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Volumn 382, Issue 1, 2004, Pages 353-362

Identification of the actin-binding domain of Ins(1,4,5)P3 3-kinase isoform B (IP3K-B)

Author keywords

Actin binding domain; F actin; Ins(1,4,5)P3 3 kinase B; Subcellular localization

Indexed keywords

CYTOSKELETONS; ENHANCED GREEN FLUORESCENT PROTEIN (EGFP); MUTATIONS; PLASMA MEMBRANES;

EID: 4344707810     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20031751     Document Type: Article
Times cited : (22)

References (48)
  • 1
    • 0034092565 scopus 로고    scopus 로고
    • Inositol tetrakisphosphate as a frequency regulator in calcium oscillations in HeLa cells
    • Zhu, D. M., Tekle, E., Huang, C. Y. and Chock, P. B. (2000) Inositol tetrakisphosphate as a frequency regulator in calcium oscillations in HeLa cells. J. Biol. Chem. 275, 6063-6066
    • (2000) J. Biol. Chem. , vol.275 , pp. 6063-6066
    • Zhu, D.M.1    Tekle, E.2    Huang, C.Y.3    Chock, P.B.4
  • 2
    • 0035347166 scopus 로고    scopus 로고
    • Back in the water: The return of the inositol phosphates
    • Irvine, R. F. and Schell, M. J. (2001) Back in the water: The return of the inositol phosphates. Nat. Rev. Mol. Cell Biol. 2, 327-338
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 327-338
    • Irvine, R.F.1    Schell, M.J.2
  • 4
    • 0033029825 scopus 로고    scopus 로고
    • Inositol 1,3,4,5-tetrakisphosphate as a second messenger - A special role in neurones?
    • Irvine, R. F., McNulty, T. J. and Schell, M. J. (1999) Inositol 1,3,4,5-tetrakisphosphate as a second messenger - a special role in neurones? Chem. Phys. Lipids 98, 49-57
    • (1999) Chem. Phys. Lipids , vol.98 , pp. 49-57
    • Irvine, R.F.1    McNulty, T.J.2    Schell, M.J.3
  • 5
    • 0025303820 scopus 로고
    • Molecular cloning and expression of a complementary DNA for inositol 1,4,5-trisphosphate 3-kinase
    • Choi, K. Y., Kim, H. K., Lee, S. Y., Moon, K. H., Sim, S. S., Kim, J. W., Chung, H. K. and Rhee, S. G. (1990) Molecular cloning and expression of a complementary DNA for inositol 1,4,5-trisphosphate 3-kinase. Science 248, 64-66
    • (1990) Science , vol.248 , pp. 64-66
    • Choi, K.Y.1    Kim, H.K.2    Lee, S.Y.3    Moon, K.H.4    Sim, S.S.5    Kim, J.W.6    Chung, H.K.7    Rhee, S.G.8
  • 7
    • 0025860881 scopus 로고
    • Molecular cloning and expression of a new putative inositol 1,4,5-trisphosphate 3-kinase isoenzyme
    • Takazawa, K., Perret, J., DuMont, J. E. and Erneux, C. (1991) Molecular cloning and expression of a new putative inositol 1,4,5-trisphosphate 3-kinase isoenzyme. Biochem. J. 278, 883-886
    • (1991) Biochem. J. , vol.278 , pp. 883-886
    • Takazawa, K.1    Perret, J.2    DuMont, J.E.3    Erneux, C.4
  • 8
    • 0026016472 scopus 로고
    • Molecular cloning and expression of a human brain inositol 1,4,5-trisphosphate 3-kinase
    • Takazawa, K., Perret, J., DuMont, J. E. and Erneux, C. (1991) Molecular cloning and expression of a human brain inositol 1,4,5-trisphosphate 3-kinase. Biochem. Biophys. Res. Commun. 174, 529-535
    • (1991) Biochem. Biophys. Res. Commun. , vol.174 , pp. 529-535
    • Takazawa, K.1    Perret, J.2    DuMont, J.E.3    Erneux, C.4
  • 9
    • 0033522236 scopus 로고    scopus 로고
    • A novel A-isoform-like inositol 1,4,5-trisphosphate 3-kinase from chicken erythrocytes exhibits alternative splicing and conservation of intron positions between vertebrates and invertebrates
