메뉴 건너뛰기




Volumn 7, Issue 10, 2009, Pages

Capzb2 interacts with β-tubulin to regulate growth cone morphology and neurite outgrowth

Author keywords

[No Author keywords available]

Indexed keywords

BETA TUBULIN; CAPPING PROTEIN CAPZB2; CELL PROTEIN; F ACTIN; UNCLASSIFIED DRUG; ACTIN; PROTEIN CAPZ; TUBULIN;

EID: 70350503424     PISSN: 15449173     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.1000208     Document Type: Article
Times cited : (27)

References (32)
  • 1
    • 0346750747 scopus 로고    scopus 로고
    • Actin and microtubules in neurite initiation: Are MAPs the missing link?
    • Dehmelt L, Halpain S (2004) Actin and microtubules in neurite initiation: are MAPs the missing link? J Neurobiol 58: 18-33.
    • (2004) J Neurobiol , vol.58 , pp. 18-33
    • Dehmelt, L.1    Halpain, S.2
  • 2
    • 0141953237 scopus 로고    scopus 로고
    • Cytoskeletal dynamics and transport in growth cone motility and guidance
    • DOI 10.1016/S0896-6273(03)00633-0
    • Dent EW, Gertler FB (2003) Cytoskeletal dynamics and transport in growth cone motility and axon guidance. Neuron 40: 209-227. (Pubitemid 37244093)
    • (2003) Neuron , vol.40 , Issue.2 , pp. 209-227
    • Dent, E.W.1    Gertler, F.B.2
  • 3
    • 0348011611 scopus 로고    scopus 로고
    • How actin filaments and microtubules steer growth cones to their targets
    • Zhou FQ, Cohan CS (2004) How actin filaments and microtubules steer growth cones to their targets. J Neurobiol 58: 84-91.
    • (2004) J Neurobiol , vol.58 , pp. 84-91
    • Zhou, F.Q.1    Cohan, C.S.2
  • 5
    • 3442882504 scopus 로고    scopus 로고
    • Distribution of GAP-43, beta-III tubulin and F-actin in developing and regenerating axons and their growth cones in vitro, following neurotrophin treatment
    • DOI 10.1023/B:NEUR.0000021903.24849.6c
    • Avwenagha O, Campbell G, Bird MM (2003) Distribution of GAP-43, beta-III tubulin and F-actin in developing and regenerating axons and their growth cones in vitro, following neurotrophin treatment. J Neurocytol 32: 1077-1089. (Pubitemid 39004718)
    • (2003) Journal of Neurocytology , vol.32 , Issue.9 , pp. 1077-1089
    • Avwenagha, O.1    Campbell, G.2    Bird, M.M.3
  • 6
    • 4644319108 scopus 로고    scopus 로고
    • Binding partners L1 cell adhesion molecule and the ezrin-radixin-moesin (ERM) proteins are involved in development and the regenerative response to injury of hippocampal and cortical neurons
    • Haas MA, Vickers JC, Dickson TC (2004) Binding partners L1 cell adhesion molecule and the ezrin-radixin-moesin (ERM) proteins are involved in development and the regenerative response to injury of hippocampal and cortical neurons. Eur J Neurosci 20: 1436-1444.
    • (2004) Eur J Neurosci , vol.20 , pp. 1436-1444
    • Haas, M.A.1    Vickers, J.C.2    Dickson, T.C.3
  • 7
    • 0022616904 scopus 로고
    • Cytoskeletal protein abnormalities in neurodegenerative diseases
    • Goldman JE, Yen SH (1986) Cytoskeletal protein abnormalities in neurodegenerative diseases. Ann Neurol 19: 209-223.
    • (1986) Ann Neurol , vol.19 , pp. 209-223
    • Goldman, J.E.1    Yen, S.H.2
  • 8
    • 85046909683 scopus 로고    scopus 로고
    • Cell death mechanisms in neurodegeneration
    • Jellinger KA (2001) Cell death mechanisms in neurodegeneration. J Cell Mol Med 5: 1-17.
    • (2001) J Cell Mol Med , vol.5 , pp. 1-17
    • Jellinger, K.A.1
  • 9
    • 0033770166 scopus 로고    scopus 로고
    • Neurodegeneration: Diseases of the cytoskeleton?
    • McMurray CT (2000) Neurodegeneration: diseases of the cytoskeleton? Cell Death Differ 7: 861-865.
    • (2000) Cell Death Differ , vol.7 , pp. 861-865
    • McMurray, C.T.1
  • 12
    • 3943102116 scopus 로고    scopus 로고
    • Unraveling the mechanisms involved in motor neuron degeneration in ALS
    • Bruijn LI, Miller TM, Cleveland DW (2004) Unraveling the mechanisms involved in motor neuron degeneration in ALS. Annu Rev Neurosci 27: 723-749.
    • (2004) Annu Rev Neurosci , vol.27 , pp. 723-749
    • Bruijn, L.I.1    Miller, T.M.2    Cleveland, D.W.3
  • 13
