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Volumn 103, Issue 4, 2007, Pages 1319-1333

TRPV1 expression-dependent initiation and regulation of filopodia

Author keywords

Cytoskeletal rearrangement; Filopodia; Microtubules; Myosin; Neurite; TRPV

Indexed keywords

VANILLOID RECEPTOR 1;

EID: 35448937926     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2007.04846.x     Document Type: Article
Times cited : (48)

References (87)
  • 1
    • 33646508347 scopus 로고    scopus 로고
    • The effect of neurotrophic factors on morphology, TRPV1 expression and capsaicin responses of cultured human DRG sensory neurons
    • Anand U., Otto W. R., Casula M. A., Day N. C., Davis J. B., Bountra C., Birch R. Anand P. (2006) The effect of neurotrophic factors on morphology, TRPV1 expression and capsaicin responses of cultured human DRG sensory neurons. Neurosci. Lett. 399, 51 56.
    • (2006) Neurosci. Lett. , vol.399 , pp. 51-56
    • Anand, U.1    Otto, W.R.2    Casula, M.A.3    Day, N.C.4    Davis, J.B.5    Bountra, C.6    Birch, R.7    Anand, P.8
  • 3
    • 0345133276 scopus 로고    scopus 로고
    • Myosin XVa localizes to the tips of inner ear sensory cell stereocilia and is essential for staircase formation of the hair bundle
    • Belyantseva I. A., Boger E. T. Friedman T. B. (2003) Myosin XVa localizes to the tips of inner ear sensory cell stereocilia and is essential for staircase formation of the hair bundle. Proc. Natl Acad. Sci. USA 100, 13958 13963.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 13958-13963
    • Belyantseva, I.A.1    Boger, E.T.2    Friedman, T.B.3
  • 4
    • 34047250470 scopus 로고    scopus 로고
    • Calmodulin-like protein increases filopodia-dependent cell motility via up-regulation of myosin-10
    • Bennett R. D., Mauer A. S. Strehler E. E. (2007) Calmodulin-like protein increases filopodia-dependent cell motility via up-regulation of myosin-10. J. Biol. Chem. 282, 3205 3212.
    • (2007) J. Biol. Chem. , vol.282 , pp. 3205-3212
    • Bennett, R.D.1    Mauer, A.S.2    Strehler, E.E.3
  • 5
    • 0036122307 scopus 로고    scopus 로고
    • Myosin-X is an unconventional myosin that undergoes intrafilopodial motility
    • Berg J. S. Cheney R. E. (2002) Myosin-X is an unconventional myosin that undergoes intrafilopodial motility. Nat. Cell Biol. 4, 246 250.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 246-250
    • Berg, J.S.1    Cheney, R.E.2
  • 6
    • 0033766768 scopus 로고    scopus 로고
    • Myosin-X, a novel myosin with pleckstrin homology domains, associates with regions of dynamic actin
    • Berg J. S., Derfler B. H., Pennisi C. M., Corey D. P. Cheney R. E. (2000) Myosin-X, a novel myosin with pleckstrin homology domains, associates with regions of dynamic actin. J. Cell Sci. 113, 3439 3451.
    • (2000) J. Cell Sci. , vol.113 , pp. 3439-3451
    • Berg, J.S.1    Derfler, B.H.2    Pennisi, C.M.3    Corey, D.P.4    Cheney, R.E.5
  • 7
    • 0037104657 scopus 로고    scopus 로고
    • CAMP- dependent protein kinase regulates desensitization of the capsaicin receptor (VR1) by direct phosphorylation
    • Bhave G, Zhu W, Wang H, Brasier D. J., Oxford G. S. Gereau III. R. W. (2002) cAMP- dependent protein kinase regulates desensitization of the capsaicin receptor (VR1) by direct phosphorylation. Neuron 35, 721 731.
