메뉴 건너뛰기




Volumn 77, Issue 3, 2001, Pages 730-740

A unique spacer domain of synaptotagmin IV is essential for Golgi localization

Author keywords

C2 domain; Exocytosis; Glycosylation; Golgi; Immediate early genes; Synaptotagmin

Indexed keywords

CALCIUM; GLYCOSIDASE; SIALIDASE; SYNAPTOTAGMIN;

EID: 0035008362     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2001.00266.x     Document Type: Article
Times cited : (27)

References (39)
  • 2
  • 3
    • 0032705475 scopus 로고    scopus 로고
    • Alternative splicing of synaptotagmins involving transmembrane exon skipping
    • Craxton M. and Goedert M. (1999) Alternative splicing of synaptotagmins involving transmembrane exon skipping. FEBS Lett. 460, 417-422.
    • (1999) FEBS Lett. , vol.460 , pp. 417-422
    • Craxton, M.1    Goedert, M.2
  • 4
    • 0031194048 scopus 로고    scopus 로고
    • The function of inositol high polyphosphate binding proteins
    • Fukuda M. and Mikoshiba K. (1997) The function of inositol high polyphosphate binding proteins. Bioessays 19, 593-603.
    • (1997) Bioessays , vol.19 , pp. 593-603
    • Fukuda, M.1    Mikoshiba, K.2
  • 5
    • 0033615526 scopus 로고    scopus 로고
    • A novel alternatively spliced variant of synaptotagmin VI lacking a transmembrane domain: Implications for distinct functions of the two isoforms
    • Fukuda M. and Mikoshiba K. (1999) A novel alternatively spliced variant of synaptotagmin VI lacking a transmembrane domain: implications for distinct functions of the two isoforms. J. Biol. Chem. 274, 31428-31434.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31428-31434
    • Fukuda, M.1    Mikoshiba, K.2
  • 6
    • 0034623083 scopus 로고    scopus 로고
    • Distinct self-oligomerization activities of synaptotagmin family: Unique calcium-dependent oligomerization properties of synaptotagmin VII
    • Fukuda M. and Mikoshiba K. (2000a) Distinct self-oligomerization activities of synaptotagmin family: unique calcium-dependent oligomerization properties of synaptotagmin VII. J. Biol. Chem. 275, 28180-28185.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28180-28185
    • Fukuda, M.1    Mikoshiba, K.2
  • 7
    • 0033773047 scopus 로고    scopus 로고
    • Calcium-dependent and -independent hetero-oligomerization in the synaptotagmin family
    • Fukuda M. and Mikoshiba K. (2000b) Calcium-dependent and -independent hetero-oligomerization in the synaptotagmin family. J. Biochem. 128, 627-635.
    • (2000) J. Biochem. , vol.128 , pp. 627-635
    • Fukuda, M.1    Mikoshiba, K.2
  • 8
    • 0034576763 scopus 로고    scopus 로고
    • Expression of synaptotagmin I or II promotes neurite outgrowth in PC12 cells
    • Fukuda M. and Mikoshiba K. (2000c) Expression of synaptotagmin I or II promotes neurite outgrowth in PC12 cells. Neurosci. Lett. 295, 33-36.
    • (2000) Neurosci. Lett. , vol.295 , pp. 33-36
    • Fukuda, M.1    Mikoshiba, K.2
  • 9
    • 0035281639 scopus 로고    scopus 로고
    • Characterization of KIAA1427 protein as an atypical synaptotagmin (Syt XIII)
    • Fukuda M. and Mikoshiba K. (2001) Characterization of KIAA1427 protein as an atypical synaptotagmin (Syt XIII). Biochem. J. 354, 249-257.
    • (2001) Biochem. J. , vol.354 , pp. 249-257
    • Fukuda, M.1    Mikoshiba, K.2
  • 10
    • 0027986795 scopus 로고
    • Inositol-1,3,4,5-tetrakisphosphate binding to C2B domain of IP4BP/synaptotagmin II
    • Fukuda M., Aruga J., Niinobe M., Aimoto S. and Mikoshiba K. (1994) Inositol-1,3,4,5-tetrakisphosphate binding to C2B domain of IP4BP/synaptotagmin II. J. Biol. Chem. 269, 29206-29211.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29206-29211
