메뉴 건너뛰기




Volumn 359, Issue 2, 2007, Pages 398-401

Drebrin attenuates the interaction between actin and myosin-V

Author keywords

Actin dynamics; Actin binding protein; ATPase; Dendritic spine; Drebrin; In vitro motility assay; Myosin V

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; ADENOSINE TRIPHOSPHATASE (MAGNESIUM); DREBRIN; F ACTIN; MYOSIN V;

EID: 34249948905     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.05.123     Document Type: Article
Times cited : (34)

References (29)
  • 1
    • 0034721711 scopus 로고    scopus 로고
    • Actin-based plasticity in dendritic spines
    • Matus A. Actin-based plasticity in dendritic spines. Science 290 (2000) 754-758
    • (2000) Science , vol.290 , pp. 754-758
    • Matus, A.1
  • 2
    • 15944369335 scopus 로고    scopus 로고
    • Spine architecture and synaptic plasticity
    • Carlisle H.J., and Kennedy M.B. Spine architecture and synaptic plasticity. Trends Neurosci. 28 (2005) 182-187
    • (2005) Trends Neurosci. , vol.28 , pp. 182-187
    • Carlisle, H.J.1    Kennedy, M.B.2
  • 3
    • 0033529082 scopus 로고    scopus 로고
    • Dendritic spine changes associated with hippocampal long-term synaptic plasticity
    • Engert F., and Bonhoeffer F. Dendritic spine changes associated with hippocampal long-term synaptic plasticity. Nature 399 (1999) 66-70
    • (1999) Nature , vol.399 , pp. 66-70
    • Engert, F.1    Bonhoeffer, F.2
  • 4
    • 0033583022 scopus 로고    scopus 로고
    • Rapid dendritic morphogenesis in CA1 hippocampal dendrites induced by synaptic activity
    • Maletic-Savatic M., and Svoboda M.K. Rapid dendritic morphogenesis in CA1 hippocampal dendrites induced by synaptic activity. Science 283 (1999) 1923-1927
    • (1999) Science , vol.283 , pp. 1923-1927
    • Maletic-Savatic, M.1    Svoboda, M.K.2
  • 5
    • 3042554012 scopus 로고    scopus 로고
    • Structural basis of long-term potentiation in single dendritic spines
    • Matsuzaki M., Honkura N., Ellis-Davies G.C.R., and Kasai H. Structural basis of long-term potentiation in single dendritic spines. Nature 429 (2004) 761-766
    • (2004) Nature , vol.429 , pp. 761-766
    • Matsuzaki, M.1    Honkura, N.2    Ellis-Davies, G.C.R.3    Kasai, H.4
  • 6
    • 9644278075 scopus 로고    scopus 로고
    • Shrinkage of dendritic spines associated with long-term depression of hippocampal synapses
    • Zhou Q., Homma K.J., and Poo M.-m. Shrinkage of dendritic spines associated with long-term depression of hippocampal synapses. Neuron 44 (2004) 749-757
    • (2004) Neuron , vol.44 , pp. 749-757
    • Zhou, Q.1    Homma, K.J.2    Poo, M.-m.3
  • 7
    • 30644456796 scopus 로고    scopus 로고
    • A critical role for myosin IIB in dendritic spine morphology and synaptic function
    • Ryu J., Liu L., Wang T.P., Wu D.C., Burette A., Weinberg R., Wang Y.T., and Sheng M. A critical role for myosin IIB in dendritic spine morphology and synaptic function. Neuron 49 (2006) 175-182
    • (2006) Neuron , vol.49 , pp. 175-182
    • Ryu, J.1    Liu, L.2    Wang, T.P.3    Wu, D.C.4    Burette, A.5    Weinberg, R.6    Wang, Y.T.7    Sheng, M.8
  • 8
    • 0034660288 scopus 로고    scopus 로고
    • Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein
    • Naisbitt S., Veltschanoff J., Allison D.W., Sala C., Kim E., Greig A.M., Weinberg R.J., and Sheng M. Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein. J. Neurosci. 20 (2000) 4524-4534
    • (2000) J. Neurosci. , vol.20 , pp. 4524-4534
    • Naisbitt, S.1    Veltschanoff, J.2    Allison, D.W.3    Sala, C.4    Kim, E.5    Greig, A.M.6    Weinberg, R.J.7    Sheng, M.8
  • 10
    • 85047673845 scopus 로고
    • The roles of microfilament-associated, proteins, drebrins in brain morphogenesis: a review
