메뉴 건너뛰기




Volumn 23, Issue 13, 2004, Pages 2459-2467

Dynein and kinesin share an overlapping microtubule-binding site

Author keywords

Cryo electron microscopy; Dynein; Kinesin; Protein structure; Tubulin

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DIMER; DYNEIN ADENOSINE TRIPHOSPHATASE; DYNEIN STALK HEAD PROTEIN; KINESIN; MOLECULAR MOTOR; PROTEIN; TUBULIN; UNCLASSIFIED DRUG;

EID: 3342957252     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.emboj.7600240     Document Type: Article
Times cited : (109)

References (58)
  • 1
    • 0037166943 scopus 로고    scopus 로고
    • MAP2 and tau bind longitudinally along the outer ridges of microtubule protofilaments
    • Al-Bassam J, Ozer RS, Safer D, Halpain S, Milligan RA (2002) MAP2 and tau bind longitudinally along the outer ridges of microtubule protofilaments. J Cell Biol 157: 1187-1196
    • (2002) J Cell Biol , vol.157 , pp. 1187-1196
    • Al-Bassam, J.1    Ozer, R.S.2    Safer, D.3    Halpain, S.4    Milligan, R.A.5
  • 2
    • 0016367327 scopus 로고
    • Arrangement of subunits in flagellar microtubules
    • Amos L, Klug A (1974) Arrangement of subunits in flagellar microtubules. J Cell Sci 14: 523-549
    • (1974) J Cell Sci , vol.14 , pp. 523-549
    • Amos, L.1    Klug, A.2
  • 3
    • 0031042321 scopus 로고    scopus 로고
    • The structure of microtubule-motor complexes
    • Amos LA, Hirose K (1997) The structure of microtubule-motor complexes. Curr Opin Cell Biol 9: 4-11
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 4-11
    • Amos, L.A.1    Hirose, K.2
  • 4
    • 0031460411 scopus 로고    scopus 로고
    • Distortion correction of tubular crystals: Improvements in the acetylcholine receptor structure
    • Beroukhim R, Unwin N (1997) Distortion correction of tubular crystals: improvements in the acetylcholine receptor structure. Ultramicroscopy 70: 57-81
    • (1997) Ultramicroscopy , vol.70 , pp. 57-81
    • Beroukhim, R.1    Unwin, N.2
  • 5
    • 0031603961 scopus 로고    scopus 로고
    • Purification of dynactin and dynein from brain tissue
    • Bingham JB, King SJ, Schroer TA (1998) Purification of dynactin and dynein from brain tissue. Methods Enzymol 298: 171-184
    • (1998) Methods Enzymol , vol.298 , pp. 171-184
    • Bingham, J.B.1    King, S.J.2    Schroer, T.A.3
  • 6
    • 0029068861 scopus 로고
    • Rigor and relaxed outer dynein arms in replicas of cryofixed motile flagella
    • Burgess SA (1995) Rigor and relaxed outer dynein arms in replicas of cryofixed motile flagella. J Mol Biol 250: 52-63
    • (1995) J Mol Biol , vol.250 , pp. 52-63
    • Burgess, S.A.1
  • 7
    • 0026071078 scopus 로고
    • Architecture of the outer arm dynein ATPase in an avian sperm flagellum, with further evidence for the B-link
    • Burgess SA, Dover SD, Woolley DM (1991) Architecture of the outer arm dynein ATPase in an avian sperm flagellum, with further evidence for the B-link. J Cell Sci 98: 17-26
    • (1991) J Cell Sci , vol.98 , pp. 17-26
    • Burgess, S.A.1    Dover, S.D.2    Woolley, D.M.3
  • 9
    • 0030587566 scopus 로고    scopus 로고
    • Determination of microtubule polarity by cryo-electron microscopy
    • Chretien D, Kenney JM, Fuller SD, Wade RH (1996) Determination of microtubule polarity by cryo-electron microscopy. Structure 4: 1031-1040
    • (1996) Structure , vol.4 , pp. 1031-1040
    • Chretien, D.1    Kenney, J.M.2    Fuller, S.D.3    Wade, R.H.4
  • 10
    • 0033586776 scopus 로고    scopus 로고
    • Motility of dimeric ncd on a metal-chelating surfactant: Evidence that ncd is not processive
    • deCastro MJ, Ho CH, Stewart RJ (1999) Motility of dimeric ncd on a metal-chelating surfactant: evidence that ncd is not processive. Biochemistry 38: 5076-5081
    • (1999) Biochemistry , vol.38 , pp. 5076-5081
    • DeCastro, M.J.1    Ho, C.H.2    Stewart, R.J.3
  • 11
    • 0031664002 scopus 로고    scopus 로고
    • The role of the dynein stalk in cytoplasmic and flagellar motility
    • Gee M, Vallee R (1998) The role of the dynein stalk in cytoplasmic and flagellar motility. Eur Biophys J 27: 466-473
    • (1998) Eur Biophys J , vol.27 , pp. 466-473
    • Gee, M.1    Vallee, R.2
  • 12
    • 0031444202 scopus 로고    scopus 로고
    • An extended microtubule-binding structure within the dynein motor domain
    • Gee M, Heuser JE, Vallee RB (1997) An extended microtubule-binding structure within the dynein motor domain. Nature 390: 636-639
