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Volumn 384, Issue 1, 2009, Pages 37-42

Microtubule-independent regulation of neurofilament interactions in vitro by neurofilament-bound ATPase activities

Author keywords

ATPases; Interactions; Neurofilaments; Regulation

Indexed keywords

ADENOSINE TRIPHOSPHATASE;

EID: 65549084201     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.04.045     Document Type: Article
Times cited : (3)

References (30)
  • 2
    • 33846423163 scopus 로고    scopus 로고
    • Neurofilaments switch between distinct mobile and stationary states during their transport along axons
    • Trivedi N., Jung P., and Brown A. Neurofilaments switch between distinct mobile and stationary states during their transport along axons. J. Neurosci. 27 (2007) 507-516
    • (2007) J. Neurosci. , vol.27 , pp. 507-516
    • Trivedi, N.1    Jung, P.2    Brown, A.3
  • 3
    • 33646257802 scopus 로고    scopus 로고
    • Dynein mediates retrograde neurofilament transport within axons and anterograde delivery of NFs from perikarya into axons: regulation by multiple phosphorylation events
    • Motil J., Chan W.K., Dubey M., Chaudhury P., Pimenta A., Chylinski T.M., Ortiz D.T., and Shea T.B. Dynein mediates retrograde neurofilament transport within axons and anterograde delivery of NFs from perikarya into axons: regulation by multiple phosphorylation events. Cell Motil. Cytoskeleton 63 (2006) 266-286
    • (2006) Cell Motil. Cytoskeleton , vol.63 , pp. 266-286
    • Motil, J.1    Chan, W.K.2    Dubey, M.3    Chaudhury, P.4    Pimenta, A.5    Chylinski, T.M.6    Ortiz, D.T.7    Shea, T.B.8
  • 4
    • 12544252706 scopus 로고    scopus 로고
    • Impairment of anterograde and retrograde neurofilament transport after anti-kinesin and anti-dynein antibody microinjection in chicken dorsal root ganglia
    • Theiss C., Napirei M., and Meller K. Impairment of anterograde and retrograde neurofilament transport after anti-kinesin and anti-dynein antibody microinjection in chicken dorsal root ganglia. Eur. J. Cell Biol. 84 (2005) 29-43
    • (2005) Eur. J. Cell Biol. , vol.84 , pp. 29-43
    • Theiss, C.1    Napirei, M.2    Meller, K.3
  • 5
    • 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
    • Yabe J.T., Chylinski T., Wang F.S., Pimenta A., Kattar S.D., Linsley M.D., Chan W.K., and Shea T.B. 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.7    Shea, T.B.8
  • 6
    • 34249714850 scopus 로고    scopus 로고
    • Role of phosphorylation on the structural dynamics and function of types III and IV intermediate filaments
    • (Review)
    • Sihag R.K., Inagaki M., Yamaguchi T., Shea T.B., and Pant H.C. Role of phosphorylation on the structural dynamics and function of types III and IV intermediate filaments. Exp. Cell Res. 313 (2007) 2098-2109 (Review)
    • (2007) Exp. Cell Res. , vol.313 , pp. 2098-2109
    • Sihag, R.K.1    Inagaki, M.2    Yamaguchi, T.3    Shea, T.B.4    Pant, H.C.5
  • 7
    • 42049107093 scopus 로고    scopus 로고
    • Regulation of neurofilament dynamics by phosphorylation
    • (Review)
    • Shea T.B., and Chan W.K.-H. Regulation of neurofilament dynamics by phosphorylation. Eur. J. Neurosci. 17 (2008) 1893-1901 (Review)
    • (2008) Eur. J. Neurosci. , vol.17 , pp. 1893-1901
    • Shea, T.B.1    Chan, W.K.-H.2
  • 8
    • 0023374805 scopus 로고
    • Properties of highly viscous gels formed by neurofilaments in vitro. A possible consequence of a specific inter-filament cross-bridging