    • (2002) Neuron , vol.35 , pp. 721-731
    • Bhave, G.1    Zhu, W.2    Wang, H.3    Brasier, D.J.4    Oxford, G.S.5    Gereauiii., R.W.6
  • 9
    • 33747622327 scopus 로고    scopus 로고
    • Myosin-X is a molecular motor that functions in filopodia formation
    • Bohil A. B., Robertson B. W. Cheney R. E. (2006) Myosin-X is a molecular motor that functions in filopodia formation. Proc. Natl Acad. Sci. USA 103, 12411 12416.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 12411-12416
    • Bohil, A.B.1    Robertson, B.W.2    Cheney, R.E.3
  • 12
    • 0026326667 scopus 로고
    • Substrate-bound factors stimulate engorgement of growth cone lamellipodia during neurite elongation
    • Burmeister D. W., Rivas R. J. Goldberg D. J. (1991) Substrate-bound factors stimulate engorgement of growth cone lamellipodia during neurite elongation. Cell Motil. Cytoskeleton 19, 255 268.
    • (1991) Cell Motil. Cytoskeleton , vol.19 , pp. 255-268
    • Burmeister, D.W.1    Rivas, R.J.2    Goldberg, D.J.3
  • 13
    • 0346729934 scopus 로고    scopus 로고
    • Myosin-Va binds to and mechanochemically couples microtubules to actin filaments
    • Cao T. T., Chang W., Masters S. E. Mooseker M. S. (2004) Myosin-Va binds to and mechanochemically couples microtubules to actin filaments. Mol. Biol. Cell 15, 151 161.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 151-161
    • Cao, T.T.1    Chang, W.2    Masters, S.E.3    Mooseker, M.S.4
  • 15
    • 27744542635 scopus 로고    scopus 로고
    • Local calcium transients contribute to disappearance of pFAK, focal complex removal and deadhesion of neuronal growth cones and fibroblasts
    • Conklin M. W., Lin M. S. Spitzer N. C. (2005) Local calcium transients contribute to disappearance of pFAK, focal complex removal and deadhesion of neuronal growth cones and fibroblasts. Dev. Biol. 287, 201 212.
    • (2005) Dev. Biol. , vol.287 , pp. 201-212
    • Conklin, M.W.1    Lin, M.S.2    Spitzer, N.C.3
  • 16
    • 0029998871 scopus 로고    scopus 로고
    • The dynamics of dendritic structure in developing hippocampal slices
    • Dailey M. E. Smith S. J. (1996) The dynamics of dendritic structure in developing hippocampal slices. J. Neurosci. 16, 2983 2994.
    • (1996) J. Neurosci. , vol.16 , pp. 2983-2994
    • Dailey, M.E.1    Smith, S.J.2
  • 17
    • 0141953237 scopus 로고    scopus 로고
    • Cytoskeletal dynamics and transport in growth cone motility and axon guidance
    • Dent E. W. Gertler F. B. (2003) Cytoskeletal dynamics and transport in growth cone motility and axon guidance. Neuron 40, 209 227.
    • (2003) Neuron , vol.40 , pp. 209-227
    • Dent, E.W.1    Gertler, F.B.2
  • 18
    • 33748188892 scopus 로고    scopus 로고
    • Artemin overexpression in skin enhances expression of TRPV1 and TRPA1 in cutaneous sensory neurons and leads to behavioral sensitivity to heat and cold
    • Elitt C. M., McIlwrath S. L., Lawson J. J., Malin S. A., Molliver D. C., Cornuet P. K., Koerber H. R., Davis B. M. Albers K. M. (2006) Artemin overexpression in skin enhances expression of TRPV1 and TRPA1 in cutaneous sensory neurons and leads to behavioral sensitivity to heat and cold. J. Neurosci. 26, 8578 8587.
    • (2006) J. Neurosci. , vol.26 , pp. 8578-8587
    • Elitt, C.M.1    McIlwrath, S.L.2    Lawson, J.J.3    Malin, S.A.4    Molliver, D.C.5    Cornuet, P.K.6    Koerber, H.R.7    Davis, B.M.8    Albers, K.M.9
  • 20
    • 0033103186 scopus 로고    scopus 로고
    • Braking news: Calcium in the growth cone
    • Goldberg D. J. Grabham P. W. (1999) Braking news: calcium in the growth cone. Neuron 22, 423 425.