    • Bertsch, U., Haefs, M., Möller, M., Deschermeier, C., Fanick, W., Kitzerow, A., Ozaki, S., Meyer, H. E. and Mayr, G. W. (1999) A novel A-isoform-like inositol 1,4,5-trisphosphate 3-kinase from chicken erythrocytes exhibits alternative splicing and conservation of intron positions between vertebrates and invertebrates. Gene 228, 61-71
    • (1999) Gene , vol.228 , pp. 61-71
    • Bertsch, U.1    Haefs, M.2    Möller, M.3    Deschermeier, C.4    Fanick, W.5    Kitzerow, A.6    Ozaki, S.7    Meyer, H.E.8    Mayr, G.W.9
  • 10
    • 0032548839 scopus 로고    scopus 로고
    • Inositol trisphosphate mediates a RAS-independent response to LET-23 receptor tyrosine kinase activation in C. elegans
    • Clandinin, T., DeModena, J. and Sternberg, P. (1998) Inositol trisphosphate mediates a RAS-independent response to LET-23 receptor tyrosine kinase activation in C. elegans. Cell 92, 523-533
    • (1998) Cell , vol.92 , pp. 523-533
    • Clandinin, T.1    DeModena, J.2    Sternberg, P.3
  • 11
    • 0028047526 scopus 로고
    • Isolation and sequence of a full length cDNA encoding a novel rat inositol 1,4,5-trisphosphate 3-kinase
    • Thomas, S., Brake, B., Luzio, J. P., Stanley, K. and Banting, G. (1994) Isolation and sequence of a full length cDNA encoding a novel rat inositol 1,4,5-trisphosphate 3-kinase. Biochim. Biophys. Acta 1220, 219-222
    • (1994) Biochim. Biophys. Acta , vol.1220 , pp. 219-222
    • Thomas, S.1    Brake, B.2    Luzio, J.P.3    Stanley, K.4    Banting, G.5
  • 12
    • 0037187795 scopus 로고    scopus 로고
    • Molecular profiling of behavioural development: Differential expression of mRNAs for inositol 1,4,5-trisphosphate 3-kinase isoforms in naive and experienced honeybees (Apis mellifera)
    • Kucharski, R. and Maleszka, R. (2002) Molecular profiling of behavioural development: differential expression of mRNAs for inositol 1,4,5-trisphosphate 3-kinase isoforms in naive and experienced honeybees (Apis mellifera). Brain Res. Mol. Brain Res. 99, 92-101
    • (2002) Brain Res. Mol. Brain Res. , vol.99 , pp. 92-101
    • Kucharski, R.1    Maleszka, R.2
  • 13
    • 0032521551 scopus 로고    scopus 로고
    • 2+, inositol 1,4,5-trisphosphate and GTP-binding proteins
    • 2+, inositol 1,4,5-trisphosphate and GTP-binding proteins. Biochem. J. 330, 1149-1158
    • (1998) Biochem. J. , vol.330 , pp. 1149-1158
    • Lan, L.1    Brereton, H.2    Barritt, G.J.3
  • 15
    • 0038165444 scopus 로고    scopus 로고
    • Rat inositol 1,4,5-trisphosphate 3-kinase C is enzymatically specialized for basal cellular inositol trisphosphate phosphorylation and shuttles actively between nucleus and cytoplasm
    • Nalaskowski, M. M., Bertsch, U., Fanick, W., Stockebrand, M. C., Schmale, H. and Mayr, G. W. (2003) Rat inositol 1,4,5-trisphosphate 3-kinase C is enzymatically specialized for basal cellular inositol trisphosphate phosphorylation and shuttles actively between nucleus and cytoplasm. J. Biol Chem. 278, 19765-19776
    • (2003) J. Biol. Chem. , vol.278 , pp. 19765-19776
    • Nalaskowski, M.M.1    Bertsch, U.2    Fanick, W.3    Stockebrand, M.C.4    Schmale, H.5    Mayr, G.W.6
  • 16
    • 0034531694 scopus 로고    scopus 로고
    • Cloning and expression of a cDNA encoding human inositol 1,4,5-trisphosphate 3-kinase C
    • Dewaste, V., Pouillon, V., Moreau, C. S., Shears, S. B., Takazawa, K. and Erneux, C. (2000) Cloning and expression of a cDNA encoding human inositol 1,4,5-trisphosphate 3-kinase C. Biochem. J. 352, 343-351
