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Volumn 141, Issue 2, 2005, Pages 151-155

The high and middle molecular weight neurofilament subunits regulate the association of neurofilaments with kinesin: Inhibition by phosphorylation of the high molecular weight subunit

Author keywords

Axonal transport; Cytoskeleton; Kinesin; Motor protein; Neurofilament; Phosphorylation

Indexed keywords

KINESIN; MOLECULAR MOTOR; NEUROFILAMENT PROTEIN; PROTEIN SUBUNIT;

EID: 27744476574     PISSN: 0169328X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbrainres.2005.08.009     Document Type: Article
Times cited : (50)

References (39)
  • 2
    • 0033780584 scopus 로고    scopus 로고
    • Neurofilaments run sprints not marathons
    • S.T. Brady Neurofilaments run sprints not marathons Nat. Cell Biol. 2 2000 E43 E45
    • (2000) Nat. Cell Biol. , vol.2
    • Brady, S.T.1
  • 3
    • 0029004898 scopus 로고
    • Defective axonal transport in a transgenic mouse model of amyotrophic lateral sclerosis
    • J.-F. Collard, F. Cote, and J.-P. Julien Defective axonal transport in a transgenic mouse model of amyotrophic lateral sclerosis Nature 375 1995 61 64
    • (1995) Nature , vol.375 , pp. 61-64
    • Collard, J.-F.1    Cote, F.2    Julien, J.-P.3
  • 4
    • 0026580004 scopus 로고
    • Local modulation of neurofilament phosphorylation, axonal caliber, and slow axonal transport by myelinating Schwann cells
    • S.M. deWaegh, V.M.-Y. Lee, and S.T. Brady Local modulation of neurofilament phosphorylation, axonal caliber, and slow axonal transport by myelinating Schwann cells Cell 68 1992 451 463
    • (1992) Cell , vol.68 , pp. 451-463
    • Dewaegh, S.M.1    Lee, V.M.-Y.2    Brady, S.T.3
  • 5
    • 0032482231 scopus 로고    scopus 로고
    • Absence of the mid-sized neurofilament subunit decreases axonal calibers, levels of light neurofilament (NF-L), and neurofilament content
    • G.A. Elder, V.L. FriedrichJr, P. Bosco, C. Kang, A. Gourov, P.H. Tu, V.M. Lee, and R.A. Lazzarinin Absence of the mid-sized neurofilament subunit decreases axonal calibers, levels of light neurofilament (NF-L), and neurofilament content J. Cell Biol. 141 1998 727 739
    • (1998) J. Cell Biol. , vol.141 , pp. 727-739
    • Elder, G.A.1    Friedrichjr, V.L.2    Bosco, P.3    Kang, C.4    Gourov, A.5    Tu, P.H.6    Lee, V.M.7    Lazzarinin, R.A.8
  • 6
    • 0028316048 scopus 로고
    • Phosphorylation of neurofilament H subunit as related to arrangement of neurofilaments
    • T. Gotow, and J. Tanaka Phosphorylation of neurofilament H subunit as related to arrangement of neurofilaments J. Neurosci. Res. 37 6 1994 (Apr. 15) 691 713
    • (1994) J. Neurosci. Res. , vol.37 , Issue.6 , pp. 691-713
    • Gotow, T.1    Tanaka, J.2
  • 7
    • 0022353699 scopus 로고
    • Slowing of neurofilament transport and the radial growth of developing nerve fibers
    • P.N. Hoffman, J.W. Griffin, B.G. Gold, and D.L. Price Slowing of neurofilament transport and the radial growth of developing nerve fibers J. Neurosci. 5 1985 2920 2929
    • (1985) J. Neurosci. , vol.5 , pp. 2920-2929
    • Hoffman, P.N.1    Griffin, J.W.2    Gold, B.G.3    Price, D.L.4
  • 8
    • 0032817551 scopus 로고    scopus 로고
