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Volumn 89, Issue 3, 2004, Pages 593-601

Intracellular calcium modulates the nuclear translocation of calsenilin

Author keywords

Calcium; Calsenilin; Nuclear translocation; Presenilin interactor

Indexed keywords

AMYLOID BETA PROTEIN; CAFFEINE; CALCIMYCIN; CALCIUM ION; CALCIUM IONOPHORE; CALSENILIN; CYTOPLASM PROTEIN; POTASSIUM CHANNEL; PRESENILIN 1; UNCLASSIFIED DRUG;

EID: 2042496266     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2004.02362.x     Document Type: Article
Times cited : (32)

References (44)
  • 3
    • 0031721511 scopus 로고    scopus 로고
    • Calsenilin: A calcium-binding protein that interacts with the presenilins and regulates the levels of a presenilin fragment
    • Buxbaum J. D., Choi E. K., Luo Y., Lilliehook C., Crowley A. C., Merriam D. E. and Wasco W. (1998) Calsenilin: a calcium-binding protein that interacts with the presenilins and regulates the levels of a presenilin fragment. Nat. Med. 4, 1177-1181.
    • (1998) Nat. Med. , vol.4 , pp. 1177-1181
    • Buxbaum, J.D.1    Choi, E.K.2    Luo, Y.3    Lilliehook, C.4    Crowley, A.C.5    Merriam, D.E.6    Wasco, W.7
  • 4
    • 0344643444 scopus 로고    scopus 로고
    • Ca (2+)-dependent prodynorphin transcriptional derepression in neuroblastoma cells is exerted through DREAM protein activity in a kinase-independent manner
    • Campos D., Jimenez-Diaz, L., Naranjo J. R. and Carrion A. M. (2003) Ca (2+)-dependent prodynorphin transcriptional derepression in neuroblastoma cells is exerted through DREAM protein activity in a kinase-independent manner. Mol. Cell Neurosci. 22, 135-145.
    • (2003) Mol. Cell Neurosci. , vol.22 , pp. 135-145
    • Campos, D.1    Jimenez-Diaz, L.2    Naranjo, J.R.3    Carrion, A.M.4
  • 6
    • 0035374675 scopus 로고    scopus 로고
    • Calsenilin is a substrate for caspase-3 that preferentially interacts with the familial Alzheimer's disease-associated c-terminal fragment of presenilin 2
    • Choi E. K., Zaidi N. F., Miller J. S., Crowley A. C., Merriam D. E., Lilliehook C., Buxbaum J. D. and Wasco W. (2001) Calsenilin is a substrate for caspase-3 that preferentially interacts with the familial Alzheimer's disease-associated c-terminal fragment of presenilin 2. J. Biol. Chem. 276, 19197-19204.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19197-19204
    • Choi, E.K.1    Zaidi, N.F.2    Miller, J.S.3    Crowley, A.C.4    Merriam, D.E.5    Lilliehook, C.6    Buxbaum, J.D.7    Wasco, W.8
  • 8
    • 0036160583 scopus 로고    scopus 로고
    • Serum deprivation increases ceramide levels and induces apoptosis in undifferentiated HN9.10e cells
    • Colombaioni L., Frago L. M., Varela-Nieto I., Pesi R. and Garcia-Gil M. (2002) Serum deprivation increases ceramide levels and induces apoptosis in undifferentiated HN9.10e cells. Neurochem. Int. 40, 327-336.
    • (2002) Neurochem. Int. , vol.40 , pp. 327-336
    • Colombaioni, L.1    Frago, L.M.2    Varela-Nieto, I.3    Pesi, R.4    Garcia-Gil, M.5
  • 9
    • 0035854645 scopus 로고    scopus 로고
    • Nuclear export of human beta-catenin can occur independent of CRM1 and the adenomatous polyposis coli tumor suppressor
    • Eleftheriou A., Yoshida M. and Henderson B. R. (2001) Nuclear export of human beta-catenin can occur independent of CRM1 and the adenomatous polyposis coli tumor suppressor. J. Biol. Chem. 276, 25883-25888.