    • (1999) Neuron , vol.22 , pp. 423-425
    • Goldberg, D.J.1    Grabham, P.W.2
  • 21
    • 0033866380 scopus 로고    scopus 로고
    • Regulation of growth cone behavior by calcium: New dynamics to earlier perspectives
    • Gomez T. M. Spitzer N. C. (2000) Regulation of growth cone behavior by calcium: new dynamics to earlier perspectives. J. Neurobiol. 44, 174 183.
    • (2000) J. Neurobiol. , vol.44 , pp. 174-183
    • Gomez, T.M.1    Spitzer, N.C.2
  • 22
    • 31444455532 scopus 로고    scopus 로고
    • The molecular basis for calcium-dependent axon pathfinding
    • Gomez T.M. Zheng J.Q. (2006) The molecular basis for calcium-dependent axon pathfinding. Nat. Rev. Neurosci. 7, 115 125.
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 115-125
    • Gomez, T.M.1    Zheng, J.Q.2
  • 23
    • 0035831318 scopus 로고    scopus 로고
    • Filopodial calcium transients promote substrate-dependent growth cone turning
    • Gomez T. M., Robles E., Poo M. Spitzer N. C. (2001) Filopodial calcium transients promote substrate-dependent growth cone turning. Science 291, 1983 1987.
    • (2001) Science , vol.291 , pp. 1983-1987
    • Gomez, T.M.1    Robles, E.2    Poo, M.3    Spitzer, N.C.4
  • 24
    • 0347381071 scopus 로고    scopus 로고
    • Microtubules and growth cone function
    • Gordon-Weeks P. R. (2004) Microtubules and growth cone function. J. Neurobiol. 58, 70 83.
    • (2004) J. Neurobiol. , vol.58 , pp. 70-83
    • Gordon-Weeks, P.R.1
  • 26
    • 33644842683 scopus 로고    scopus 로고
    • Rapid disassembly of dynamic microtubules upon activation of the capsaicin receptor TRPV1
    • Goswami C., Dreger M., Otto H., Schwappach B. Hucho F. (2006) Rapid disassembly of dynamic microtubules upon activation of the capsaicin receptor TRPV1. J. Neurochem. 96, 254 266.
    • (2006) J. Neurochem. , vol.96 , pp. 254-266
    • Goswami, C.1    Dreger, M.2    Otto, H.3    Schwappach, B.4    Hucho, F.5
  • 27
    • 33947244356 scopus 로고    scopus 로고
    • Identification and characterisation of novel tubulin-binding motifs located within the C-terminus of TRPV1
    • Goswami C., Hucho T. B. Hucho F. (2007a) Identification and characterisation of novel tubulin-binding motifs located within the C-terminus of TRPV1. J. Neurochem. 101, 250 262.
    • (2007) J. Neurochem. , vol.101 , pp. 250-262
    • Goswami, C.1    Hucho, T.B.2    Hucho, F.3
  • 28
    • 33846432715 scopus 로고    scopus 로고
    • TRPV1 at nerve endings regulates growth cone morphology and movement through cytoskeleton reorganization
    • Goswami C., Schmidt H. Hucho F. (2007b) TRPV1 at nerve endings regulates growth cone morphology and movement through cytoskeleton reorganization. FEBS J. 274, 760 772.
    • (2007) FEBS J. , vol.274 , pp. 760-772
    • Goswami, C.1    Schmidt, H.2    Hucho, F.3
  • 30
    • 0041708061 scopus 로고    scopus 로고
    • TRPC5 is a regulator of hippocampal neurite length and growth cone morphology Nat
    • Greka A., Navarro B., Oancea E., Duggan A. Clapham D. E. (2003) TRPC5 is a regulator of hippocampal neurite length and growth cone morphology Nat. Neuroscience 6, 37 45.
