Ael-D., Schnel E., Dakoji S. et al. (2002) Synaptic strength regulated by palmitate cycling on PSD-95. Cell 108, 849-863.
    • (2002) Cell , vol.108 , pp. 849-863
    • El-Husseini, A.-D.1    Schnel, E.2    Dakoji, S.3
  • 10
    • 0026806967 scopus 로고
    • 2+/ calmodulin-dependent protein kinase analyzed by site-directed mutagenesis
    • 2+/calmodulin-dependent protein kinase analyzed by site-directed mutagenesis. J. Biol. Chem. 267, 17 216-17 224.
    • (1992) J. Biol. Chem. , vol.267
    • Hanson, P.I.1    Schulman, H.2
  • 11
    • 0037996880 scopus 로고    scopus 로고
    • Lipid rafts in the maintenance of synapses, dendritic spines, surface AMPA receptor stability
    • Hering H., Lin C.-C. and Sheng M. (2003) Lipid rafts in the maintenance of synapses, dendritic spines, surface AMPA receptor stability. J. Neurosci. 23, 3262-3271.
    • (2003) J. Neurosci. , vol.23 , pp. 3262-3271
    • Hering, H.1    Lin, C.-C.2    Sheng, M.3
  • 12
    • 0027395956 scopus 로고
    • Localization of TGN38 to the trans-Golgi Network: Involvement of a Cytoplasmic Tyrosine-containing Sequence
    • Humphrey J. S., Peters P. J., Yuan L. C., Juan S. and Bonifacino J. S. (1993) Localization of TGN38 to the trans-Golgi Network: Involvement of a Cytoplasmic Tyrosine-containing Sequence. J. Cell Biol 120, 1123-1135.
    • (1993) J. Cell Biol. , vol.120 , pp. 1123-1135
    • Humphrey, J.S.1    Peters, P.J.2    Yuan, L.C.3    Juan, S.4    Bonifacino, J.S.5
  • 13
    • 3042662329 scopus 로고    scopus 로고
    • Brain-specific novel guanine nucleotide exchange factor candidate for Arf, synA-rfGEFc, is localized to postsynaptic density
    • Inaba Y., Tian Q. B., Okano A. et al. (2004) Brain-specific novel guanine nucleotide exchange factor candidate for Arf, synA-rfGEFc, is localized to postsynaptic density. J. Neurochem. 89, 1347-1357.
    • (2004) J. Neurochem. , vol.89 , pp. 1347-1357
    • Inaba, Y.1    Tian, Q.B.2    Okano, A.3
  • 14
    • 0019349993 scopus 로고
    • Developmental changes in morphology and molecular composition of isolated synaptic junctional structures
    • Kelly P. T. and Cotman C. W. (1981) Developmental changes in morphology and molecular composition of isolated synaptic junctional structures. Brain Res. 206, 251-257.
    • (1981) Brain Res. , vol.206 , pp. 251-257
    • Kelly, P.T.1    Cotman, C.W.2
  • 15
    • 12244260817 scopus 로고    scopus 로고
    • The postsynaptic density and dendritic raft localization of PSD-Zip70, which contains an N-myristoylation sequence and leucin-zipper motifs
    • Konno D., Ko J-A, Usui S. et al. (2002) The postsynaptic density and dendritic raft localization of PSD-Zip70, which contains an N-myristoylation sequence and leucin-zipper motifs. J. Cell Sci. 115, 4695-4706.
    • (2002) J. Cell Sci. , vol.115 , pp. 4695-4706
    • Konno, D.1    Ko, J.-A.2    Usui, S.3
  • 16
    • 0025792297 scopus 로고
    • Structural features in eukaryotic mRNAs that modulate the initiation of translation
    • Kozak M. (1991) Structural features in eukaryotic mRNAs that modulate the initiation of translation. J. Biol. Chem. 266, 19 867-19 870.
    • (1991) J. Biol. Chem. , vol.266
    • Kozak, M.1
  • 18
    • 0033067455 scopus 로고    scopus 로고
    • Glycolipid-enriched caveolae and caveolae-like domains in the nervous system
    • Masserini M., Palestini P. and Pitto M. (1999) Glycolipid-enriched caveolae and caveolae-like domains in the nervous system. J. Neurochem. 73, 1-11.