    • (2001) J. Biol. Chem. , vol.276 , pp. 25883-25888
    • Eleftheriou, A.1    Yoshida, M.2    Henderson, B.R.3
  • 10
    • 0030924190 scopus 로고    scopus 로고
    • CRM1 is an export receptor for leucine-rich nuclear export signals
    • Fornerod M., Ohno M., Yoshida M. and Mattaj I. W. (1997) CRM1 is an export receptor for leucine-rich nuclear export signals. Cell 90, 1051-1060.
    • (1997) Cell , vol.90 , pp. 1051-1060
    • Fornerod, M.1    Ohno, M.2    Yoshida, M.3    Mattaj, I.W.4
  • 11
    • 0039115156 scopus 로고    scopus 로고
    • Transport into and out of the cell nucleus
    • Gorlich D. (1998) Transport into and out of the cell nucleus. EMBO J. 17, 2721-2727.
    • (1998) EMBO J. , vol.17 , pp. 2721-2727
    • Gorlich, D.1
  • 12
    • 0027937653 scopus 로고
    • Isolation of a protein that is essential for the first step of nuclear protein import
    • Gorlich D., Prehn S., Laskey R. A. and Hartmann E. (1994) Isolation of a protein that is essential for the first step of nuclear protein import. Cell 79, 767-778.
    • (1994) Cell , vol.79 , pp. 767-778
    • Gorlich, D.1    Prehn, S.2    Laskey, R.A.3    Hartmann, E.4
  • 13
    • 0001190006 scopus 로고    scopus 로고
    • Identification of newly transcribed RNA
    • (Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Smith, J. A., Seidman, J. G., Struhl, K., eds). John Wiley and Sons, Inc., New York
    • Greenberg M. E. and Bender T. P. (1997) Identification of newly transcribed RNA. In: Current Protocols in Molecular Biology (Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Smith, J. A., Seidman, J. G., Struhl, K., eds), pp. 4.10.1-4.10.11. John Wiley and Sons, Inc., New York.
    • (1997) Current Protocols in Molecular Biology , pp. 4101-41011
    • Greenberg, M.E.1    Bender, T.P.2
  • 14
    • 0031578895 scopus 로고    scopus 로고
    • Interactions between HIV Rev. and nuclear import and export factors: The Rev. nuclear localisation signal mediates specific binding to human importin-beta
    • Henderson B. R. and Percipalle P. (1997) Interactions between HIV Rev. and nuclear import and export factors: the Rev. nuclear localisation signal mediates specific binding to human importin-beta. J. Mol. Biol. 274, 693-707.
    • (1997) J. Mol. Biol. , vol.274 , pp. 693-707
    • Henderson, B.R.1    Percipalle, P.2
  • 15
    • 0033168391 scopus 로고    scopus 로고
    • The nuclear localization signal (NLS) of PDX-1 is part of the homeodomain and represents a novel type of NLS
    • Hessabi B., Ziegler P., Schmidt I., Hessabi C. and Walther R. (1999) The nuclear localization signal (NLS) of PDX-1 is part of the homeodomain and represents a novel type of NLS. Eur. J. Biochem. 263, 170-177.
    • (1999) Eur. J. Biochem. , vol.263 , pp. 170-177
    • Hessabi, B.1    Ziegler, P.2    Schmidt, I.3    Hessabi, C.4    Walther, R.5
  • 16
    • 0040251482 scopus 로고    scopus 로고
    • Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear import of ribosomal proteins in mammalian cells
    • Jakel S. and Gorlich D. (1998) Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear import of ribosomal proteins in mammalian cells. EMBO J. 17, 4491-4502.
    • (1998) EMBO J. , vol.17 , pp. 4491-4502
    • Jakel, S.1    Gorlich, D.2
  • 17
    • 0030806304 scopus 로고    scopus 로고
    • The cytokine interleukin-5 (IL-5) effects co-transport of its receptor subunits to the nucleus in vitro
    • Jans D. A., Briggs L. J., Gustin S. E., Jans P., Ford S. and Young I. G. (1997) The cytokine interleukin-5 (IL-5) effects co-transport of its receptor subunits to the nucleus in vitro. FEBS Lett. 410, 368-372.