    • (2000) Biochem. J. , vol.352 , pp. 343-351
    • Dewaste, V.1    Pouillon, V.2    Moreau, C.S.3    Shears, S.B.4    Takazawa, K.5    Erneux, C.6
  • 17
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechensteiner, M. and Rogers, S. W. (1996) PEST sequences and regulation by proteolysis. Trends Biochem. Sci. 21, 267-271
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 267-271
    • Rechensteiner, M.1    Rogers, S.W.2
  • 18
    • 0035813147 scopus 로고    scopus 로고
    • Inositol (1,4,5)-trisphosphate 3-kinase A associates with F-actin and dendritic spines via its N-terminus
    • Schell, M. J., Erneux, C. and Irvine, R. F. (2001) Inositol (1,4,5)-trisphosphate 3-kinase A associates with F-actin and dendritic spines via its N-terminus. J. Biol. Chem. 276, 37537-37546
    • (2001) J. Biol. Chem. , vol.276 , pp. 37537-37546
    • Schell, M.J.1    Erneux, C.2    Irvine, R.F.3
  • 21
    • 0034695549 scopus 로고    scopus 로고
    • The second messenger binding site of inositol 1,4,5-trisphosphate 3-kinase is centered in the catalytic domain and related to the inositol trisphosphate receptor site
    • Bertsch, U., Deschermeier, C., Fanick, W., Girkontaite, I., Hillemeier, K., Johnen, H., Weglöhner, W., Emmrich, F. and Mayr, G. W. (2000) The second messenger binding site of inositol 1,4,5-trisphosphate 3-kinase is centered in the catalytic domain and related to the inositol trisphosphate receptor site. J. Biol. Chem. 275, 1557-1564
    • (2000) J. Biol. Chem. , vol.275 , pp. 1557-1564
    • Bertsch, U.1    Deschermeier, C.2    Fanick, W.3    Girkontaite, I.4    Hillemeier, K.5    Johnen, H.6    Weglöhner, W.7    Emmrich, F.8    Mayr, G.W.9
  • 22
    • 0001357998 scopus 로고    scopus 로고
    • Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A. and Struhl, K., eds., John Wiley and Sons Inc., New York
    • Kingston, R. E. (1996) In Current Protocols in Molecular Biology (Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A. and Struhl, K., eds.), pp. 4.2.5-4.2.9, John Wiley and Sons Inc., New York
    • (1996) Current Protocols in Molecular Biology , pp. 425-429
    • Kingston, R.E.1
  • 23
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 25
    • 0345704610 scopus 로고
    • Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor
    • Greene, L. A. and Tischler, A. S. (1976) Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor. Proc. Natl. Acad. Sci. U.S.A. 73, 2424-2428
    • (1976) Proc. Natl. Acad. Sci. U.S.A. , vol.73 , pp. 2424-2428
    • Greene, L.A.1    Tischler, A.S.2
  • 26
    • 0021796469 scopus 로고
    • Molecular cloning of a gene sequence regulated by nerve growth factor
    • Levi, A., Elderidge, J. D. and Paterson, B. M. (1985) Molecular cloning of a gene sequence regulated by nerve growth factor. Science 229, 393-395
    • (1985) Science , vol.229 , pp. 393-395
    • Levi, A.1    Elderidge, J.D.2    Paterson, B.M.3
  • 28
    • 0036711574 scopus 로고    scopus 로고
    • The human homologue of yeast ArgRIII protein is an inositol phosphate multikinase with predominantly nuclear localization
    • Nalaskowski, M. M., Deschermeier, C., Fanick, W. and Mayr, G. W. (2002) The human homologue of yeast ArgRIII protein is an inositol phosphate multikinase with predominantly nuclear localization. Biochem. J. 366, 549-556
    • (2002) Biochem. J. , vol.366 , pp. 549-556
    • Nalaskowski, M.M.1    Deschermeier, C.2    Fanick, W.3    Mayr, G.W.4