    • Shirao T. The roles of microfilament-associated, proteins, drebrins in brain morphogenesis: a review. J. Biochem. 117 (1995) 231-236
    • (1995) J. Biochem. , vol.117 , pp. 231-236
    • Shirao, T.1
  • 11
    • 0023718581 scopus 로고
    • Nucleotide sequences of two embryonic drebrins, developmentally regulated brain proteins, and developmental change in their mRNAs
    • Kojima N., Kato Y., Shirao T., and Obata K. Nucleotide sequences of two embryonic drebrins, developmentally regulated brain proteins, and developmental change in their mRNAs. Brain Res. 464 (1988) 207-215
    • (1988) Brain Res. , vol.464 , pp. 207-215
    • Kojima, N.1    Kato, Y.2    Shirao, T.3    Obata, K.4
  • 12
    • 0030040876 scopus 로고    scopus 로고
    • Inhibition by drebrin of the actin-bundling activity of brain fascin, a protein localized in filopodia of growth cones
    • Sasaki Y., Hayashi K., Shirao T., Ishikawa R., and Kohama K. Inhibition by drebrin of the actin-bundling activity of brain fascin, a protein localized in filopodia of growth cones. J. Neurochem. 66 (1996) 980-988
    • (1996) J. Neurochem. , vol.66 , pp. 980-988
    • Sasaki, Y.1    Hayashi, K.2    Shirao, T.3    Ishikawa, R.4    Kohama, K.5
  • 13
    • 0029825623 scopus 로고    scopus 로고
    • Modulatory role of drebrin on the cytoskeleton within dendritic spines in the rat cerebral cortex
    • Hayashi K., Ishikawa R., Ye L.-H., He X.-L., Takata K., Kohama K., and Shirao T. Modulatory role of drebrin on the cytoskeleton within dendritic spines in the rat cerebral cortex. J. Neurosci. 16 (1996) 7161-7170
    • (1996) J. Neurosci. , vol.16 , pp. 7161-7170
    • Hayashi, K.1    Ishikawa, R.2    Ye, L.-H.3    He, X.-L.4    Takata, K.5    Kohama, K.6    Shirao, T.7
  • 14
    • 0041342023 scopus 로고    scopus 로고
    • Drebrin-dependent actin clustering in dendritic filopodia governs synaptic targeting of postsynaptic density-95 and dendritic spine morphogenesis
    • Takahashi H., Sekino Y., Tanaka S., Mizui T., Kishi S., and Shirao T. Drebrin-dependent actin clustering in dendritic filopodia governs synaptic targeting of postsynaptic density-95 and dendritic spine morphogenesis. J. Neurosci. 23 (2003) 6586-6595
    • (2003) J. Neurosci. , vol.23 , pp. 6586-6595
    • Takahashi, H.1    Sekino, Y.2    Tanaka, S.3    Mizui, T.4    Kishi, S.5    Shirao, T.6
  • 15
    • 0033562792 scopus 로고    scopus 로고
    • Change in the shape of dendritic spines caused by overexpression of drebrin in cultured cortical neurons
    • Hayashi K., and Shirao T. Change in the shape of dendritic spines caused by overexpression of drebrin in cultured cortical neurons. J. Neurosci. 15 (1999) 3918-3925
    • (1999) J. Neurosci. , vol.15 , pp. 3918-3925
    • Hayashi, K.1    Shirao, T.2
  • 16
    • 23644462713 scopus 로고    scopus 로고
    • Overexpression of drebrin A in immature neurons induces the accumulation of F-actin and PSD-95 into dendritc filopodia, and the formation of large abnormal protrusions
    • Mizui T., Takahashi H., Sekino Y., and Shirao T. Overexpression of drebrin A in immature neurons induces the accumulation of F-actin and PSD-95 into dendritc filopodia, and the formation of large abnormal protrusions. Mol. Cell. Neurosci. 30 (2005) 149-157
    • (2005) Mol. Cell. Neurosci. , vol.30 , pp. 149-157
    • Mizui, T.1    Takahashi, H.2    Sekino, Y.3    Shirao, T.4
  • 17
    • 2342622581 scopus 로고    scopus 로고
    • Antisense knockdown of drebrin A, a dendritic spine protein, causes stronger reference, impaired pre-pulse inhibition, and an increased sensitivity to psychostimulant
    • Kobayashi R., Sekino Y., Shirao T., Tanaka S., Ogura T., Inada K., and Saji M. Antisense knockdown of drebrin A, a dendritic spine protein, causes stronger reference, impaired pre-pulse inhibition, and an increased sensitivity to psychostimulant. Neurosci. Res. 49 (2004) 205-217