    • (2003) Neuroscience , vol.6 , pp. 37-45
    • Greka, A.1    Navarro, B.2    Oancea, E.3    Duggan, A.4    Clapham, D.E.5
  • 31
    • 0021752265 scopus 로고
    • Distinct populations of microtubules: Tyrosinated and nontyrosinated alpha tubulin are distributed differently in vivo
    • Gundersen G. G., Kalnoski M. H. Bulinski J. C. (1984) Distinct populations of microtubules: tyrosinated and nontyrosinated alpha tubulin are distributed differently in vivo. Cell 38, 779 789.
    • (1984) Cell , vol.38 , pp. 779-789
    • Gundersen, G.G.1    Kalnoski, M.H.2    Bulinski, J.C.3
  • 34
    • 0034016830 scopus 로고    scopus 로고
    • Man to trypanosome: The tubulin tyrosination/detyrosination cycle revisited
    • Idriss H. T. (2000) Man to trypanosome: the tubulin tyrosination/ detyrosination cycle revisited. Cell Motil. Cytoskeleton 45, 173 184.
    • (2000) Cell Motil. Cytoskeleton , vol.45 , pp. 173-184
    • Idriss, H.T.1
  • 36
    • 0035721695 scopus 로고    scopus 로고
    • Biochemical characterization of the vanilloid receptor 1 expressed in a dorsal root ganglia derived cell line
    • Jahnel R., Dreger M., Gillen C., Bender O., Kurreck J. Hucho F. (2001) Biochemical characterization of the vanilloid receptor 1 expressed in a dorsal root ganglia derived cell line. Eur. J. Biochem. 268, 5489 5496.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5489-5496
    • Jahnel, R.1    Dreger, M.2    Gillen, C.3    Bender, O.4    Kurreck, J.5    Hucho, F.6
  • 38
    • 0033662411 scopus 로고    scopus 로고
    • Filopodia, spines, and the generation of synaptic diversity
    • Jontes J. D. Smith S. J. (2000) Filopodia, spines, and the generation of synaptic diversity. Neuron 27, 11 14.
    • (2000) Neuron , vol.27 , pp. 11-14
    • Jontes, J.D.1    Smith, S.J.2
  • 40
    • 0023403268 scopus 로고
    • Microtubules containing detyrosinated tubulin are less dynamic
    • Kreis T. E. (1987) Microtubules containing detyrosinated tubulin are less dynamic. EMBO J. 6, 2597 2606.
    • (1987) EMBO J. , vol.6 , pp. 2597-2606
    • Kreis, T.E.1
  • 41
    • 18844424570 scopus 로고    scopus 로고
    • Identification of a protein that interacts with the vanilloid receptor
    • Lee S. Y. (2005) Identification of a protein that interacts with the vanilloid receptor. Biochem. Biophys. Res. Commun. 331, 1445 1451.
    • (2005) Biochem. Biophys. Res. Commun. , vol.331 , pp. 1445-1451
    • Lee, S.Y.1
  • 42
    • 0141429959 scopus 로고    scopus 로고
    • Localization of a class III myosin to filopodia tips in transfected HeLa cells requires an actin-binding site in its tail domain
    • Les Erickson F., Corsa A. C., Dose A. C. Burnside B. (2003) Localization of a class III myosin to filopodia tips in transfected HeLa cells requires an actin-binding site in its tail domain. Mol. Biol. Cell 14, 4173 4180.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4173-4180
    • Les Erickson, F.1    Corsa, A.C.2    Dose, A.C.3    Burnside, B.4
  • 43
    • 0029863153 scopus 로고    scopus 로고
    • Myosin drives retrograde F-actin flow in neuronal growth cones
    • Lin C. H., Espreafico E. M., Mooseker M. S. Forscher P. (1996) Myosin drives retrograde F-actin flow in neuronal growth cones. Neuron 16, 769 782.
    • (1996) Neuron , vol.16 , pp. 769-782
    • Lin, C.H.1    Espreafico, E.M.2    Mooseker, M.S.3    Forscher, P.4
  • 44
    • 14544268543 scopus 로고    scopus 로고
    • Local calcium transients regulate the spontaneous motility of dendritic filopodia
    • Lohmann C., Finski A. Bonhoeffer T. (2005) Local calcium transients regulate the spontaneous motility of dendritic filopodia. Nat. Neurosci. 8, 305 312.