    • (1997) FEBS Lett. , vol.410 , pp. 368-372
    • Jans, D.A.1    Briggs, L.J.2    Gustin, S.E.3    Jans, P.4    Ford, S.5    Young, I.G.6
  • 22
    • 0033050069 scopus 로고    scopus 로고
    • Transcriptional repressor ERF is a Ras/mitogen-activated protein kinase target that regulates cellular proliferation
    • Le Gallic L., Sgouras D., Beal G. Jr and Mavrothalassitis G. (1999) Transcriptional repressor ERF is a Ras/mitogen-activated protein kinase target that regulates cellular proliferation. Mol Cell Biol. 19, 4121-4133.
    • (1999) Mol Cell Biol. , vol.19 , pp. 4121-4133
    • Le Gallic, L.1    Sgouras, D.2    Beal Jr., G.3    Mavrothalassitis, G.4
  • 23
    • 0027283659 scopus 로고
    • Growth factors induce nuclear translocation of MAP kinases (p42mapk and p44mapk) but not of their activator MAP kinase kinase (p45mapkk) in fibroblasts
    • Lenormand P., Sardet C., Pages G., L'Allemain G., Brunet A. and Pouyssegur J. (1993) Growth factors induce nuclear translocation of MAP kinases (p42mapk and p44mapk) but not of their activator MAP kinase kinase (p45mapkk) in fibroblasts. J. Cell Biol. 122, 1079-1088.
    • (1993) J. Cell Biol. , vol.122 , pp. 1079-1088
    • Lenormand, P.1    Sardet, C.2    Pages, G.3    L'Allemain, G.4    Brunet, A.5    Pouyssegur, J.6
  • 25
    • 0042977521 scopus 로고    scopus 로고
    • The ins and outs of STAT1 nuclear transport
    • August 12, 2003. Review
    • McBride K. M. and Reich N. C. (2003) The ins and outs of STAT1 nuclear transport. Sci. STKE 2003 August 12, 2003 (195): RE13. Review.
    • (2003) Sci. STKE 2003 , Issue.195
    • McBride, K.M.1    Reich, N.C.2
  • 26
    • 0029909366 scopus 로고    scopus 로고
    • Identification of the nuclear localization signal of mouse DNA primase: Nuclear transport of p46 subunit is facilitated by interaction with p54 subunit
    • Mizuno T., Okamoto T., Yokoi M., Izumi M., Kobayashi A., Hachiya T., Tamai K., Inoue T. and Hanaoka F. (1996) Identification of the nuclear localization signal of mouse DNA primase: nuclear transport of p46 subunit is facilitated by interaction with p54 subunit. J. Cell Sci. 109, 2627-2636.
    • (1996) J. Cell Sci. , vol.109 , pp. 2627-2636
    • Mizuno, T.1    Okamoto, T.2    Yokoi, M.3    Izumi, M.4    Kobayashi, A.5    Hachiya, T.6    Tamai, K.7    Inoue, T.8    Hanaoka, F.9
  • 27
    • 0037177892 scopus 로고    scopus 로고
    • Molecular cloning and characterization of CALP/KChIP4, a novel EF-hand protein interacting with presenilin 2 and voltage-gated potassium channel subunit Kv4
    • Morohashi Y., Hatano N., Ohya S., Takikawa R., Watabiki T., Takasugi N., Imaizumi Y., Tomita T. and Iwatsubo T. (2002) Molecular cloning and characterization of CALP/KChIP4, a novel EF-hand protein interacting with presenilin 2 and voltage-gated potassium channel subunit Kv4. J. Biol. Chem. 277, 14965-14975.