    • (2004) Neurosci. Res. , vol.49 , pp. 205-217
    • Kobayashi, R.1    Sekino, Y.2    Shirao, T.3    Tanaka, S.4    Ogura, T.5    Inada, K.6    Saji, M.7
  • 18
    • 0020538452 scopus 로고
    • Isolation and characterization of tropomyosin-containing microfilaments from cultured cells
    • Matsumura F., Yamashiro-Matsumura S., and Lin J.J.-C. Isolation and characterization of tropomyosin-containing microfilaments from cultured cells. J. Biol. Chem. 258 (1983) 6636-6644
    • (1983) J. Biol. Chem. , vol.258 , pp. 6636-6644
    • Matsumura, F.1    Yamashiro-Matsumura, S.2    Lin, J.J.-C.3
  • 20
    • 0032500661 scopus 로고    scopus 로고
    • Regulation of actin bundling activities of fascin by caldesmon coupled with tropomyosin
    • Ishikawa R., Yamashiro S., Kohama K., and Matsumura F. Regulation of actin bundling activities of fascin by caldesmon coupled with tropomyosin. J. Biol. Chem. 273 (1998) 26991-26997
    • (1998) J. Biol. Chem. , vol.273 , pp. 26991-26997
    • Ishikawa, R.1    Yamashiro, S.2    Kohama, K.3    Matsumura, F.4
  • 21
    • 0033850082 scopus 로고    scopus 로고
    • ADP inhibition of myosin V ATPase activity
    • De La Cruz E.M., Sweeney H.L., and Ostap E.M. ADP inhibition of myosin V ATPase activity. Biophys. J. 79 (2000) 1524-1529
    • (2000) Biophys. J. , vol.79 , pp. 1524-1529
    • De La Cruz, E.M.1    Sweeney, H.L.2    Ostap, E.M.3
  • 23
    • 0028139040 scopus 로고
    • Drebrin, a development-associated brain protein from rat embryo, causes the dissociation of tropomyosin from actin filaments
    • Ishikawa R., Hayashi K., Shirao T., Xue Y., Takagi T., Sasaki Y., and Kohama K. Drebrin, a development-associated brain protein from rat embryo, causes the dissociation of tropomyosin from actin filaments. J. Biol. Chem. 269 (1994) 29928-29933
    • (1994) J. Biol. Chem. , vol.269 , pp. 29928-29933
    • Ishikawa, R.1    Hayashi, K.2    Shirao, T.3    Xue, Y.4    Takagi, T.5    Sasaki, Y.6    Kohama, K.7
  • 26
    • 33751428390 scopus 로고    scopus 로고
    • Myosin-Va facilitates the accumulation of mRNA/protein complex in dendritic spines
    • Yoshimura A., Fujii R., Watanabe Y., Okabe S., Fukui K., and Takumi T. Myosin-Va facilitates the accumulation of mRNA/protein complex in dendritic spines. Curr. Biol. 16 (2006) 2345-2351
    • (2006) Curr. Biol. , vol.16 , pp. 2345-2351
    • Yoshimura, A.1    Fujii, R.2    Watanabe, Y.3    Okabe, S.4    Fukui, K.5    Takumi, T.6
  • 27
    • 33646830444 scopus 로고    scopus 로고
    • Down-regulation of drebrin A expression suppresses synaptic targeting of NMDA receptors in developing hippocampal neurones
    • Takahashi H., Mizui T., and Shirao S. Down-regulation of drebrin A expression suppresses synaptic targeting of NMDA receptors in developing hippocampal neurones. J. Neurochem. 97 Suppl. 1 (2006) 110-115
    • (2006) J. Neurochem. , vol.97 , Issue.SUPPL. 1 , pp. 110-115
    • Takahashi, H.1    Mizui, T.2    Shirao, S.3
  • 28
    • 0037459061 scopus 로고    scopus 로고
    • The molecular motor toolbox for intracellular transport
    • Vale R.D. The molecular motor toolbox for intracellular transport. Cell 112 (2003) 467-480
    • (2003) Cell , vol.112 , pp. 467-480
    • Vale, R.D.1
  • 29
    • 4344664038 scopus 로고    scopus 로고
    • Dynamics and inheritance of the endoplasmic reticulum
    • Du U., Ferro-Novick S., and Novick P. Dynamics and inheritance of the endoplasmic reticulum. J. Cell Sci. 117 (2004) 2871-2878
    • (2004) J. Cell Sci. , vol.117 , pp. 2871-2878
    • Du, U.1    Ferro-Novick, S.2    Novick, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.