    • Fukuda, M.1    Aruga, J.2    Niinobe, M.3    Aimoto, S.4    Mikoshiba, K.5
  • 11
    • 0028859443 scopus 로고
    • Functional diversity of C2 domains of synaptotagmin family: Mutational analysis of inositol high polyphosphate binding domain
    • Fukuda M., Kojima T., Aruga J., Niinobe M. and Mikoshiba K. (1995a) Functional diversity of C2 domains of synaptotagmin family: mutational analysis of inositol high polyphosphate binding domain. J. Biol. Chem. 270, 26523-26527.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26523-26527
    • Fukuda, M.1    Kojima, T.2    Aruga, J.3    Niinobe, M.4    Mikoshiba, K.5
  • 12
    • 0028832353 scopus 로고
    • Role of the C2B domain of synaptotagmin in vesicular release and recycling as determined by specific antibody injection into the squid giant synapse preterminal
    • Fukuda M., Moreira J. E., Lewis F. M. T., Sugimori M., Niinobe M., Mikoshiba K. and Llinás R. (1995b) Role of the C2B domain of synaptotagmin in vesicular release and recycling as determined by specific antibody injection into the squid giant synapse preterminal. Proc. Natl Acad. Sci. USA 92, 10708-10712.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 10708-10712
    • Fukuda, M.1    Moreira, J.E.2    Lewis, F.M.T.3    Sugimori, M.4    Niinobe, M.5    Mikoshiba, K.6    Llinás, R.7
  • 13
    • 0029872616 scopus 로고    scopus 로고
    • 2+-dependent phospholipid binding to the C2A domain of synaptotagmin IV
    • 2+-dependent phospholipid binding to the C2A domain of synaptotagmin IV. J. Biol. Chem. 271, 8430-8434.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8430-8434
    • Fukuda, M.1    Kojima, T.2    Mikoshiba, K.3
  • 14
    • 0030895606 scopus 로고    scopus 로고
    • Regulation by bivalent cations of phospholipid binding to the C2A domain of synaptotagmin III
    • Fukuda M., Kojima T. and Mikoshiba K. (1997) Regulation by bivalent cations of phospholipid binding to the C2A domain of synaptotagmin III. Biochem. J. 323, 421-425.
    • (1997) Biochem. J. , vol.323 , pp. 421-425
    • Fukuda, M.1    Kojima, T.2    Mikoshiba, K.3
  • 15
    • 0033615704 scopus 로고    scopus 로고
    • Conserved N-terminal cysteine motif is essential for homo-and heterodimer formation of synaptotagmins III, V, VI, and X
    • Fukuda M., Kanno E. and Mikoshiba K. (1999) Conserved N-terminal cysteine motif is essential for homo-and heterodimer formation of synaptotagmins III, V, VI, and X. J. Biol. Chem. 274, 31421-31427.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31421-31427
    • Fukuda, M.1    Kanno, E.2    Mikoshiba, K.3
  • 16
  • 17
    • 0027933686 scopus 로고
    • A third synaptotagmin gene, Syt3, in the mouse
    • Hilbush B. S. and Morgan J. I. (1994) A third synaptotagmin gene, Syt3, in the mouse. Proc. Natl Acad. Sci. USA 91, 8195-8199.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 8195-8199
    • Hilbush, B.S.1    Morgan, J.I.2
  • 18
    • 0032524341 scopus 로고    scopus 로고
    • Inositol 1,3,4,5-tetrakisphosphate binding activities of neuronal and non-neuronal synaptotagmins: Identification of conserved amino acid substitutions that abolish inositol 1,3,4,5-tetrakisphosphate binding to synaptotagmins III, V, and X
    • Ibata K., Fukuda M. and Mikoshiba K. (1998) Inositol 1,3,4,5-tetrakisphosphate binding activities of neuronal and non-neuronal synaptotagmins: identification of conserved amino acid substitutions that abolish inositol 1,3,4,5-tetrakisphosphate binding to synaptotagmins III, V, and X. J. Biol. Chem. 273, 12267-12273.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12267-12273
