메뉴 건너뛰기




Volumn 10, Issue , 2009, Pages

The proline-rich domain of tau plays a role in interactions with actin

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; F ACTIN; G ACTIN; PROLINE; TAU PROTEIN;

EID: 71049158071     PISSN: None     EISSN: 14712121     Source Type: Journal    
DOI: 10.1186/1471-2121-10-81     Document Type: Article
Times cited : (95)

References (31)
  • 1
    • 0008538685 scopus 로고
    • A protein factor essential for microtubule assembly
    • 432646, 1057175, 10.1073/pnas.72.5.1858
    • Weingarten MD, Lockwood AH, Hwo SY, Kirschner MW. A protein factor essential for microtubule assembly. Proc Natl Acad Sci USA 1975, 72(5):1858-1862. 432646, 1057175, 10.1073/pnas.72.5.1858.
    • (1975) Proc Natl Acad Sci USA , vol.72 , Issue.5 , pp. 1858-1862
    • Weingarten, M.D.1    Lockwood, A.H.2    Hwo, S.Y.3    Kirschner, M.W.4
  • 2
    • 0027058857 scopus 로고
    • Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau
    • 275678, 1421571
    • Drechsel DN, Hyman AA, Cobb MH, Kirschner MW. Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau. Mol Biol Cell 1992, 3(10):1141-1154. 275678, 1421571.
    • (1992) Mol Biol Cell , vol.3 , Issue.10 , pp. 1141-1154
    • Drechsel, D.N.1    Hyman, A.A.2    Cobb, M.H.3    Kirschner, M.W.4
  • 3
    • 0000130253 scopus 로고    scopus 로고
    • The tau proteins in neuronal growth and development
    • Brandt R. The tau proteins in neuronal growth and development. Front Biosci 1996, 1:d118-130.
    • (1996) Front Biosci , vol.1
    • Brandt, R.1
  • 4
    • 0028785529 scopus 로고
    • Subpopulations of tau interact with microtubules and actin filaments in various cell types
    • 10.1002/cbf.290130404, 10232926
    • Henriquez JP, Cross D, Vial C, Maccioni RB. Subpopulations of tau interact with microtubules and actin filaments in various cell types. Cell Biochem Funct 1995, 13(4):239-250. 10.1002/cbf.290130404, 10232926.
    • (1995) Cell Biochem Funct , vol.13 , Issue.4 , pp. 239-250
    • Henriquez, J.P.1    Cross, D.2    Vial, C.3    Maccioni, R.B.4
  • 5
    • 0036219461 scopus 로고    scopus 로고
    • Tubulin, actin, and tau protein interactions and the study of their macromolecular assemblies
    • 10.1002/jcb.10133, 11948687
    • Farias GA, Munoz JP, Garrido J, Maccioni RB. Tubulin, actin, and tau protein interactions and the study of their macromolecular assemblies. J Cell Biochem 2002, 85(2):315-324. 10.1002/jcb.10133, 11948687.
    • (2002) J Cell Biochem , vol.85 , Issue.2 , pp. 315-324
    • Farias, G.A.1    Munoz, J.P.2    Garrido, J.3    Maccioni, R.B.4
  • 6
    • 0018934798 scopus 로고
    • Viscometric analysis of the gelation of Acanthamoeba extracts and purification of two gelation factors
    • 2110633, 6892818, 10.1083/jcb.85.2.414
    • MacLean-Fletcher SD, Pollard TD. Viscometric analysis of the gelation of Acanthamoeba extracts and purification of two gelation factors. J Cell Biol 1980, 85(2):414-428. 2110633, 6892818, 10.1083/jcb.85.2.414.
    • (1980) J Cell Biol , vol.85 , Issue.2 , pp. 414-428
    • MacLean-Fletcher, S.D.1    Pollard, T.D.2
  • 7
    • 0025335664 scopus 로고
    • The tubulin-binding sequence of brain microtubule-associated proteins, tau and MAP-2, is also involved in actin binding
    • 1131531, 2115775
    • Correas I, Padilla R, Avila J. The tubulin-binding sequence of brain microtubule-associated proteins, tau and MAP-2, is also involved in actin binding. Biochem J 1990, 269(1):61-64. 1131531, 2115775.