    • (1999) J. Neurochem. , vol.73 , pp. 1-11
    • Masserini, M.1    Palestini, P.2    Pitto, M.3
  • 19
    • 0029039937 scopus 로고
    • The dynamic role of palmitoylation in signal transduction
    • Milligan G., Parenti M. and Magee A. I. (1995) The dynamic role of palmitoylation in signal transduction. Trends Biochem. Sci. 20, 181-187.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 181-187
    • Milligan, G.1    Parenti, M.2    Magee, A.I.3
  • 20
    • 0028906288 scopus 로고
    • Molecular characterization and spatial distribution of SAP97, a novel presynaptic protein homologous to SAP90 and the Drosophila discs-large tumor suppressor protein
    • Muller B. M., Kistner U., Veh R. W., Cases-Langhoff C., Becker B., Gundelfinger E. D. and Garner C. C. (1995) Molecular characterization and spatial distribution of SAP97, a novel presynaptic protein homologous to SAP90 and the Drosophila discs-large tumor suppressor protein. J. Neurosci. 15, 2354-2366.
    • (1995) J. Neurosci. , vol.15 , pp. 2354-2366
    • Muller, B.M.1    Kistner, U.2    Veh, R.W.3    Cases-Langhoff, C.4    Becker, B.5    Gundelfinger, E.D.6    Garner, C.C.7
  • 21
    • 0030936823 scopus 로고    scopus 로고
    • Reversible palmitoylation of signaling proteins
    • Mumby S. M. (1997) Reversible palmitoylation of signaling proteins. Curr. Opin. Cell Biol. 9, 148-154.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 148-154
    • Mumby, S.M.1
  • 22
    • 0034738046 scopus 로고    scopus 로고
    • Occurrence of a transcription factor, signal transducer and activators of transcription 3 (Stat3), in the postsynaptic density of the rat brain
    • Murata S., Usuda N., Okano A., Kobayashi S. and Suzuki T. (2000) Occurrence of a transcription factor, signal transducer and activators of transcription 3 (Stat3), in the postsynaptic density of the rat brain. Mol. Brain Res. 78, 80-90.
    • (2000) Mol. Brain Res. , vol.78 , pp. 80-90
    • Murata, S.1    Usuda, N.2    Okano, A.3    Kobayashi, S.4    Suzuki, T.5
  • 23
    • 0025294106 scopus 로고
    • 2+/calmodulin is inhibited by autophosphorylation of threonine within the calmodulin-binding domain
    • 2+/calmodulin is inhibited by autophosphorylation of threonine within the calmodulin-binding domain. J. Biol. Chem. 265, 11 204-11 212.
    • (1990) J. Biol. Chem. , vol.265
    • Patton, B.L.1    Miller, S.G.2    Kennedy, M.B.3
  • 24
    • 0028173679 scopus 로고
    • Myristylation and palmitylation of Src family members: The fats of the matter
    • Resh M. D. (1994) Myristylation and palmitylation of Src family members: the fats of the matter. Cell 76, 411-413.
    • (1994) Cell , vol.76 , pp. 411-413
    • Resh, M.D.1
  • 25
    • 0029014901 scopus 로고
    • Myristoylation and differential palmitoylation of the HCK protein-tyrosine kinases govern their attachment to membranes and association with caveolae
    • Robbins S. M., Quintrell N. A. and Bishop J. M. (1995) Myristoylation and differential palmitoylation of the HCK protein-tyrosine kinases govern their attachment to membranes and association with caveolae. Mol. Cell. Biol. 15, 3507-3515.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3507-3515
    • Robbins, S.M.1    Quintrell, N.A.2    Bishop, J.M.3
  • 26
    • 0029240330 scopus 로고
    • Palmitoylation in G-protein signaling pathways
    • Ross E. M. (1995) Palmitoylation in G-protein signaling pathways. Curr. Biol. 5, 107-109.
    • (1995) Curr. Biol. , vol.5 , pp. 107-109
    • Ross, E.M.1
  • 28
    • 0024477304 scopus 로고
    • 2+/calmodulin-dependent protein kinase: Domain structure and regulation
    • 2+/ calmodulin-dependent protein kinase: domain structure and regulation. Trends Biochem. Sci. 14, 62-66.
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 62-66
    • Schulman, H.1    Lou, L.L.2
  • 29
    • 0023058975 scopus 로고
    • A conserved AU sequence from the 3 untranslated region of GM-CSF mRNA mediates selective mRNA degradation
    • Shaw G. and Kamen R. (1986) A conserved AU sequence from the 3 untranslated region of GM-CSF mRNA mediates selective mRNA degradation. Cell 46, 659-667.
    • (1986) Cell , vol.46 , pp. 659-667
    • Shaw, G.1    Kamen, R.2
  • 30
    • 0033515884 scopus 로고    scopus 로고
    • Dynamic control of CaMKII translocation and localization in hippocampal neurons by NMDA receptor stimulation
    • Shen K. and Meyer T. (1999) Dynamic control of CaMKII translocation and localization in hippocampal neurons by NMDA receptor stimulation. Science 284, 162-166.