    • Leterrier J.F., and Eyer J. Properties of highly viscous gels formed by neurofilaments in vitro. A possible consequence of a specific inter-filament cross-bridging. Biochem. J. 245 (1987) 93-101
    • (1987) Biochem. J. , vol.245 , pp. 93-101
    • Leterrier, J.F.1    Eyer, J.2
  • 9
    • 0023875031 scopus 로고
    • Influence of the phosphorylation state of neurofilament proteins on the interactions between purified filaments in vitro
    • Eyer J., and Leterrier J.F. Influence of the phosphorylation state of neurofilament proteins on the interactions between purified filaments in vitro. Biochem. J. 252 (1988) 655-660
    • (1988) Biochem. J. , vol.252 , pp. 655-660
    • Eyer, J.1    Leterrier, J.F.2
  • 10
    • 0024321887 scopus 로고
    • Effect of a single dose of beta,beta′-iminodipropionitrile in vivo on the properties of neurofilaments in vitro: comparison with the effect of iminodipropionitrile added directly to neurofilaments in vitro
    • Eyer J., Mclean W.G., and Leterrier J.F. Effect of a single dose of beta,beta′-iminodipropionitrile in vivo on the properties of neurofilaments in vitro: comparison with the effect of iminodipropionitrile added directly to neurofilaments in vitro. J. Neurochem. 52 (1989) 1759-1765
    • (1989) J. Neurochem. , vol.52 , pp. 1759-1765
    • Eyer, J.1    Mclean, W.G.2    Leterrier, J.F.3
  • 11
    • 0028859412 scopus 로고
    • Progressive hyperphosphorylation of neurofilament heavy subunits with aging: possible involvement in the mechanism of neurofilament accumulation
    • Gou J.P., Eyer J., and Leterrier J.F. Progressive hyperphosphorylation of neurofilament heavy subunits with aging: possible involvement in the mechanism of neurofilament accumulation. Biochem. Biophys. Res. Commun. 215 (1995) 368-376
    • (1995) Biochem. Biophys. Res. Commun. , vol.215 , pp. 368-376
    • Gou, J.P.1    Eyer, J.2    Leterrier, J.F.3
  • 12
    • 0030009043 scopus 로고    scopus 로고
    • Mechanical effects of neurofilament cross-bridges. Modulation by phosphorylation, lipids, and interactions with F-actin
    • Leterrier J.F., Käs J., Hartwig J., Vegners R., and Janmey P.A. Mechanical effects of neurofilament cross-bridges. Modulation by phosphorylation, lipids, and interactions with F-actin. J. Biol. Chem. 271 (1996) 15687-15694
    • (1996) J. Biol. Chem. , vol.271 , pp. 15687-15694
    • Leterrier, J.F.1    Käs, J.2    Hartwig, J.3    Vegners, R.4    Janmey, P.A.5
  • 13
    • 0032078841 scopus 로고    scopus 로고
    • Regulation of neurofilament interactions in vitro by natural and synthetic polypeptides sharing Lys-Ser-Pro sequences with the heavy neurofilament subunit NF-H: neurofilament crossbridging by antiparallel sidearm overlapping
    • Gou J.P., Gotow T., Janmey P.A., and Leterrier J.F. Regulation of neurofilament interactions in vitro by natural and synthetic polypeptides sharing Lys-Ser-Pro sequences with the heavy neurofilament subunit NF-H: neurofilament crossbridging by antiparallel sidearm overlapping. Med. Biol. Eng. Comput. 36 (1998) 371-387
    • (1998) Med. Biol. Eng. Comput. , vol.36 , pp. 371-387
    • Gou, J.P.1    Gotow, T.2    Janmey, P.A.3    Leterrier, J.F.4
  • 14
    • 0033783031 scopus 로고    scopus 로고
    • Bidirectional translocation of neurofilaments along microtubules mediated in part by dynein/dynactin