    • (1990) Biochem J , vol.269 , Issue.1 , pp. 61-64
    • Correas, I.1    Padilla, R.2    Avila, J.3
  • 8
    • 0027321473 scopus 로고
    • Microtubule-associated protein interactions with actin filaments: evidence for differential behavior of neuronal MAP-2 and tau in the presence of phosphatidyl-inositol
    • 10.1006/bbrc.1993.1107, 8439322
    • Yamauchi PS, Purich DL. Microtubule-associated protein interactions with actin filaments: evidence for differential behavior of neuronal MAP-2 and tau in the presence of phosphatidyl-inositol. Biochem Biophys Res Commun 1993, 190(3):710-715. 10.1006/bbrc.1993.1107, 8439322.
    • (1993) Biochem Biophys Res Commun , vol.190 , Issue.3 , pp. 710-715
    • Yamauchi, P.S.1    Purich, D.L.2
  • 9
    • 0027261518 scopus 로고
    • A tau fragment containing a repetitive sequence induces bundling of actin filaments
    • 10.1111/j.1471-4159.1993.tb03611.x, 8360695
    • Moraga DM, Nunez P, Garrido J, Maccioni RB. A tau fragment containing a repetitive sequence induces bundling of actin filaments. J Neurochem 1993, 61(3):979-986. 10.1111/j.1471-4159.1993.tb03611.x, 8360695.
    • (1993) J Neurochem , vol.61 , Issue.3 , pp. 979-986
    • Moraga, D.M.1    Nunez, P.2    Garrido, J.3    Maccioni, R.B.4
  • 10
    • 0022257526 scopus 로고
    • Ca2+ and calmodulin regulate microtubule-associated protein-actin filament interaction in a flip-flop switch
    • 10.1016/0167-4889(85)90200-9, 4005297
    • Sobue K, Tanaka T, Ashino N, Kakiuchi S. Ca2+ and calmodulin regulate microtubule-associated protein-actin filament interaction in a flip-flop switch. Biochim Biophys Acta 1985, 845(3):366-372. 10.1016/0167-4889(85)90200-9, 4005297.
    • (1985) Biochim Biophys Acta , vol.845 , Issue.3 , pp. 366-372
    • Sobue, K.1    Tanaka, T.2    Ashino, N.3    Kakiuchi, S.4
  • 11
    • 0022235642 scopus 로고
    • Calmodulin inhibits interaction of actin with MAP2 and Tau, two major microtubule-associated proteins
    • Kotani S, Nishida E, Kumagai H, Sakai H. Calmodulin inhibits interaction of actin with MAP2 and Tau, two major microtubule-associated proteins. J Biol Chem 1985, 260(19):10779-10783.
    • (1985) J Biol Chem , vol.260 , Issue.19 , pp. 10779-10783
    • Kotani, S.1    Nishida, E.2    Kumagai, H.3    Sakai, H.4
  • 12
    • 0028359217 scopus 로고
    • Organization of actin and microtubules during process formation in tau-expressing Sf9 cells
    • 10.1002/cm.970280308, 7954853
    • Knowles R, LeClerc N, Kosik KS. Organization of actin and microtubules during process formation in tau-expressing Sf9 cells. Cell Motil Cytoskeleton 1994, 28(3):256-264. 10.1002/cm.970280308, 7954853.
    • (1994) Cell Motil Cytoskeleton , vol.28 , Issue.3 , pp. 256-264
    • Knowles, R.1    LeClerc, N.2    Kosik, K.S.3
  • 13
    • 33746565567 scopus 로고    scopus 로고
    • Tau associates with actin in differentiating PC12 cells
    • 10.1096/fj.05-5206com, 16816120
    • Yu JZ, Rasenick MM. Tau associates with actin in differentiating PC12 cells. FASEB J 2006, 20(9):1452-1461. 10.1096/fj.05-5206com, 16816120.
    • (2006) FASEB J , vol.20 , Issue.9 , pp. 1452-1461
    • Yu, J.Z.1    Rasenick, M.M.2
  • 14
    • 33947286683 scopus 로고    scopus 로고
    • Abnormal bundling and accumulation of F-actin mediates tau-induced neuronal degeneration in vivo
    • 10.1038/ncb1528, 17187063
    • Fulga TA, Elson-Schwab I, Khurana V, Steinhilb ML, Spires TL, Hyman BT, Feany MB. Abnormal bundling and accumulation of F-actin mediates tau-induced neuronal degeneration in vivo. Nat Cell Biol 2007, 9(2):139-148. 10.1038/ncb1528, 17187063.