    • (1999) Science , vol.284 , pp. 162-166
    • Shen, K.1    Meyer, T.2
  • 31
    • 0033860922 scopus 로고    scopus 로고
    • Molecular memory by reversible translocation of calcium/calmodulin- dependent protein kinase II
    • Shen K., Teruel M. N., Connor J. H., Shenolikar S. and Meyer T. (2000) Molecular memory by reversible translocation of calcium/calmodulin-dependent protein kinase II. Nat. Neurosci. 3, 881-886.
    • (2000) Nat. Neurosci. , vol.3 , pp. 881-886
    • Shen, K.1    Teruel, M.N.2    Connor, J.H.3    Shenolikar, S.4    Meyer, T.5
  • 32
    • 0028175989 scopus 로고
    • Cysteine3 of Src family protein tyrosine kinase determines palmitoylation and localization in caveolae
    • Shenoy-Scaria A. M., Dietzen D. J., Kwong J., Link D. C. and Lublin D. M. (1994) Cysteine3 of Src family protein tyrosine kinase determines palmitoylation and localization in caveolae. J. Cell Biol. 126, 353-363.
    • (1994) J. Cell Biol. , vol.126 , pp. 353-363
    • Shenoy-Scaria, A.M.1    Dietzen, D.J.2    Kwong, J.3    Link, D.C.4    Lublin, D.M.5
  • 33
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K. and Ikonen E. (1997) Functional rafts in cell membranes. Nature 387, 569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 34
    • 0025139450 scopus 로고
    • An improved method for immobilizing IgG antibodies on protein A-agarose
    • Sisson T. H. and Castor C. W. (1990) An improved method for immobilizing IgG antibodies on protein A-agarose. J. Immunol. Meth. 127, 215-220.
    • (1990) J. Immunol. Meth. , vol.127 , pp. 215-220
    • Sisson, T.H.1    Castor, C.W.2
  • 36
    • 0032584956 scopus 로고    scopus 로고
    • NMDA receptor subunits in the postsynaptic density of rat brain: Expression and phosphorylation by endogenous protein kinases
    • Suen P. C., Wu K., Xu J. L., Lin S. Y., Levine E. S. and Black I. B. (1998) NMDA receptor subunits in the postsynaptic density of rat brain: expression and phosphorylation by endogenous protein kinases. Mol. Brain Res. 59, 215-228.
    • (1998) Mol. Brain Res. , vol.59 , pp. 215-228
    • Suen, P.C.1    Wu, K.2    Xu, J.L.3    Lin, S.Y.4    Levine, E.S.5    Black, I.B.6
  • 37
    • 0036768289 scopus 로고    scopus 로고
    • Lipid rafts at postsynaptic sites: Distribution, function and linkage to postsynaptic density
    • Suzuki T. (2002) Lipid rafts at postsynaptic sites: distribution, function and linkage to postsynaptic density. Neurosci. Res. 44, 1-9.
    • (2002) Neurosci. Res. , vol.44 , pp. 1-9
    • Suzuki, T.1
  • 38
    • 0028111814 scopus 로고
    • 2+/calmodulin-dependent protein kinase II into postsynaptic density after decapitation
    • 2+/calmodulin-dependent protein kinase II into postsynaptic density after decapitation. J. Neurochem. 63, 1529-1537.
    • (1994) J. Neurochem. , vol.63 , pp. 1529-1537
    • Suzuki, T.1    Okumura-Noji, K.2    Tanaka, R.3    Tada, T.4
  • 39
    • 0030869946 scopus 로고    scopus 로고
    • Postsynaptic mechanisms. Localization of α-internexin in the postsynaptic density of the rat brain
    • Suzuki T., Mitake S., Okumura-Noji K., Shimizu H., Tada T. and Fujii T. (1997) Postsynaptic mechanisms. Localization of α-internexin in the postsynaptic density of the rat brain. Brain Res. 765, 74-80.
    • (1997) Brain Res. , vol.765 , pp. 74-80
    • Suzuki, T.1    Mitake, S.2    Okumura-Noji, K.3    Shimizu, H.4    Tada, T.5    Fujii, T.6
  • 40
    • 0033573767 scopus 로고    scopus 로고
    • Presence of molecular chaperones, heat shock cognate (Hsc) 70 and heat shock proteins (Hsp) 40, in the postsynaptic structures of rat brain
    • Suzuki T., Usuda N., Murata S., Nakazawa A., Ohtsuka K. and Takagi H. (1999) Presence of molecular chaperones, heat shock cognate (Hsc) 70 and heat shock proteins (Hsp) 40, in the postsynaptic structures of rat brain. Brain Res. 816, 99-110.