    • Disruption of type IV intermediate filament network in mice lacking the neurofilament medium and heavy subunits
    • H. Jacomy, Q. Zhu, S. Couillard-Despres, J.M. Beaulieu, and J.P. Julien Disruption of type IV intermediate filament network in mice lacking the neurofilament medium and heavy subunits J. Neurochem. 73 1999 972 984
    • (1999) J. Neurochem. , vol.73 , pp. 972-984
    • Jacomy, H.1    Zhu, Q.2    Couillard-Despres, S.3    Beaulieu, J.M.4    Julien, J.P.5
  • 9
    • 19544366223 scopus 로고    scopus 로고
    • Neurofilament subunits undergo more rapid translocation within retinas than in optic axons
    • C. Jung, and T.B. Shea Neurofilament subunits undergo more rapid translocation within retinas than in optic axons Mol. Brain Res. 122 2004 188 192
    • (2004) Mol. Brain Res. , vol.122 , pp. 188-192
    • Jung, C.1    Shea, T.B.2
  • 10
    • 0033977488 scopus 로고    scopus 로고
    • C-terminal phosphorylation of the high molecular weight neurofilament subunit correlates with decreased neurofilament axonal transport velocity
    • C. Jung, J.T. Yabe, and T.B. Shea C-terminal phosphorylation of the high molecular weight neurofilament subunit correlates with decreased neurofilament axonal transport velocity Brain Res. 856 2000 12 19
    • (2000) Brain Res. , vol.856 , pp. 12-19
    • Jung, C.1    Yabe, J.T.2    Shea, T.B.3
  • 11
    • 0033810408 scopus 로고    scopus 로고
    • Hypophosphorylated neurofilament subunits undergo axonal transport faster than extensively phosphorylated subunits
    • C. Jung, J.T. Yabe, S. Lee, and T.B. Shea Hypophosphorylated neurofilament subunits undergo axonal transport faster than extensively phosphorylated subunits Cell Motil. Cytoskel. 47 2000 120 129
    • (2000) Cell Motil. Cytoskel. , vol.47 , pp. 120-129
    • Jung, C.1    Yabe, J.T.2    Lee, S.3    Shea, T.B.4
  • 12
    • 0022996137 scopus 로고
    • Phosphorylation of neurofilament proteins during their axonal transport
    • Y. Komiya, T. Tashiro, and M. Kuokawa Phosphorylation of neurofilament proteins during their axonal transport Biomed. Res. 7 1986 345 348
    • (1986) Biomed. Res. , vol.7 , pp. 345-348
    • Komiya, Y.1    Tashiro, T.2    Kuokawa, M.3
  • 13
    • 0026535236 scopus 로고
    • Slow axonal transport mechanisms move neurofilaments relentlessly in mouse optic axons
    • R.J. Lasek, P. Paggi, and M.J. Katz Slow axonal transport mechanisms move neurofilaments relentlessly in mouse optic axons J. Cell Biol. 117 1992 607 616
    • (1992) J. Cell Biol. , vol.117 , pp. 607-616
    • Lasek, R.J.1    Paggi, P.2    Katz, M.J.3
  • 14
    • 0027212960 scopus 로고
    • The maximum rate of neurofilament transport in axons: A view of molecular transport mechanisms continuously engaged
    • R.J. Lasek, P. Paggi, and M.J. Katz The maximum rate of neurofilament transport in axons: a view of molecular transport mechanisms continuously engaged Brain Res. 616 1993 58 64
    • (1993) Brain Res. , vol.616 , pp. 58-64
    • Lasek, R.J.1    Paggi, P.2    Katz, M.J.3
  • 16
    • 0024242689 scopus 로고
    • Multiple phosphorylated variants of the high molecular mass subunit of neurofilaments in axons of retinal cell neurons: Characterization and evidence for their differential association with stationary and moving neurofilaments