    • (2002) J. Biol. Chem. , vol.277 , pp. 14965-14975
    • Morohashi, Y.1    Hatano, N.2    Ohya, S.3    Takikawa, R.4    Watabiki, T.5    Takasugi, N.6    Imaizumi, Y.7    Tomita, T.8    Iwatsubo, T.9
  • 28
    • 0028962511 scopus 로고
    • Previously identified protein of uncertain function is karyopherin alpha and together with karyopherin beta docks import substrate at nuclear pore complexes
    • Moroianu J., Blobel G. and Radu A. (1995) Previously identified protein of uncertain function is karyopherin alpha and together with karyopherin beta docks import substrate at nuclear pore complexes. Proc. Natl Acad. Sci. USA 92, 2008-2011.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2008-2011
    • Moroianu, J.1    Blobel, G.2    Radu, A.3
  • 29
    • 0030748907 scopus 로고    scopus 로고
    • Evidence for a role of CRM1 in signal-mediated nuclear protein export
    • Ossareh-Nazari B., Bachelerie F. and Dargemont C. (1997) Evidence for a role of CRM1 in signal-mediated nuclear protein export. Science 278, 141-144.
    • (1997) Science , vol.278 , pp. 141-144
    • Ossareh-Nazari, B.1    Bachelerie, F.2    Dargemont, C.3
  • 30
    • 0035977032 scopus 로고    scopus 로고
    • A composite nuclear export signal in the TBP-associated factor TAFII105
    • Rashevsky-Finkel A., Silkov A. and Dikstein R. (2001) A composite nuclear export signal in the TBP-associated factor TAFII105. J. Biol. Chem. 276, 44963-44969.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44963-44969
    • Rashevsky-Finkel, A.1    Silkov, A.2    Dikstein, R.3
  • 31
    • 0035341218 scopus 로고    scopus 로고
    • Interleukin 3-dependent activation of DREAM is involved in transcriptional silencing of the apoptotic Hrk gene in hematopoietic progenitor cells
    • Sanz, C., Mellstrom B., Link W. A., Naranjo J. R. and Fernandez-Luna J. L. (2001) Interleukin 3-dependent activation of DREAM is involved in transcriptional silencing of the apoptotic Hrk gene in hematopoietic progenitor cells. EMBO J. 20, 2286-2292.
    • (2001) EMBO J. , vol.20 , pp. 2286-2292
    • Sanz, C.1    Mellstrom, B.2    Link, W.A.3    Naranjo, J.R.4    Fernandez-Luna, J.L.5
  • 32
    • 0034957426 scopus 로고    scopus 로고
    • Reversible nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase upon serum depletion
    • Schmitz, H. D. (2001) Reversible nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase upon serum depletion. Eur. J. Cell Biol. 80, 419-427.
    • (2001) Eur. J. Cell Biol. , vol.80 , pp. 419-427
    • Schmitz, H.D.1
  • 33
    • 0036895725 scopus 로고    scopus 로고
    • PKA modulation of Kv4.2-encoded A-type potassium channels requires formation of a supramolecular complex
    • Schrader L. A., Anderson A. E., Mayne A., Pfaffinger P. J. and Sweatt J. D. (2002) PKA modulation of Kv4.2-encoded A-type potassium channels requires formation of a supramolecular complex. J. Neurosci. 22, 10123-10133.
    • (2002) J. Neurosci. , vol.22 , pp. 10123-10133
    • Schrader, L.A.1    Anderson, A.E.2    Mayne, A.3    Pfaffinger, P.J.4    Sweatt, J.D.5
  • 35
    • 0033601256 scopus 로고    scopus 로고
    • Nuclear import of hepatic glucokinase depends upon glucokinase regulatory protein, whereas export is due to a nuclear export signal sequence in glucokinase
    • Shiota C., Coffey J., Grimsby J., Grippo J. F. and Magnuson M. A. (1999) Nuclear import of hepatic glucokinase depends upon glucokinase regulatory protein, whereas export is due to a nuclear export signal sequence in glucokinase. J. Biol. Chem. 274, 37125-37130.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37125-37130
    • Shiota, C.1    Coffey, J.2    Grimsby, J.3    Grippo, J.F.4    Magnuson, M.A.5
  • 36
    • 0026548929 scopus 로고
    • Characterization of a novel nuclear localization signal in the HTLV-I tax transactivator protein
    • Smith M. R. and Greene W. C. (1992) Characterization of a novel nuclear localization signal in the HTLV-I tax transactivator protein. Virology. 187, 316-320.