    • 0348011603 scopus 로고    scopus 로고
    • Functions of Intermediate Filaments in Neuronal Development and Disease
    • DOI 10.1002/neu.10270
    • Lariviere RC, Julien JP (2004) Functions of intermediate filaments in neuronal development and disease. J Neurobiol 58: 131-148. (Pubitemid 37543344)
    • (2004) Journal of Neurobiology , vol.58 , Issue.1 , pp. 131-148
    • Lariviere, R.C.1    Julien, J.-P.2
  • 14
    • 0027480960 scopus 로고    scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • The Huntington's Disease Collaborative Research Group
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's Disease Collaborative Research Group. Cell 72: 971-983.
    • Cell , vol.72 , pp. 971-983
  • 16
    • 33645124562 scopus 로고    scopus 로고
    • Mutations in the Drosophila orthologs of the F-actin capping protein alpha- and beta-subunits cause actin accumulation and subsequent retinal degeneration
    • Delalle I, Pfleger CM, Buff E, Lueras P, Hariharan IK (2005) Mutations in the Drosophila orthologs of the F-actin capping protein alpha- and beta-subunits cause actin accumulation and subsequent retinal degeneration. Genetics 171: 1757-1765.
    • (2005) Genetics , vol.171 , pp. 1757-1765
    • Delalle, I.1    Pfleger, C.M.2    Buff, E.3    Lueras, P.4    Hariharan, I.K.5
  • 17
    • 0028173631 scopus 로고
    • 2-terminal domains of the alpha 1 and beta subunits are not required for actin capping, and alpha 1 beta and alpha 2 beta heterodimers bind differentially to actin
    • Casella JF, Torres MA (1994) Interaction of Cap Z with actin. The NH2- terminal domains of the alpha 1 and beta subunits are not required for actin capping, and alpha 1 beta and alpha 2 beta heterodimers bind differentially to actin. J Biol Chem 269: 6992-6998. (Pubitemid 24191098)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.9 , pp. 6992-6998
    • Casella, J.F.1    Torres, M.A.2
  • 18
    • 0042420366 scopus 로고    scopus 로고
    • How capping protein binds the barbed end of the actin filament
    • DOI 10.1016/S0960-9822(03)00559-1
    • Wear MA, Yamashita A, Kim K, Maeda Y, Cooper JA (2003) How capping protein binds the barbed end of the actin filament. Curr Biol 13: 1531-1537. (Pubitemid 37078410)
    • (2003) Current Biology , vol.13 , Issue.17 , pp. 1531-1537
    • Wear, M.A.1    Yamashita, A.2    Kim, K.3    Maeda, Y.4    Cooper, J.A.5
  • 19
    • 0030967785 scopus 로고    scopus 로고
    • Vertebrates have conserved capping protein alpha isoforms with specific expression patterns
    • Hart MC, Korshunova YO, Cooper JA (1997) Vertebrates have conserved capping protein alpha isoforms with specific expression patterns. Cell Motil Cytoskeleton 38: 120-132.
    • (1997) Cell Motil Cytoskeleton , vol.38 , pp. 120-132
    • Hart, M.C.1    Korshunova, Y.O.2    Cooper, J.A.3
  • 20
    • 0027959864 scopus 로고
    • Differential localization and sequence analysis of capping protein beta- Subunit isoforms of vertebrates
    • DOI 10.1083/jcb.127.2.453
    • Schafer DA, Korshunova YO, Schroer TA, Cooper JA (1994) Differential localization and sequence analysis of capping protein beta-subunit isoforms of vertebrates. J Cell Biol 127: 453-465. (Pubitemid 24313733)
    • (1994) Journal of Cell Biology , vol.127 , Issue.2 , pp. 453-465
    • Schafer, D.A.1    Korshunova, Y.O.2    Schroer, T.A.3    Cooper, J.A.4
  • 21
    • 4043115604 scopus 로고    scopus 로고
    • Lamellipodial versus filopodial mode of the actin nanomachinery: Pivotal role of the filament barbed end
    • DOI 10.1016/j.cell.2004.07.019, PII S0092867404007068
    • Mejillano MR, Kojima S, Applewhite DA, Gertler FB, Svitkina TM, et al. (2004) Lamellipodial versus filopodial mode of the actin nanomachinery: pivotal role of the filament barbed end. Cell 118: 363-373. (Pubitemid 39061116)
    • (2004) Cell , vol.118 , Issue.3 , pp. 363-373
    • Mejillano, M.R.1    Kojima, S.-I.2    Applewhite, D.A.3    Gertler, F.B.4    Svitkina, T.M.5    Borisy, G.G.6
  • 22
    • 33847315536 scopus 로고    scopus 로고
    • Spatial and temporal relationships between actinfilament nucleation, capping, and disassembly