    • S.E. Lewis, and R.A. Nixon Multiple phosphorylated variants of the high molecular mass subunit of neurofilaments in axons of retinal cell neurons: characterization and evidence for their differential association with stationary and moving neurofilaments J. Cell Biol. 107 1988 2689 2701
    • (1988) J. Cell Biol. , vol.107 , pp. 2689-2701
    • Lewis, S.E.1    Nixon, R.A.2
  • 18
    • 0028900588 scopus 로고
    • Two distinct functions of the carboxyl-terminal tail domain of NF-M upon neurofilament assembly: Cross-bridge formation and longitudinal elongation of filaments
    • T. Nakagawa, J. Chen, Z. Zhang, Y. Kanai, and N. Hirokawa Two distinct functions of the carboxyl-terminal tail domain of NF-M upon neurofilament assembly: cross-bridge formation and longitudinal elongation of filaments J. Cell Biol. 129 1995 411 429
    • (1995) J. Cell Biol. , vol.129 , pp. 411-429
    • Nakagawa, T.1    Chen, J.2    Zhang, Z.3    Kanai, Y.4    Hirokawa, N.5
  • 19
    • 0032192425 scopus 로고    scopus 로고
    • Dynamic behavior and organization of cytoskeletal proteins in neurons: Reconciling old and new findings
    • R.A. Nixon Dynamic behavior and organization of cytoskeletal proteins in neurons: reconciling old and new findings BioEssays 20 1998 798 807
    • (1998) BioEssays , vol.20 , pp. 798-807
    • Nixon, R.A.1
  • 20
    • 0022617701 scopus 로고
    • Multiple fates of newly synthesized neurofilament proteins: Evidence for a stationary neurofilament network distributed non-uniformly along axons of retinal ganglion cell neurons
    • R.A. Nixon, and K.B. Logvinenko Multiple fates of newly synthesized neurofilament proteins: evidence for a stationary neurofilament network distributed non-uniformly along axons of retinal ganglion cell neurons J. Cell Biol. 102 1986 647 659
    • (1986) J. Cell Biol. , vol.102 , pp. 647-659
    • Nixon, R.A.1    Logvinenko, K.B.2
  • 21
    • 0027931132 scopus 로고
    • Phosphorylation on carboxyl terminus domains of neurofilament proteins in retinal ganglion cell neurons in vivo: Influences on regional neurofilament accumulation, interneurofilament spacing, and axon caliber
    • R.A. Nixon, P.A. Paskevitc, R.K. Sihag, and C.Y. Thayer Phosphorylation on carboxyl terminus domains of neurofilament proteins in retinal ganglion cell neurons in vivo: influences on regional neurofilament accumulation, interneurofilament spacing, and axon caliber J. Cell Biol. 126 1994 1031 1146
    • (1994) J. Cell Biol. , vol.126 , pp. 1031-1146
    • Nixon, R.A.1    Paskevitc, P.A.2    Sihag, R.K.3    Thayer, C.Y.4
  • 22
    • 0029367097 scopus 로고
    • Neurofilament phosphorylation
    • H.C. Pant, and Veeranna Neurofilament phosphorylation Biochem. Cell. Biol. 73 1995 575 592
    • (1995) Biochem. Cell. Biol. , vol.73 , pp. 575-592
    • Pant, H.C.1    Veeranna2
  • 24
    • 0038632271 scopus 로고    scopus 로고
    • Defective axonal transport in mouse models of amyotrophic lateral sclerosis: A review
    • M.V. Rao, and R.A. Nixon Defective axonal transport in mouse models of amyotrophic lateral sclerosis: a review Neurochem. Res. 28 2003 1041 1047
    • (2003) Neurochem. Res. , vol.28 , pp. 1041-1047
    • Rao, M.V.1    Nixon, R.A.2
  • 25
    • 0034666282 scopus 로고    scopus 로고