    • (2005) Nat. Neurosci. , vol.8 , pp. 305-312
    • Lohmann, C.1    Finski, A.2    Bonhoeffer, T.3
  • 45
  • 46
    • 33745801976 scopus 로고    scopus 로고
    • RhoA-kinase and myosin II are required for the maintenance of growth cone polarity and guidance by nerve growth factor
    • Loudon R. P., Silver L. D., Yee Jr. H. F. Gallo G. (2006) RhoA-kinase and myosin II are required for the maintenance of growth cone polarity and guidance by nerve growth factor. J. Neurobiol. 66, 847 867.
    • (2006) J. Neurobiol. , vol.66 , pp. 847-867
    • Loudon, R.P.1    Silver, L.D.2    Yeejr., H.F.3    Gallo, G.4
  • 47
    • 15744394354 scopus 로고    scopus 로고
    • TRPV1b, a functional human vanilloid receptor splice variant
    • Lu G., Henderson D., Liu L., Reinhart P. H. Simon S. A. (2005) TRPV1b, a functional human vanilloid receptor splice variant. Mol. Pharmacol. 67, 1119 1127.
    • (2005) Mol. Pharmacol. , vol.67 , pp. 1119-1127
    • Lu, G.1    Henderson, D.2    Liu, L.3    Reinhart, P.H.4    Simon, S.A.5
  • 48
    • 0031039519 scopus 로고    scopus 로고
    • Tubulin post-translational modifications-enzymes and their mechanisms of action
    • MacRae T. H. (1997) Tubulin post-translational modifications-enzymes and their mechanisms of action. Eur. J. Biochem. 244, 265 278.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 265-278
    • MacRae, T.H.1
  • 49
    • 0032825265 scopus 로고    scopus 로고
    • Regulated actin cytoskeleton assembly at filopodium tips controls their extension and retraction
    • Mallavarapu A. Mitchison T. (1999) Regulated actin cytoskeleton assembly at filopodium tips controls their extension and retraction. J. Cell Biol. 146, 1097 1106.
    • (1999) J. Cell Biol. , vol.146 , pp. 1097-1106
    • Mallavarapu, A.1    Mitchison, T.2
  • 51
    • 33644775671 scopus 로고    scopus 로고
    • Myosin II functions in actin-bundle turnover in neuronal growth cones
    • Medeiros N. A., Burnette D. T. Forscher P. (2006) Myosin II functions in actin-bundle turnover in neuronal growth cones. Nat. Cell Biol. 8, 215 226.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 215-226
    • Medeiros, N.A.1    Burnette, D.T.2    Forscher, P.3
  • 52
    • 33746032231 scopus 로고    scopus 로고
    • Subcellular translocation of the eGFP-tagged TRPL channel in Drosophila photoreceptors requires activation of the phototransduction cascade
    • Meyer N. E., Joel-Almagor T., Frechter S., Minke B. Huber A. (2006) Subcellular translocation of the eGFP-tagged TRPL channel in Drosophila photoreceptors requires activation of the phototransduction cascade. J. Cell Sci. 119, 2592 2603.
    • (2006) J. Cell Sci. , vol.119 , pp. 2592-2603
    • Meyer, N.E.1    Joel-Almagor, T.2    Frechter, S.3    Minke, B.4    Huber, A.5
  • 53
    • 0030049170 scopus 로고    scopus 로고
    • Actin-based cell motility and cell locomotion
    • Mitchison T. J. Cramer L. P. (1996) Actin-based cell motility and cell locomotion. Cell 84, 371 379.
    • (1996) Cell , vol.84 , pp. 371-379
    • Mitchison, T.J.1    Cramer, L.P.2
  • 54
    • 2942614748 scopus 로고    scopus 로고
    • Regulated exocytosis contributes to protein kinase C potentiation of vanilloid receptor activity
    • Morenilla-Palao C., Planells-Cases R., Garcia-Sanz N. Ferrer-Montiel A. (2004) Regulated exocytosis contributes to protein kinase C potentiation of vanilloid receptor activity. J. Biol. Chem. 279, 25665 25672.