    • Iwasa JH, Mullins RD (2007) Spatial and temporal relationships between actinfilament nucleation, capping, and disassembly. Curr Biol 17: 395-406.
    • (2007) Curr Biol , vol.17 , pp. 395-406
    • Iwasa, J.H.1    Mullins, R.D.2
  • 23
    • 0037182576 scopus 로고    scopus 로고
    • Focal loss of actin bundles causes microtubule redistribution and growth cone turning
    • Zhou FQ, Waterman-Storer CM, Cohan CS (2002) Focal loss of actin bundles causes microtubule redistribution and growth cone turning. J Cell Biol 157: 839-849.
    • (2002) J Cell Biol , vol.157 , pp. 839-849
    • Zhou, F.Q.1    Waterman-Storer, C.M.2    Cohan, C.S.3
  • 24
    • 0024511885 scopus 로고
    • Differential localisation of tyrosinated, detyrosinated, and acetylated alpha-tubulins in neurites and growth cones of dorsal root ganglion neurons
    • Robson SJ, Burgoyne RD (1989) Differential localisation of tyrosinated, detyrosinated, and acetylated alpha-tubulins in neurites and growth cones of dorsal root ganglion neurons. Cell Motil Cytoskeleton 12: 273-282.
    • (1989) Cell Motil Cytoskeleton , vol.12 , pp. 273-282
    • Robson, S.J.1    Burgoyne, R.D.2
  • 26
    • 4043147895 scopus 로고    scopus 로고
    • Capping protein: New insights into mechanism and regulation
    • DOI 10.1016/j.tibs.2004.06.003, PII S0968000404001483
    • Wear MA, Cooper JA (2004) Capping protein: new insights into mechanism and regulation. Trends Biochem Sci 29: 418-428. (Pubitemid 39061086)
    • (2004) Trends in Biochemical Sciences , vol.29 , Issue.8 , pp. 418-428
    • Wear, M.A.1    Cooper, J.A.2
  • 27
    • 0025930998 scopus 로고
    • Microtubule behavior in the growth cones of living neurons during axon elongation
    • Tanaka EM, Kirschner MW (1991) Microtubule behavior in the growth cones of living neurons during axon elongation. J Cell Biol 115: 345-363. (Pubitemid 21926032)
    • (1991) Journal of Cell Biology , vol.115 , Issue.2 , pp. 345-363
    • Tanaka, E.M.1    Kirschner, M.W.2
  • 28
    • 0035894852 scopus 로고    scopus 로고
    • Axon branching requires interactions between dynamic microtubules and actin filaments
    • Dent EW, Kalil K (2001) Axon branching requires interactions between dynamic microtubules and actin filaments. J Neurosci 21: 9757-9769.
    • (2001) J Neurosci , vol.21 , pp. 9757-9769
    • Dent, E.W.1    Kalil, K.2
  • 29
    • 0037043343 scopus 로고    scopus 로고
    • Filopodia and actin arcs guide the assembly and transport of two populations of microtubules with unique dynamic parameters in neuronal growth cones
    • DOI 10.1083/jcb.200203038
    • Schaefer AW, Kabir N, Forscher P (2002) Filopodia and actin arcs guide the assembly and transport of two populations of microtubules with unique dynamic parameters in neuronal growth cones. J Cell Biol 158: 139-152. (Pubitemid 34886728)
    • (2002) Journal of Cell Biology , vol.158 , Issue.1 , pp. 139-152
    • Schaefer, A.W.1    Kabir, N.2    Forscher, P.3
  • 30
    • 1542395746 scopus 로고    scopus 로고
    • Hippocampal protein-protein interactions in spatial memory
    • DOI 10.1002/hipo.10152
    • Nelson TJ, Backlund PS Jr, Alkon DL (2004) Hippocampal protein-protein interactions in spatial memory. Hippocampus 14: 46-57. (Pubitemid 38351171)
    • (2004) Hippocampus , vol.14 , Issue.1 , pp. 46-57
    • Nelson, T.J.1    Backlund Jr., P.S.2    Alkon, D.L.3
  • 32
    • 17144399857 scopus 로고    scopus 로고
    • High-efficiency protein extraction from polyacrylamide gels for molecular mass measurement by matrix-assisted laser desorption/ionization-time of flight-mass spectrometry
    • DOI 10.1002/elps.200410187
    • Jin Y, Manabe T (2005) High-efficiency protein extraction from polyacrylamide gels for molecular mass measurement by matrix-assisted laser desorption/ ionization-time of flight-mass spectrometry. Electrophoresis 26: 1019-1028. (Pubitemid 40514792)
    • (2005) Electrophoresis , vol.26 , Issue.6 , pp. 1019-1028
    • Jin, Y.1    Manabe, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.