    • Ibata, K.1    Fukuda, M.2    Mikoshiba, K.3
  • 19
    • 0033969088 scopus 로고    scopus 로고
    • Synaptotagmin IV is present at the Golgi and distal parts of neurites
    • Ibata K., Fukuda M., Hamada T., Kabayama H. and Mikoshiba K. (2000) Synaptotagmin IV is present at the Golgi and distal parts of neurites. J. Neurochem. 74, 518-526.
    • (2000) J. Neurochem. , vol.74 , pp. 518-526
    • Ibata, K.1    Fukuda, M.2    Hamada, T.3    Kabayama, H.4    Mikoshiba, K.5
  • 20
    • 0029134920 scopus 로고
    • Malfolded cytochrome P-450 (MI) localized in unusual membrane structures of the endoplasmic reticulum in cultured animal cells
    • Ishihara N., Yamashina S., Sakaguchi M., Mihara K. and Omura T. (1995) Malfolded cytochrome P-450 (MI) localized in unusual membrane structures of the endoplasmic reticulum in cultured animal cells. J. Biochem. 118, 397-404.
    • (1995) J. Biochem. , vol.118 , pp. 397-404
    • Ishihara, N.1    Yamashina, S.2    Sakaguchi, M.3    Mihara, K.4    Omura, T.5
  • 21
    • 0032889757 scopus 로고    scopus 로고
    • Functional involvement of synaptotagmin I/II C2A domain in neurite outgrowth of chick dorsal root ganglion neuron
    • Kabayama H., Takei K., Fukuda M., Ibata K. and Mikoshiba K. (1999) Functional involvement of synaptotagmin I/II C2A domain in neurite outgrowth of chick dorsal root ganglion neuron. Neuroscience 88, 999-1003.
    • (1999) Neuroscience , vol.88 , pp. 999-1003
    • Kabayama, H.1    Takei, K.2    Fukuda, M.3    Ibata, K.4    Mikoshiba, K.5
  • 22
    • 0034097165 scopus 로고    scopus 로고
    • Targeting of synaptotagmin to neurite terminals in neuronally differentiated PC12 cells
    • Krasnov P. A. and Enikolopov G. (2000) Targeting of synaptotagmin to neurite terminals in neuronally differentiated PC12 cells. J. Cell Sci. 113, 1389-1404.
    • (2000) J. Cell Sci. , vol.113 , pp. 1389-1404
    • Krasnov, P.A.1    Enikolopov, G.2
  • 23
    • 0030868429 scopus 로고    scopus 로고
    • 2 domain of synaptotagmin is required for exocytosis of insulin from pancreatic β-cells: Action of synaptotagmin at low micromolar calcium
    • 2 domain of synaptotagmin is required for exocytosis of insulin from pancreatic β-cells: action of synaptotagmin at low micromolar calcium. EMBO J. 16, 5837-5846.
    • (1997) EMBO J. , vol.16 , pp. 5837-5846
    • Lang, J.1    Fukuda, M.2    Zhang, H.3    Mikoshiba, K.4    Wollheim, C.B.5
  • 25
    • 0033584339 scopus 로고    scopus 로고
    • Synaptic function modulated by changes in the ratio of synaptotagmin I and IV
    • Littleton J. T., Serano T. L., Rubin G. M., Ganetzky B. and Chapman E. R. (1999) Synaptic function modulated by changes in the ratio of synaptotagmin I and IV. Nature 400, 757-760.
    • (1999) Nature , vol.400 , pp. 757-760
    • Littleton, J.T.1    Serano, T.L.2    Rubin, G.M.3    Ganetzky, B.4    Chapman, E.R.5
  • 26
    • 0038066072 scopus 로고    scopus 로고
    • Synaptotagmins in membrane traffic: Which vesicles do the tagmins tag?
    • Marquèze B., Berton F. and Seagar M. (2000) Synaptotagmins in membrane traffic: which vesicles do the tagmins tag? Biochimie 82, 409-420.
    • (2000) Biochimie , vol.82 , pp. 409-420
    • Marquèze, B.1    Berton, F.2    Seagar, M.3
  • 28
    • 0028799119 scopus 로고
    • Role of the C2A domain of synaptotagmin in transmitter release as determined by specific antibody injection into the squid giant synapse preterminal
    • Mikoshiba K., Fukuda M., Moreira J. E., Lewis F. M. T., Sugimori M., Niinobe M. and Llinás R. (1995) Role of the C2A domain of synaptotagmin in transmitter release as determined by specific antibody injection into the squid giant synapse preterminal. Proc. Natl Acad. Sci. USA 92, 10703-10707.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 10703-10707