    • (2004) J. Biol. Chem. , vol.279 , pp. 25665-25672
    • Morenilla-Palao, C.1    Planells-Cases, R.2    Garcia-Sanz, N.3    Ferrer-Montiel, A.4
  • 56
    • 16244372090 scopus 로고    scopus 로고
    • Calcium regulation of actin dynamics in dendritic spines
    • Oertner T. G. Matus A. (2005) Calcium regulation of actin dynamics in dendritic spines. Cell Calcium. 37, 477 482.
    • (2005) Cell Calcium. , vol.37 , pp. 477-482
    • Oertner, T.G.1    Matus, A.2
  • 57
    • 0037144453 scopus 로고    scopus 로고
    • Protein kinase C(alpha) is required for vanilloid receptor 1 activation. Evidence for multiple signaling pathways
    • Olah Z., Karai L. Iadarola M. J. (2002) Protein kinase C(alpha) is required for vanilloid receptor 1 activation. Evidence for multiple signaling pathways. J. Biol. Chem. 277, 35752 35759.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35752-35759
    • Olah, Z.1    Karai, L.2    Iadarola, M.J.3
  • 58
    • 0039154020 scopus 로고
    • Neuronal traits of clonal cell lines derived by fusion of dorsal root ganglia neurons with neuroblastoma cells
    • Platika D., Boulos M. H., Baizer L. Fishman M. C. (1985) Neuronal traits of clonal cell lines derived by fusion of dorsal root ganglia neurons with neuroblastoma cells. Proc. Natl Acad. Sci. USA 82, 3499 3503.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 3499-3503
    • Platika, D.1    Boulos, M.H.2    Baizer, L.3    Fishman, M.C.4
  • 59
    • 0037799198 scopus 로고    scopus 로고
    • A modular PIP2 binding site as a determinant of capsaicin receptor sensitivity
    • Prescott E. D. Julius D. (2003) A modular PIP2 binding site as a determinant of capsaicin receptor sensitivity. Science 300, 1284 1288.
    • (2003) Science , vol.300 , pp. 1284-1288
    • Prescott, E.D.1    Julius, D.2
  • 60
    • 0038689057 scopus 로고    scopus 로고
    • Filopodial calcium transients regulate growth cone motility and guidance through local activation of calpain
    • Robles E., Huttenlocher A. Gomez T. M. (2003) Filopodial calcium transients regulate growth cone motility and guidance through local activation of calpain. Neuron 38, 597 609.
    • (2003) Neuron , vol.38 , pp. 597-609
    • Robles, E.1    Huttenlocher, A.2    Gomez, T.M.3
  • 62
    • 0344442832 scopus 로고    scopus 로고
    • Mobility and cycling of synaptic protein-containing vesicles in axonal growth cone filopodia
    • Sabo S. L. McAllister A. K. (2003) Mobility and cycling of synaptic protein-containing vesicles in axonal growth cone filopodia. Nat. Neurosci. 6, 1264 1269.
    • (2003) Nat. Neurosci. , vol.6 , pp. 1264-1269
    • Sabo, S.L.1    McAllister, A.K.2
  • 63
    • 0242693917 scopus 로고    scopus 로고
    • Spike formation by fibroblasts adhering to fibrillar collagen I gel
    • Sato K., Hattori S., Irie S. Kawashima S. (2003) Spike formation by fibroblasts adhering to fibrillar collagen I gel. Cell Struct. Funct. 28, 229 241.