    • Shah J.V., Flanagan L.A., Janmey P.A., and Leterrier J.F. Bidirectional translocation of neurofilaments along microtubules mediated in part by dynein/dynactin. Mol. Biol. Cell 11 (2000) 3495-3508
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3495-3508
    • Shah, J.V.1    Flanagan, L.A.2    Janmey, P.A.3    Leterrier, J.F.4
  • 15
    • 0019135186 scopus 로고
    • Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-association
    • MacLean-Fletcher S., and Pollard T.D. Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-association. Biochem. Biophys. Res. Commun. 96 (1980) 18-27
    • (1980) Biochem. Biophys. Res. Commun. , vol.96 , pp. 18-27
    • MacLean-Fletcher, S.1    Pollard, T.D.2
  • 16
    • 0017903789 scopus 로고
    • Selective precipitation of 32Pi onto filter papers. Application to ATPase and cyclic AMP phosphodiesterase determination
    • Reimann E.M., and Umfleet R.A. Selective precipitation of 32Pi onto filter papers. Application to ATPase and cyclic AMP phosphodiesterase determination. Biochim. Biophys. Acta 523 (1978) 516-521
    • (1978) Biochim. Biophys. Acta , vol.523 , pp. 516-521
    • Reimann, E.M.1    Umfleet, R.A.2
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0019088395 scopus 로고
    • Study of the 10-nm-filament fraction isolated during the standard microtubule preparation
    • Delacourte A., Filliatreau G., Boutteau F., Biserte G., and Schrevel J. Study of the 10-nm-filament fraction isolated during the standard microtubule preparation. Biochem. J. 191 (1980) 543-546
    • (1980) Biochem. J. , vol.191 , pp. 543-546
    • Delacourte, A.1    Filliatreau, G.2    Boutteau, F.3    Biserte, G.4    Schrevel, J.5
  • 20
    • 0020702325 scopus 로고
    • Characteristics of the protein kinase activity associated with rat neurofilament preparations
    • Julien J.P., Smoluk G.D., and Mushynski W.E. Characteristics of the protein kinase activity associated with rat neurofilament preparations. Biochim. Biophys. Acta 755 (1983) 25-31
    • (1983) Biochim. Biophys. Acta , vol.755 , pp. 25-31
    • Julien, J.P.1    Smoluk, G.D.2    Mushynski, W.E.3
  • 21
    • 0020573836 scopus 로고
    • A rat brain protein kinase phosphorylating specifically neurofilaments
    • Toru-Delbauffe D., and Pierre M. A rat brain protein kinase phosphorylating specifically neurofilaments. FEBS Lett. 162 (1983) 230-234
    • (1983) FEBS Lett. , vol.162 , pp. 230-234
    • Toru-Delbauffe, D.1    Pierre, M.2
  • 22
    • 0023608935 scopus 로고
    • MAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties
    • Paschal B.M., Shpetner H.S., and Vallee R.B. MAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties. J. Cell Biol. 105 (1987) 1273-1282
    • (1987) J. Cell Biol. , vol.105 , pp. 1273-1282
    • Paschal, B.M.1    Shpetner, H.S.2    Vallee, R.B.3
  • 23
    • 0024078184 scopus 로고
    • Characterization of the microtubule-activated ATPase of brain cytoplasmic dynein (MAP 1C)
    • Shpetner H.S., Paschal B.M., and Vallee R.B. Characterization of the microtubule-activated ATPase of brain cytoplasmic dynein (MAP 1C). J. Cell Biol. 107 (1988) 1001-1009
    • (1988) J. Cell Biol. , vol.107 , pp. 1001-1009
    • Shpetner, H.S.1    Paschal, B.M.2    Vallee, R.B.3
  • 24
    • 0023644592 scopus 로고
    • Microtubule activation of kinesin ATPase activity
    • (Erratum in: Nature 326 (1987) 830)
    • Cohn S. Microtubule activation of kinesin ATPase activity. Nature 326 (1987) 16-17 (Erratum in: Nature 326 (1987) 830)