    • Neurofilaments are transported rapidly but intermittently in axons: Implications for slow axonal transport
    • S. Roy, P. Coffee, G. Smith, R.K. Liem, S.T. Brady, and M.M. Black Neurofilaments are transported rapidly but intermittently in axons: implications for slow axonal transport J. Neurosci. 20 2000 6849 6861
    • (2000) J. Neurosci. , vol.20 , pp. 6849-6861
    • Roy, S.1    Coffee, P.2    Smith, G.3    Liem, R.K.4    Brady, S.T.5    Black, M.M.6
  • 26
    • 0034722377 scopus 로고    scopus 로고
    • Local control of neurofilament accumulation during radial growth of myelinating axons in vivo: Selective role of site-specific phosphorylation
    • I. Sanchez, L. Hassinger, R.K. Sihag, D.W. Cleveland, P. Mohan, and R.A. Nixon Local control of neurofilament accumulation during radial growth of myelinating axons in vivo: selective role of site-specific phosphorylation J. Cell Biol. 151 2000 1013 1024
    • (2000) J. Cell Biol. , vol.151 , pp. 1013-1024
    • Sanchez, I.1    Hassinger, L.2    Sihag, R.K.3    Cleveland, D.W.4    Mohan, P.5    Nixon, R.A.6
  • 27
    • 0025371617 scopus 로고
    • Bundling and cross-linking of intermediate filaments of the nervous system
    • G. Shaw, and Z.C. Hou Bundling and cross-linking of intermediate filaments of the nervous system J. Neurosci. Res. 25 1990 561 568
    • (1990) J. Neurosci. Res. , vol.25 , pp. 561-568
    • Shaw, G.1    Hou, Z.C.2
  • 28
    • 0035510709 scopus 로고    scopus 로고
    • Kinesin, dynein and neurofilament transport
    • T.B. Shea, and L. Flanagan Kinesin, dynein and neurofilament transport Trends Neurosci. 24 2001 644 648
    • (2001) Trends Neurosci. , vol.24 , pp. 644-648
    • Shea, T.B.1    Flanagan, L.2
  • 29
    • 0034209092 scopus 로고    scopus 로고
    • Occam's razor slices through the mysteries of neurofilament axonal transport: Can it really be so simple?
    • T.B. Shea, and J.T. Yabe Occam's razor slices through the mysteries of neurofilament axonal transport: can it really be so simple? Traffic 1 2000 522 523
    • (2000) Traffic , vol.1 , pp. 522-523
    • Shea, T.B.1    Yabe, J.T.2
  • 30
    • 0142026833 scopus 로고    scopus 로고
    • Does C-terminal phosphorylation regulate neurofilament transport? Recent evidence suggests that it does
    • T.B. Shea, C. Jung, and H.C. Pant Does C-terminal phosphorylation regulate neurofilament transport? Recent evidence suggests that it does Trends Neurosci. 26 2003 397 400
    • (2003) Trends Neurosci. , vol.26 , pp. 397-400
    • Shea, T.B.1    Jung, C.2    Pant, H.C.3
  • 31
    • 0029778167 scopus 로고    scopus 로고
    • Visualization of slow axonal transport in vivo
    • S. Terada, T. Nakata, A.C. Peterson, and N. Hirokawa Visualization of slow axonal transport in vivo Science 273 1996 784 788
    • (1996) Science , vol.273 , pp. 784-788
    • Terada, S.1    Nakata, T.2    Peterson, A.C.3    Hirokawa, N.4
  • 32
    • 12544252706 scopus 로고    scopus 로고
    • Impairment of anterograde and retrograde neuro-lament transport after anti-kinesin and anti-dynein antibody microinjection in chicken dorsal root ganglia
    • C. Theiss, M. Napirei, K. Karl Meller. Impairment of anterograde and retrograde neuro-lament transport after anti-kinesin and anti-dynein antibody microinjection in chicken dorsal root ganglia. EurJ. Cell. Biol. 84 (2005) 29-4313,14