    • (1999) Brain Res. , vol.816 , pp. 99-110
    • Suzuki, T.1    Usuda, N.2    Murata, S.3    Nakazawa, A.4    Ohtsuka, K.5    Takagi, H.6
  • 41
    • 0035906258 scopus 로고    scopus 로고
    • Biochemical evidence for localization of AMPA-type glutamate receptor subunits in the dendritic raft
    • Suzuki T., Ito J., Takagi H., Saitoh R, Nawa H. and Shimizu H. (2001) Biochemical evidence for localization of AMPA-type glutamate receptor subunits in the dendritic raft. Mol. Brain Res. 89, 20-28.
    • (2001) Mol. Brain Res. , vol.89 , pp. 20-28
    • Suzuki, T.1    Ito, J.2    Takagi, H.3    Saitoh, R.4    Nawa, H.5    Shimizu, H.6
  • 42
    • 0035923722 scopus 로고    scopus 로고
    • BAALC, the human member of a novel mammalian neuroectoderm gene lineage, is implicated in hematopoiesis and acute leukemia
    • Tanner S. M., Austin J. L., Leone G. et al. (2001) BAALC, the human member of a novel mammalian neuroectoderm gene lineage, is implicated in hematopoiesis and acute leukemia. Proc. Natl Acad. Sci. USA 98, 13 901-13 906.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98
    • Tanner, S.M.1    Austin, J.L.2    Leone, G.3
  • 43
    • 0032848886 scopus 로고    scopus 로고
    • Identification of mRNAs localizing in the postsynaptic region
    • Tian Q. B., Nakayama K., Okano A. and Suzuki T. (1999) Identification of mRNAs localizing in the postsynaptic region. Mol. Brain Res. 72, 147-157.
    • (1999) Mol. Brain Res. , vol.72 , pp. 147-157
    • Tian, Q.B.1    Nakayama, K.2    Okano, A.3    Suzuki, T.4
  • 44
    • 0142148231 scopus 로고    scopus 로고
    • A novel ubiquitin-specific protease, synUSP, is localized at the post-synaptic density and post-synaptic lipid raft
    • Tian Q. B., Okano A., Nakayama K., Miyazawa S., Endo S. and Suzuki T. (2003) A novel ubiquitin-specific protease, synUSP, is localized at the post-synaptic density and post-synaptic lipid raft. J. Neurochem. 87, 665-675.
    • (2003) J. Neurochem. , vol.87 , pp. 665-675
    • Tian, Q.B.1    Okano, A.2    Nakayama, K.3    Miyazawa, S.4    Endo, S.5    Suzuki, T.6
  • 45
    • 0024455621 scopus 로고
    • Tissue-specific expression of four types of rat calmodulin-dependent protein kinase II mRNAs
    • Tobimatsu T. and Fujisawa H. (1989) Tissue-specific expression of four types of rat calmodulin-dependent protein kinase II mRNAs. J. Biol. Chem. 264, 17 907-17 912.
    • (1989) J. Biol. Chem. , vol.264
    • Tobimatsu, T.1    Fujisawa, H.2
  • 46
    • 0023666521 scopus 로고
    • Acylation of proteins with myristic acid occurs cotranslationally
    • Wilcox C., Hu J. S. and Olson E. N. (1987) Acylation of proteins with myristic acid occurs cotranslationally. Science 238, 1275-1278.
    • (1987) Science , vol.238 , pp. 1275-1278
    • Wilcox, C.1    Hu, J.S.2    Olson, E.N.3
  • 47
    • 0342313718 scopus 로고    scopus 로고
    • Homer: A link between neural activity and glutamate receptor function
    • Xiao B., Tu J. C. and Worley P. F. (2000) Homer: a link between neural activity and glutamate receptor function. Curr. Opin. Neurobiol. 10, 370-374.
    • (2000) Curr. Opin. Neurobiol. , vol.10 , pp. 370-374
    • Xiao, B.1    Tu, J.C.2    Worley, P.F.3
  • 48
    • 0028873973 scopus 로고
    • Expression of mRNAs encoding subunits of the NMDA receptor in developing rat brain
    • Zhong J., Carrozza D. P., Williams K., Pritchett D. B. and MolinoffP. B. (1995) Expression of mRNAs encoding subunits of the NMDA receptor in developing rat brain. J. Neurochem. 64, 531-539.
    • (1995) J. Neurochem. , vol.64 , pp. 531-539
    • Zhong, J.1    Carrozza, D.P.2    Williams, K.3    Pritchett, D.B.4    Molinoff, P.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.