  • 29
    • 0014199107 scopus 로고
    • Studies on the isolation and molecular properties of homogeneous globular actin
    • Rees, M. K. and Young, M. (1967) Studies on the isolation and molecular properties of homogeneous globular actin. J. Biol. Chem. 242, 4449-4458
    • (1967) J. Biol. Chem. , vol.242 , pp. 4449-4458
    • Rees, M.K.1    Young, M.2
  • 30
    • 0019853076 scopus 로고
    • 7-Chloro-4-nitro-2-oxo-1-3-diazole actin as a probe for actin polymerization
    • Detmers, P., Weber, A., Elzinga, M. and Stephens, R. E. (1981) 7-Chloro-4-nitro-2-oxo-1-3-diazole actin as a probe for actin polymerization. J. Biol. Chem. 256, 99-105
    • (1981) J. Biol. Chem. , vol.256 , pp. 99-105
    • Detmers, P.1    Weber, A.2    Elzinga, M.3    Stephens, R.E.4
  • 31
    • 0017176529 scopus 로고
    • Head to tail polymerization of actin
    • Wegner, A. (1976) Head to tail polymerization of actin. J. Mol. Biol. 108, 139-150
    • (1976) J. Mol. Biol. , vol.108 , pp. 139-150
    • Wegner, A.1
  • 32
    • 0022068293 scopus 로고
    • Preferential cleavage at aspartyl-prolyl peptide bonds in dilute acid
    • Marcus, F. (1985) Preferential cleavage at aspartyl-prolyl peptide bonds in dilute acid. Int. J. Pept. Protein Res. 25, 542-546
    • (1985) Int. J. Pept. Protein Res. , vol.25 , pp. 542-546
    • Marcus, F.1
  • 33
    • 0035103385 scopus 로고    scopus 로고
    • Nonproteolytic cleavage of aspartyl proline bonds in the cellulosomal scaffoldin subunit from Clostridium thermocellum
    • Lamed, R., Kenig, R., Morag, E., Yaron, S., Shonam, Y. and Bayer, E. A. (2001) Nonproteolytic cleavage of aspartyl proline bonds in the cellulosomal scaffoldin subunit from Clostridium thermocellum. Appl. Biochem. Biotechnol. 1, 67-73
    • (2001) Appl. Biochem. Biotechnol. , vol.1 , pp. 67-73
    • Lamed, R.1    Kenig, R.2    Morag, E.3    Yaron, S.4    Shonam, Y.5    Bayer, E.A.6
  • 34
    • 0036291401 scopus 로고    scopus 로고
    • Cloning and expression of a full-length cDNA encoding human inositol 1,4,5-trisphosphate 3-kinase B
    • Dewaste, V., Roymans, D., Moreau, C. and Erneux, C. (2002) Cloning and expression of a full-length cDNA encoding human inositol 1,4,5-trisphosphate 3-kinase B. Biochem. Biophys. Res. Commun. 291, 400-405
    • (2002) Biochem. Biophys. Res. Commun. , vol.291 , pp. 400-405
    • Dewaste, V.1    Roymans, D.2    Moreau, C.3    Erneux, C.4
  • 35
    • 0034953789 scopus 로고    scopus 로고
    • The interaction of plectin with actin: Evidence for cross-linking of actin filaments by dimerization of the actin-binding domain of plectin
    • Fontao, L., Geerts, D., Kuikman, I., Koster, J., Kramer, D. and Sonnenberg, A. (2001) The interaction of plectin with actin: evidence for cross-linking of actin filaments by dimerization of the actin-binding domain of plectin. J. Cell Sci. 114, 2065-2076
    • (2001) J. Cell Sci. , vol.114 , pp. 2065-2076
    • Fontao, L.1    Geerts, D.2    Kuikman, I.3    Koster, J.4    Kramer, D.5    Sonnenberg, A.6
  • 36
    • 0035972165 scopus 로고    scopus 로고
    • Activation of the Arp2/3 complex by the actin filament binding protein Abp1p
    • Goode, B. L., Rodal, A. A., Barnes, G. and Drubin, D. G. (2001) Activation of the Arp2/3 complex by the actin filament binding protein Abp1p. J. Cell Biol. 153, 627-634
    • (2001) J. Cell Biol. , vol.153 , pp. 627-634
    • Goode, B.L.1    Rodal, A.A.2    Barnes, G.3    Drubin, D.G.4