    • (2007) Nat Cell Biol , vol.9 , Issue.2 , pp. 139-148
    • Fulga, T.A.1    Elson-Schwab, I.2    Khurana, V.3    Steinhilb, M.L.4    Spires, T.L.5    Hyman, B.T.6    Feany, M.B.7
  • 15
    • 0033850407 scopus 로고    scopus 로고
    • Tau protein isoforms, phosphorylation and role in neurodegenerative disorders
    • 10.1016/S0165-0173(00)00019-9, 10967355
    • Buee L, Bussiere T, Buee-Scherrer V, Delacourte A, Hof PR. Tau protein isoforms, phosphorylation and role in neurodegenerative disorders. Brain Res Brain Res Rev 2000, 33(1):95-130. 10.1016/S0165-0173(00)00019-9, 10967355.
    • (2000) Brain Res Brain Res Rev , vol.33 , Issue.1 , pp. 95-130
    • Buee, L.1    Bussiere, T.2    Buee-Scherrer, V.3    Delacourte, A.4    Hof, P.R.5
  • 16
    • 0027406644 scopus 로고
    • Functional organization of microtubule-associated protein tau. Identification of regions which affect microtubule growth, nucleation, and bundle formation in vitro
    • Brandt R, Lee G. Functional organization of microtubule-associated protein tau. Identification of regions which affect microtubule growth, nucleation, and bundle formation in vitro. J Biol Chem 1993, 268(5):3414-3419.
    • (1993) J Biol Chem , vol.268 , Issue.5 , pp. 3414-3419
    • Brandt, R.1    Lee, G.2
  • 17
    • 0028820411 scopus 로고
    • Domains of tau protein, differential phosphorylation, and dynamic instability of microtubules
    • 366657, 8590813
    • Trinczek B, Biernat J, Baumann K, Mandelkow EM, Mandelkow E. Domains of tau protein, differential phosphorylation, and dynamic instability of microtubules. Mol Biol Cell 1995, 6(12):1887-1902. 366657, 8590813.
    • (1995) Mol Biol Cell , vol.6 , Issue.12 , pp. 1887-1902
    • Trinczek, B.1    Biernat, J.2    Baumann, K.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 18
    • 0031035402 scopus 로고    scopus 로고
    • Functional interactions between the proline-rich and repeat regions of tau enhance microtubule binding and assembly
    • 276085, 9190213
    • Goode BL, Denis PE, Panda D, Radeke MJ, Miller HP, Wilson L, Feinstein SC. Functional interactions between the proline-rich and repeat regions of tau enhance microtubule binding and assembly. Mol Biol Cell 1997, 8(2):353-365. 276085, 9190213.
    • (1997) Mol Biol Cell , vol.8 , Issue.2 , pp. 353-365
    • Goode, B.L.1    Denis, P.E.2    Panda, D.3    Radeke, M.J.4    Miller, H.P.5    Wilson, L.6    Feinstein, S.C.7
  • 19
    • 49749097123 scopus 로고    scopus 로고
    • Binding to the minor groove of the double-strand, tau protein prevents DNA from damage by peroxidation
    • 2432501, 18596978, 10.1371/journal.pone.0002600
    • Wei Y, Qu MH, Wang XS, Chen L, Wang DL, Liu Y, Hua Q, He RQ. Binding to the minor groove of the double-strand, tau protein prevents DNA from damage by peroxidation. PLoS ONE 2008, 3(7):e2600. 2432501, 18596978, 10.1371/journal.pone.0002600.
    • (2008) PLoS ONE , vol.3 , Issue.7
    • Wei, Y.1    Qu, M.H.2    Wang, X.S.3    Chen, L.4    Wang, D.L.5    Liu, Y.6    Hua, Q.7    He, R.Q.8
  • 21
    • 0026758380 scopus 로고
    • Microtubule bundling by tau proteins in vivo: analysis of functional domains
    • 556906, 1396588
    • Kanai Y, Chen J, Hirokawa N. Microtubule bundling by tau proteins in vivo: analysis of functional domains. EMBO J 1992, 11(11):3953-3961. 556906, 1396588.
    • (1992) EMBO J , vol.11 , Issue.11 , pp. 3953-3961
    • Kanai, Y.1    Chen, J.2    Hirokawa, N.3
  • 22
    • 44949259180 scopus 로고    scopus 로고
    • Complementary dimerization of microtubule-associated tau protein: Implications for microtubule bundling and tau-mediated pathogenesis
    • 2396711, 18495933, 10.1073/pnas.0802036105
    • Rosenberg KJ, Ross JL, Feinstein HE, Feinstein SC, Israelachvili J. Complementary dimerization of microtubule-associated tau protein: Implications for microtubule bundling and tau-mediated pathogenesis. Proc Natl Acad Sci USA 2008, 105(21):7445-7450. 2396711, 18495933, 10.1073/pnas.0802036105.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.21 , pp. 7445-7450
    • Rosenberg, K.J.1    Ross, J.L.2    Feinstein, H.E.3    Feinstein, S.C.4    Israelachvili, J.5
  • 23
    • 10944228450 scopus 로고    scopus 로고
    • Tau and src family tyrosine kinases
    • Lee G. Tau and src family tyrosine kinases. Biochim Biophys Acta 2005, 1739(2-3):323-330.