    • (2005) Eur. J. Cell. Biol. , vol.84 , pp. 29-4313
    • Theiss, C.1    Napirei, M.2    Karl Meller, K.3
  • 33
    • 0033776708 scopus 로고    scopus 로고
    • Rapid movement of axonal neurofilaments interrupted by prolonged pauses
    • L. Wang, C.L. Ho, D. Sun, R.K. Liem, and A. Brown Rapid movement of axonal neurofilaments interrupted by prolonged pauses Nat. Cell Biol. 2 2000 137 141
    • (2000) Nat. Cell Biol. , vol.2 , pp. 137-141
    • Wang, L.1    Ho, C.L.2    Sun, D.3    Liem, R.K.4    Brown, A.5
  • 35
    • 0032694199 scopus 로고    scopus 로고
    • Kinesin-mediated transport of neurofilament protein oligomers in growing axons
    • J.T. Yabe, A. Pimenta, and T.B. Shea Kinesin-mediated transport of neurofilament protein oligomers in growing axons J. Cell. Sci. 112 1999 3799 3814
    • (1999) J. Cell. Sci. , vol.112 , pp. 3799-3814
    • Yabe, J.T.1    Pimenta, A.2    Shea, T.B.3
  • 36
    • 0242305485 scopus 로고    scopus 로고
    • Phospho-dependent association of neurofilament proteins with kinesin in situ
    • J.T. Yabe, C. Jung, W.K.-H. Chan, and T.B. Shea Phospho-dependent association of neurofilament proteins with kinesin in situ Cell Motil. Cytoskel. 42 2000 230 240
    • (2000) Cell Motil. Cytoskel. , vol.42 , pp. 230-240
    • Yabe, J.T.1    Jung, C.2    Chan, W.K.-H.3    Shea, T.B.4
  • 37
    • 0035313106 scopus 로고    scopus 로고
    • Neurofilaments consist of distinct populations that can be distinguished by C-terminal phosphorylation, bundling and axonal transport rate in growing axonal neurites
    • J.T. Yabe, T. Chylinski, F.-S. Wang, A. Pimenta, S.D. Kattar, M.-D. Linsley, W.K.-H. Chan, and T.B. Shea Neurofilaments consist of distinct populations that can be distinguished by C-terminal phosphorylation, bundling and axonal transport rate in growing axonal neurites J. Neurosci. 21 2001 2195 2205
    • (2001) J. Neurosci. , vol.21 , pp. 2195-2205
    • Yabe, J.T.1    Chylinski, T.2    Wang, F.-S.3    Pimenta, A.4    Kattar, S.D.5    Linsley, M.-D.6    Chan, W.K.-H.7    Shea, T.B.8
  • 38
    • 0142250822 scopus 로고    scopus 로고
    • Neurofilament transport in vivo minimally requires hetero-oligomer formation
    • A. Yuan, M.V. Rao, A. Kumar, J.-P. Julien, and R.A. Nixon Neurofilament transport in vivo minimally requires hetero-oligomer formation J. Neurosci. 23 2003 9452 9458
    • (2003) J. Neurosci. , vol.23 , pp. 9452-9458
    • Yuan, A.1    Rao, M.V.2    Kumar, A.3    Julien, J.-P.4    Nixon, R.A.5
  • 39
    • 0032487532 scopus 로고    scopus 로고
    • Disruption of the NF-H gene increases axonal microtubule content and velocity of neurofilament transport: Relief of axonopathy resulting from the toxin β,β′-iminodiproprionitrile
    • Q. Zhu, M. Lindenbaum, F. Levavasseur, H. Jacomy, and J.-P. Julien Disruption of the NF-H gene increases axonal microtubule content and velocity of neurofilament transport: relief of axonopathy resulting from the toxin β,β′-iminodiproprionitrile J. Cell Biol. 143 1998 183 193
    • (1998) J. Cell Biol. , vol.143 , pp. 183-193
    • Zhu, Q.1    Lindenbaum, M.2    Levavasseur, F.3    Jacomy, H.4    Julien, J.-P.5


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