    • Mikoshiba, K.1    Fukuda, M.2    Moreira, J.E.3    Lewis, F.M.T.4    Sugimori, M.5    Niinobe, M.6    Llinás, R.7
  • 29
    • 0030888066 scopus 로고    scopus 로고
    • Roles of synaptotagmin C2 domains in neurotransmitter secretion and inositol high-polyphosphate binding at mammalian cholinergic synapses
    • Mochida S., Fukuda M., Niinobe M., Kobayashi H. and Mikoshiba K. (1997) Roles of synaptotagmin C2 domains in neurotransmitter secretion and inositol high-polyphosphate binding at mammalian cholinergic synapses. Neurvscience 77, 937-943.
    • (1997) Neurvscience , vol.77 , pp. 937-943
    • Mochida, S.1    Fukuda, M.2    Niinobe, M.3    Kobayashi, H.4    Mikoshiba, K.5
  • 31
    • 0022540905 scopus 로고
    • Biogenesis of the crystalloid endoplasmic reticulum in UT-1 cells: Evidence that newly formed endoplasmic reticulum emerges from the nuclear envelope
    • Pathak R. K., Luskey K. L. and Anderson R. G. W. (1986) Biogenesis of the crystalloid endoplasmic reticulum in UT-1 cells: evidence that newly formed endoplasmic reticulum emerges from the nuclear envelope. J. Cell Biol. 102, 2158-2168.
    • (1986) J. Cell Biol. , vol.102 , pp. 2158-2168
    • Pathak, R.K.1    Luskey, K.L.2    Anderson, R.G.W.3
  • 33
    • 0030222771 scopus 로고    scopus 로고
    • 2-domain proteins that regulate membrane traffic
    • 2-domain proteins that regulate membrane traffic. Neuron 17, 379-388.
    • (1996) Neuron , vol.17 , pp. 379-388
    • Südhof, T.C.1    Rizo, J.2
  • 35
    • 0032525067 scopus 로고    scopus 로고
    • Functional analysis of the C2A domain of synaptotagmin 1: Implications for calcium-regulated secretion
    • Thomas D. M. and Elferink L. A. (1998) Functional analysis of the C2A domain of synaptotagmin 1: implications for calcium-regulated secretion. J. Neurosci. 18, 3511-3520.
    • (1998) J. Neurosci. , vol.18 , pp. 3511-3520
    • Thomas, D.M.1    Elferink, L.A.2
  • 36
    • 0032816016 scopus 로고    scopus 로고
    • Functional and biochemical analysis of the C2 domains of synaptotagmin IV
    • Thomas D. M., Ferguson G. D., Herschman H. R. and Elferink L. A. (1999) Functional and biochemical analysis of the C2 domains of synaptotagmin IV. Mol. Biol. Cell. 10, 2285-2295.
    • (1999) Mol. Biol. Cell. , vol.10 , pp. 2285-2295
    • Thomas, D.M.1    Ferguson, G.D.2    Herschman, H.R.3    Elferink, L.A.4
  • 38
    • 0028901750 scopus 로고
    • Synaptotagmin IV is an immediate early gene induced by depolarization in PC12 cells and in brain
    • Vician L., Lim I. K., Ferguson G., Tocco G., Baudry M. and Herschman H. R. (1995) Synaptotagmin IV is an immediate early gene induced by depolarization in PC12 cells and in brain. Proc. Natl. Acad. Sci. USA 92, 2164-2168.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2164-2168
    • Vician, L.1    Lim, I.K.2    Ferguson, G.3    Tocco, G.4    Baudry, M.5    Herschman, H.R.6
  • 39
    • 0029993184 scopus 로고    scopus 로고
    • Formation of crystalloid endoplasmic reticulum in COS cells upon over-expression of microsomal aldehyde dehydrogenase by cDNA transfection
    • Yamamoto A., Masaki R. and Tashiro Y. (1996) Formation of crystalloid endoplasmic reticulum in COS cells upon over-expression of microsomal aldehyde dehydrogenase by cDNA transfection. J. Cell Sci. 109, 1727-1738.
    • (1996) J. Cell Sci. , vol.109 , pp. 1727-1738
    • Yamamoto, A.1    Masaki, R.2    Tashiro, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.