    • (2005) Biochim Biophys Acta , vol.1739 , Issue.2-3 , pp. 323-330
    • Lee, G.1
  • 24
    • 1842432582 scopus 로고    scopus 로고
    • MAP2c, but not tau, binds and bundles F-actin via its microtubule binding domain
    • 10.1016/j.cub.2004.01.058, 15028210
    • Roger B, Al-Bassam J, Dehmelt L, Milligan RA, Halpain S. MAP2c, but not tau, binds and bundles F-actin via its microtubule binding domain. Curr Biol 2004, 14(5):363-371. 10.1016/j.cub.2004.01.058, 15028210.
    • (2004) Curr Biol , vol.14 , Issue.5 , pp. 363-371
    • Roger, B.1    Al-Bassam, J.2    Dehmelt, L.3    Milligan, R.A.4    Halpain, S.5
  • 25
    • 0030012323 scopus 로고    scopus 로고
    • The polyelectrolyte nature of F-actin and the mechanism of actin bundle formation
    • 10.1074/jbc.271.15.8556, 8621482
    • Tang JX, Janmey PA. The polyelectrolyte nature of F-actin and the mechanism of actin bundle formation. J Biol Chem 1996, 271(15):8556-8563. 10.1074/jbc.271.15.8556, 8621482.
    • (1996) J Biol Chem , vol.271 , Issue.15 , pp. 8556-8563
    • Tang, J.X.1    Janmey, P.A.2
  • 26
    • 33745900235 scopus 로고    scopus 로고
    • The proline-rich domain and the microtubule binding domain of protein tau acting as RNA binding domains
    • 10.2174/092986606777790566, 17018010
    • Wang X, Wang D, Zhao J, Qu M, Zhou X, He H, He R. The proline-rich domain and the microtubule binding domain of protein tau acting as RNA binding domains. Protein Pept Lett 2006, 13(7):679-685. 10.2174/092986606777790566, 17018010.
    • (2006) Protein Pept Lett , vol.13 , Issue.7 , pp. 679-685
    • Wang, X.1    Wang, D.2    Zhao, J.3    Qu, M.4    Zhou, X.5    He, H.6    He, R.7
  • 28
    • 0025600995 scopus 로고
    • Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization
    • 552204, 2124967
    • Goedert M, Jakes R. Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization. EMBO J 1990, 9(13):4225-4230. 552204, 2124967.
    • (1990) EMBO J , vol.9 , Issue.13 , pp. 4225-4230
    • Goedert, M.1    Jakes, R.2
  • 29
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich JA, Watt S. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J Biol Chem 1971, 246(15):4866-4871.
    • (1971) J Biol Chem , vol.246 , Issue.15 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 30
    • 0031968344 scopus 로고    scopus 로고
    • Mechanical properties of actin filament networks depend on preparation, polymerization conditions, and storage of actin monomers
    • 1299613, 9591697, 10.1016/S0006-3495(98)77979-2
    • Xu J, Schwarz WH, Kas JA, Stossel TP, Janmey PA, Pollard TD. Mechanical properties of actin filament networks depend on preparation, polymerization conditions, and storage of actin monomers. Biophys J 1998, 74(5):2731-2740. 1299613, 9591697, 10.1016/S0006-3495(98)77979-2.
    • (1998) Biophys J , vol.74 , Issue.5 , pp. 2731-2740
    • Xu, J.1    Schwarz, W.H.2    Kas, J.A.3    Stossel, T.P.4    Janmey, P.A.5    Pollard, T.D.6
  • 31
    • 0019421552 scopus 로고
    • Microtubule-associated proteins (MAPs) and the organization of actin filaments in vitro
    • 2111865, 6270155, 10.1083/jcb.90.2.467
    • Sattilaro RF, Dentler WL, LeCluyse EL. Microtubule-associated proteins (MAPs) and the organization of actin filaments in vitro. J Cell Biol 1981, 90(2):467-473. 2111865, 6270155, 10.1083/jcb.90.2.467.
    • (1981) J Cell Biol , vol.90 , Issue.2 , pp. 467-473
    • Sattilaro, R.F.1    Dentler, W.L.2    LeCluyse, E.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.