    • (2003) Cell Struct. Funct. , vol.28 , pp. 229-241
    • Sato, K.1    Hattori, S.2    Irie, S.3    Kawashima, S.4
  • 65
    • 0034723256 scopus 로고    scopus 로고
    • Molecular cloning of an N- terminal splice variant of the capsaicin receptor. Loss of N-terminal domain suggests functional divergence among capsaicin receptor subtypes
    • Schumacher M. A., Moff I., Sudanagunta S. P. Levine J. D. (2000) Molecular cloning of an N- terminal splice variant of the capsaicin receptor. Loss of N-terminal domain suggests functional divergence among capsaicin receptor subtypes. J. Biol. Chem. 275, 2756 2762.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2756-2762
    • Schumacher, M.A.1    Moff, I.2    Sudanagunta, S.P.3    Levine, J.D.4
  • 66
    • 29444456617 scopus 로고    scopus 로고
    • An N-terminal variant of Trpv1 channel is required for osmosensory transduction
    • Sharif Naeini R., Witty M. F., Seguela P. Bourque C. W. (2006) An N-terminal variant of Trpv1 channel is required for osmosensory transduction. Nat. Neurosci. 9, 93 98.
    • (2006) Nat. Neurosci. , vol.9 , pp. 93-98
    • Sharif Naeini, R.1    Witty, M.F.2    Seguela, P.3    Bourque, C.W.4
  • 67
    • 0036719449 scopus 로고    scopus 로고
    • Breaking the neuronal sphere: Regulation of the actin cytoskeleton in neuritogenesis
    • da Silva J. S. Dotti C. G. (2002) Breaking the neuronal sphere: regulation of the actin cytoskeleton in neuritogenesis. Nat. Rev. Neurosci. 3, 694 704.
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 694-704
    • Da Silva, J.S.1    Dotti, C.G.2
  • 68
    • 0017902937 scopus 로고
    • Direct visualization of the 10-nm (100-A)-filament network in whole and enucleated cultured cells
    • Small J. V. Celis J. E. (1978) Direct visualization of the 10-nm (100-A)-filament network in whole and enucleated cultured cells. J. Cell Sci. 31, 393 409.
    • (1978) J. Cell Sci. , vol.31 , pp. 393-409
    • Small, J.V.1    Celis, J.E.2
  • 69
    • 24644441368 scopus 로고    scopus 로고
    • The comings and goings of actin: Coupling protrusion and retraction in cell motility
    • Small J. V. Resch G. P. (2005) The comings and goings of actin: coupling protrusion and retraction in cell motility. Curr. Opin. Cell Biol. 17, 517 523.
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 517-523
    • Small, J.V.1    Resch, G.P.2
  • 71
    • 0035097592 scopus 로고    scopus 로고
    • The cell biology of neuronal navigation
    • Song H. Poo M. (2001) The cell biology of neuronal navigation. Nat. Cell Biol. 3, E81 E88.
    • (2001) Nat. Cell Biol. , vol.3
    • Song, H.1    Poo, M.2
  • 72
    • 25844435342 scopus 로고    scopus 로고
    • Myosin-X: A molecular motor at the cell's fingertips
    • Sousa A. D. Cheney R. E. (2005) Myosin-X: a molecular motor at the cell's fingertips. Trends Cell Biol. 15, 533 539.
    • (2005) Trends Cell Biol. , vol.15 , pp. 533-539
    • Sousa, A.D.1    Cheney, R.E.2
  • 73
    • 31644448163 scopus 로고    scopus 로고
    • Myo10 in brain: Developmental regulation, identification of a headless isoform and dynamics in neurons
    • Sousa A. D., Berg J. S., Robertson B. W., Meeker R. B. Cheney R. E. (2006) Myo10 in brain: developmental regulation, identification of a headless isoform and dynamics in neurons. J. Cell Sci. 119, 184 194.
    • (2006) J. Cell Sci. , vol.119 , pp. 184-194
    • Sousa, A.D.1    Berg, J.S.2    Robertson, B.W.3    Meeker, R.B.4    Cheney, R.E.5
  • 74
    • 0035167052 scopus 로고    scopus 로고
    • Filopodial initiation and a novel filament- organizing center, the focal ring
    • Steketee M., Balazovich K. Tosney K. W. (2001) Filopodial initiation and a novel filament- organizing center, the focal ring. Mol. Biol. Cell 12, 2378 2395.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2378-2395
    • Steketee, M.1    Balazovich, K.2    Tosney, K.W.3
  • 76
    • 33644796336 scopus 로고    scopus 로고
    • Regulation of TRPV1 by a novel renally expressed rat TRPV1 splice variant
    • Tian W., Fu Y., Wang D. H. Cohen D. M. (2006) Regulation of TRPV1 by a novel renally expressed rat TRPV1 splice variant. Am. J. Physiol. Renal Physiol. 290, F117 F126.