    • (1987) Nature , vol.326 , pp. 16-17
    • Cohn, S.1
  • 25
    • 0023657014 scopus 로고
    • GTP regeneration influences interactions of microtubules, neurofilaments, and microtubule-associated proteins in vitro
    • Flynn G., and Purich D.L. GTP regeneration influences interactions of microtubules, neurofilaments, and microtubule-associated proteins in vitro. J. Biol. Chem. 262 (1987) 15443-15447
    • (1987) J. Biol. Chem. , vol.262 , pp. 15443-15447
    • Flynn, G.1    Purich, D.L.2
  • 26
    • 0019812603 scopus 로고
    • Reorganization of axoplasmic organelles following beta,beta′-iminodipropionitrile administration
    • Papasozomenos S.C., Autilio-Gambetti L., and Gambetti P. Reorganization of axoplasmic organelles following beta,beta′-iminodipropionitrile administration. J. Cell Biol. 91 (1981) 866-871
    • (1981) J. Cell Biol. , vol.91 , pp. 866-871
    • Papasozomenos, S.C.1    Autilio-Gambetti, L.2    Gambetti, P.3
  • 27
    • 0021835558 scopus 로고
    • Cytoskeletal architecture and immunocytochemical localization of microtubule-associated proteins in regions of axons associated with rapid axonal transport: the beta,beta′-iminodipropionitrile-intoxicated axon as a model system
    • Hirokawa N., Bloom G.S., and Vallee R.B. Cytoskeletal architecture and immunocytochemical localization of microtubule-associated proteins in regions of axons associated with rapid axonal transport: the beta,beta′-iminodipropionitrile-intoxicated axon as a model system. J. Cell Biol. 101 (1985) 227-239
    • (1985) J. Cell Biol. , vol.101 , pp. 227-239
    • Hirokawa, N.1    Bloom, G.S.2    Vallee, R.B.3
  • 28
    • 39149108125 scopus 로고    scopus 로고
    • Intermediate filaments: versatile building blocks of cell structure
    • (Review)
    • Goldman R.D., Grin B., Mendez M.G., and Kuczmarski E.R. Intermediate filaments: versatile building blocks of cell structure. Curr. Opin. Cell Biol. 20 (2008) 28-34 (Review)
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 28-34
    • Goldman, R.D.1    Grin, B.2    Mendez, M.G.3    Kuczmarski, E.R.4
  • 29
    • 34249727384 scopus 로고    scopus 로고
    • The motility and dynamic properties of intermediate filaments and their constituent proteins
    • (Review)
    • Chou Y.H., Flitney F.W., Chang L., Mendez M., Grin B., and Goldman R.D. The motility and dynamic properties of intermediate filaments and their constituent proteins. Exp. Cell Res. 313 (2007) 2236-2243 (Review)
    • (2007) Exp. Cell Res. , vol.313 , pp. 2236-2243
    • Chou, Y.H.1    Flitney, F.W.2    Chang, L.3    Mendez, M.4    Grin, B.5    Goldman, R.D.6
  • 30
    • 65549105668 scopus 로고    scopus 로고
    • a mechanism for selective slowing of axonal transport of phosphorylated neurofilaments
    • Divalent cation-mediated interaction of phosphorylated neurofilaments competes with kinesin-dependent neurofilament-microtubule association:, submitted for publication
    • J. Kushkuley, W.K.-H. Chan, S. Lee, J. Eyer, J.F. Leterrier, T.B. Shea, Divalent cation-mediated interaction of phosphorylated neurofilaments competes with kinesin-dependent neurofilament-microtubule association: a mechanism for selective slowing of axonal transport of phosphorylated neurofilaments, submitted for publication.
    • Kushkuley, J.1    Chan, W.K.-H.2    Lee, S.3    Eyer, J.4    Leterrier, J.F.5    Shea, T.B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.