    • (1992) Virology , vol.187 , pp. 316-320
    • Smith, M.R.1    Greene, W.C.2
  • 37
    • 0026664729 scopus 로고
    • Analysis of a developmentally regulated nuclear localization signal in Xenopus
    • Standiford D. M. and Richter J. D. (1992) Analysis of a developmentally regulated nuclear localization signal in Xenopus. J. Cell Biol. 118, 991-1002.
    • (1992) J. Cell Biol. , vol.118 , pp. 991-1002
    • Standiford, D.M.1    Richter, J.D.2
  • 38
    • 0032911885 scopus 로고    scopus 로고
    • The arginine-rich domains present in human immunodeficiency virus type 1 Tat and Rev. function as direct importin beta-dependent nuclear localization signals
    • Truant R. and Cullen B. R. (1999) The arginine-rich domains present in human immunodeficiency virus type 1 Tat and Rev. function as direct importin beta-dependent nuclear localization signals. Mol. Cell. Biol. 2, 1210-1217.
    • (1999) Mol. Cell. Biol. , vol.2 , pp. 1210-1217
    • Truant, R.1    Cullen, B.R.2
  • 39
    • 0036858376 scopus 로고    scopus 로고
    • Calcium responses to caffeine and muscarinic receptor agonists are altered in traumatically injured neurons
    • Weber J. T., Rzigalinski B. A. and Ellis E. F. (2002) Calcium responses to caffeine and muscarinic receptor agonists are altered in traumatically injured neurons. J. Neurotrauma 19, 433-443.
    • (2002) J. Neurotrauma , vol.19 , pp. 433-443
    • Weber, J.T.1    Rzigalinski, B.A.2    Ellis, E.F.3
  • 40
    • 0028988731 scopus 로고
    • Identification of hSRP1 alpha as a functional receptor for nuclear localization sequences
    • Weis K., Mattaj I. W. and Lamond A. I. (1995) Identification of hSRP1 alpha as a functional receptor for nuclear localization sequences. Science 268, 1049-1053.
    • (1995) Science , vol.268 , pp. 1049-1053
    • Weis, K.1    Mattaj, I.W.2    Lamond, A.I.3
  • 41
    • 0035182145 scopus 로고    scopus 로고
    • CRM1- and Ran-independent nuclear export of beta-catenin
    • Wiechens N. and Fagotto F. (2001) CRM1- and Ran-independent nuclear export of beta-catenin. Curr. Biol. 11, 18-27.
    • (2001) Curr. Biol. , vol.11 , pp. 18-27
    • Wiechens, N.1    Fagotto, F.2
  • 42
    • 0037023770 scopus 로고    scopus 로고
    • Characterization of an unusual importin alpha binding motif in the borna disease virus p 10 protein that directs nuclear import
    • Wolff T., Unterstab G., Heins G., Richt J. A. and Kann M. (2002) Characterization of an unusual importin alpha binding motif in the borna disease virus p 10 protein that directs nuclear import. J. Biol. Chem. 277, 12151-12157.
    • (2002) J. Biol. Chem. , vol.277 , pp. 12151-12157
    • Wolff, T.1    Unterstab, G.2    Heins, G.3    Richt, J.A.4    Kann, M.5
  • 43
    • 0141960055 scopus 로고    scopus 로고
    • Nuclear translocation of phosphorylated STAT3 is essential for vascular endothelial growth factor-induced human dermal microvascular endothelial cell migration and tube formation
    • Yahata Y., Shirakata Y., Tokumaru S., Yamasaki K., Sayama K., Hanakawa Y., Detmar M. and Hashimoto K. (2003) Nuclear translocation of phosphorylated STAT3 is essential for vascular endothelial growth factor-induced human dermal microvascular endothelial cell migration and tube formation. J. Biol. Chem. 278, 40026-40031.
    • (2003) J. Biol. Chem. , vol.278 , pp. 40026-40031
    • Yahata, Y.1    Shirakata, Y.2    Tokumaru, S.3    Yamasaki, K.4    Sayama, K.5    Hanakawa, Y.6    Detmar, M.7    Hashimoto, K.8


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