    • (2006) Am. J. Physiol. Renal Physiol. , vol.290
    • Tian, W.1    Fu, Y.2    Wang, D.H.3    Cohen, D.M.4
  • 79
    • 4444258203 scopus 로고    scopus 로고
    • An alternative splicing product of the murine trpv1 gene dominant negatively modulates the activity of TRPV1 channels
    • Wang C., Hu H. Z., Colton C. K., Wood J. D. Zhu M. X. (2004a) An alternative splicing product of the murine trpv1 gene dominant negatively modulates the activity of TRPV1 channels. J. Biol. Chem. 279, 37423 37430.
    • (2004) J. Biol. Chem. , vol.279 , pp. 37423-37430
    • Wang, C.1    Hu, H.Z.2    Colton, C.K.3    Wood, J.D.4    Zhu, M.X.5
  • 81
    • 4644326930 scopus 로고    scopus 로고
    • A microtubule-binding myosin required for nuclear anchoring and spindle assembly
    • Weber K. L., Sokac A. M., Berg J. S., Cheney R. E. Bement W. M. (2004) A microtubule-binding myosin required for nuclear anchoring and spindle assembly. Nature 431, 325 329.
    • (2004) Nature , vol.431 , pp. 325-329
    • Weber, K.L.1    Sokac, A.M.2    Berg, J.S.3    Cheney, R.E.4    Bement, W.M.5
  • 82
    • 0023406178 scopus 로고
    • Turnover of the carboxy-terminal tyrosine of alpha- tubulin and means of reaching elevated levels of detyrosination in living cells
    • Wehland J. Weber K. (1987) Turnover of the carboxy-terminal tyrosine of alpha- tubulin and means of reaching elevated levels of detyrosination in living cells. J. Cell Sci. 88, 185 203.
    • (1987) J. Cell Sci. , vol.88 , pp. 185-203
    • Wehland, J.1    Weber, K.2
  • 83
    • 0345169048 scopus 로고    scopus 로고
    • Post-translational modifications regulate microtubule function
    • Westermann S. Weber K. (2003) Post-translational modifications regulate microtubule function. Nat Rev Mol Cell Biol. 4, 938 947.
    • (2003) Nat Rev Mol Cell Biol. , vol.4 , pp. 938-947
    • Westermann, S.1    Weber, K.2
  • 85
    • 0029065159 scopus 로고
    • Dendritic spines as basic functional units of neuronal integration
    • Yuste R. Denk W. (1995) Dendritic spines as basic functional units of neuronal integration. Nature. 375, 682 684.
    • (1995) Nature. , vol.375 , pp. 682-684
    • Yuste, R.1    Denk, W.2
  • 86
    • 29244484493 scopus 로고    scopus 로고
    • NGF rapidly increases membrane expression of TRPV1 heat-gated ion channels
    • Zhang X., Huang J. McNaughton P. A. (2005) NGF rapidly increases membrane expression of TRPV1 heat-gated ion channels. EMBO J. 24, 4211 4223.
    • (2005) EMBO J. , vol.24 , pp. 4211-4223
    • Zhang, X.1    Huang, J.2    McNaughton, P.A.3
  • 87
    • 0030200393 scopus 로고    scopus 로고
    • Evidence for a role of dendritic filopodia in synaptogenesis and spine formation
    • Ziv N. E. Smith S. J. (1996) Evidence for a role of dendritic filopodia in synaptogenesis and spine formation. Neuron 17, 91 102.
    • (1996) Neuron , vol.17 , pp. 91-102
    • Ziv, N.E.1    Smith, S.J.2


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