  • 37
    • 0033576288 scopus 로고    scopus 로고
    • Influence of the C-terminus of Wiskott-Aldrich syndrome protein (WASp) and the Arp2/3 complex on actin polymerization
    • Higgs, H. N., Blanchoin, L. and Pollard, T. D. (1999) Influence of the C-terminus of Wiskott-Aldrich syndrome protein (WASp) and the Arp2/3 complex on actin polymerization. Biochemistry 38, 15212-15222
    • (1999) Biochemistry , vol.38 , pp. 15212-15222
    • Higgs, H.N.1    Blanchoin, L.2    Pollard, T.D.3
  • 38
    • 0242552264 scopus 로고    scopus 로고
    • 3 3-kinase separates the catalytic domain from the membrane anchoring domain
    • 3 3-kinase separates the catalytic domain from the membrane anchoring domain. Biochem. J. 375, 643-651
    • (2003) Biochem. J. , vol.375 , pp. 643-651
    • Pattni, K.1    Millard, H.2    Banting, G.3
  • 39
    • 0033539916 scopus 로고    scopus 로고
    • Functional genomic analysis reveals the utility of the I/LWEQ module as a predictor of protein:actin interaction
    • McCann, R. O. and Craig, S. W. (1999) Functional genomic analysis reveals the utility of the I/LWEQ module as a predictor of protein:actin interaction. Biochem. Biophys. Res. Commun. 266, 135-140
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 135-140
    • McCann, R.O.1    Craig, S.W.2
  • 40
    • 0037138384 scopus 로고    scopus 로고
    • WH2 domain: A small, versatile adapter for actin monomers
    • Paunola, E., Mattila, P. K. and Lappalainen, P. (2002) WH2 domain: a small, versatile adapter for actin monomers. FEBS Lett. 513, 92-97
    • (2002) FEBS Lett. , vol.513 , pp. 92-97
    • Paunola, E.1    Mattila, P.K.2    Lappalainen, P.3
  • 41
    • 0031878090 scopus 로고    scopus 로고
    • The ADF homology (ADF-H) domain: A highly exploited actin-binding module
    • Lappalainen, P., Kessels, M. M., Cope, M. J. and Drubin, D. G. (1998) The ADF homology (ADF-H) domain: a highly exploited actin-binding module. Mol. Biol. Cell 8, 1951-1959
    • (1998) Mol. Biol. Cell , vol.8 , pp. 1951-1959
    • Lappalainen, P.1    Kessels, M.M.2    Cope, M.J.3    Drubin, D.G.4
  • 42
    • 0029748612 scopus 로고    scopus 로고
    • Structure function relationship of the mouse GAP1m
    • Fukuda, M. and Mikoshiba, K. (1996) Structure function relationship of the mouse GAP1m. J. Biol. Chem. 271, 18838-18842
    • (1996) J. Biol. Chem. , vol.271 , pp. 18838-18842
    • Fukuda, M.1    Mikoshiba, K.2
  • 44
    • 0032497843 scopus 로고    scopus 로고
    • Bridging the GAP in inositol 1,3,4,5-tetrakisphosphate signalling
    • Cullen, P. J. (1998) Bridging the GAP in inositol 1,3,4,5- tetrakisphosphate signalling. Biochim. Biophys. Acta 1436, 35-47
    • (1998) Biochim. Biophys. Acta , vol.1436 , pp. 35-47
    • Cullen, P.J.1
  • 47
    • 0032497840 scopus 로고    scopus 로고
    • The versatility of inositol phosphates as cellular signals
    • Shears, S. B. (1998) The versatility of inositol phosphates as cellular signals. Biochim. Biophys. Acta 1436, 49-67
    • (1998) Biochim. Biophys. Acta , vol.1436 , pp. 49-67
    • Shears, S.B.1
  • 48
    • 0035347166 scopus 로고    scopus 로고
    • Back in the water: The return of the inositol phosphates
    • Irvine, R. F. and Schell, M. J. (2001) Back in the water: the return of the inositol phosphates. Nat. Rev. Mol. Biol. 2, 327-338
    • (2001) Nat. Rev. Mol. Biol. , vol.2 , pp. 327-338
    • Irvine, R.F.1    Schell, M.J.2


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