    • (1997) Nature , vol.390 , pp. 636-639
    • Gee, M.1    Heuser, J.E.2    Vallee, R.B.3
  • 13
    • 0026425402 scopus 로고
    • Multiple nucleotide-binding sites in the sequence of dynein beta heavy chain
    • Gibbons IR, Gibbons BH, Mocz G, Asai DJ (1991) Multiple nucleotide-binding sites in the sequence of dynein beta heavy chain. Nature 352: 640-643
    • (1991) Nature , vol.352 , pp. 640-643
    • Gibbons, I.R.1    Gibbons, B.H.2    Mocz, G.3    Asai, D.J.4
  • 14
    • 0021630304 scopus 로고
    • Structural comparison of purified dynein proteins with in situ dynein arms
    • Goodenough U, Heuser J (1984) Structural comparison of purified dynein proteins with in situ dynein arms. J Mol Biol 180: 1083-1118
    • (1984) J Mol Biol , vol.180 , pp. 1083-1118
    • Goodenough, U.1    Heuser, J.2
  • 15
    • 0020410980 scopus 로고
    • Substructure of the outer dynein arm
    • Goodenough UW, Heuser JE (1982) Substructure of the outer dynein arm. J Cell Biol 95: 798-815
    • (1982) J Cell Biol , vol.95 , pp. 798-815
    • Goodenough, U.W.1    Heuser, J.E.2
  • 16
    • 0013942764 scopus 로고
    • Observations on the substructure of flagellar fibres
    • Grimstone AV, Klug A (1966) Observations on the substructure of flagellar fibres. J Cell Sci 1: 351-362
    • (1966) J Cell Sci , vol.1 , pp. 351-362
    • Grimstone, A.V.1    Klug, A.2
  • 17
    • 0027957063 scopus 로고
    • Competition between motor molecules (kinesin and cytoplasmic dynein) and fibrous microtubule-associated proteins in binding to microtubules
    • Hagiwara H, Yorifuji H, Sato-Yoshitake R, Hirokawa N (1994) Competition between motor molecules (kinesin and cytoplasmic dynein) and fibrous microtubule-associated proteins in binding to microtubules. J Biol Chem 269: 3581-3589
    • (1994) J Biol Chem , vol.269 , pp. 3581-3589
    • Hagiwara, H.1    Yorifuji, H.2    Sato-Yoshitake, R.3    Hirokawa, N.4
  • 18
    • 0034646431 scopus 로고    scopus 로고
    • Processive movement of single 22S dynein molecules occurs only at low ATP concentrations
    • Hirakawa E, Higuchi H, Toyoshima YY (2000) Processive movement of single 22S dynein molecules occurs only at low ATP concentrations. Proc Natl Acad Sci USA 97: 2533-2537
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 2533-2537
    • Hirakawa, E.1    Higuchi, H.2    Toyoshima, Y.Y.3
  • 19
    • 0032559260 scopus 로고    scopus 로고
    • Kinesin and dynein superfamily proteins and the mechanism of organelle transport
    • Hirokawa N (1998) Kinesin and dynein superfamily proteins and the mechanism of organelle transport. Science 279: 519-526
    • (1998) Science , vol.279 , pp. 519-526
    • Hirokawa, N.1
  • 20
    • 0028979598 scopus 로고
    • Nucleotide-dependent angular change in kinesin motor domain bound to tubulin
    • Hirose K, Lockhart A, Cross RA, Amos LA (1995) Nucleotide-dependent angular change in kinesin motor domain bound to tubulin. Nature 376: 277-279
    • (1995) Nature , vol.376 , pp. 277-279
    • Hirose, K.1    Lockhart, A.2    Cross, R.A.3    Amos, L.A.4
  • 22
    • 84889120137 scopus 로고
    • Improved methods of building protein models in electron density maps and the location of errors in these models
    • Jones T, Zou J, Cowan S, Kjelgaard M (1991) Improved methods of building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47: 110-119
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.1    Zou, J.2    Cowan, S.3    Kjelgaard, M.4
  • 23
    • 0028597558 scopus 로고
    • Direct visualization of the microtubule lattice seam both in vitro and in vivo
    • Kikkawa M, Ishikawa T, Nakata T, Wakabayashi T, Hirokawa N (1994) Direct visualization of the microtubule lattice seam both in vitro and in vivo. J Cell Biol 127: 1965-1971
    • (1994) J Cell Biol , vol.127 , pp. 1965-1971
    • Kikkawa, M.1    Ishikawa, T.2    Nakata, T.3    Wakabayashi, T.4    Hirokawa, N.5
  • 24
    • 0028979606 scopus 로고
    • Three-dimensional structure of the kinesin head-microtubule complex
    • Kikkawa M, Ishikawa T, Wakabayashi T, Hirokawa N (1995) Three-dimensional structure of the kinesin head-microtubule complex. Nature 376: 274-277
    • (1995) Nature , vol.376 , pp. 274-277
    • Kikkawa, M.1    Ishikawa, T.2    Wakabayashi, T.3    Hirokawa, N.4
  • 25
    • 0034695259 scopus 로고    scopus 로고
    • 15 Å resolution model of the monomeric kinesin motor, KIF1A
    • Kikkawa M, Okada Y, Hirokawa N (2000) 15 Å resolution model of the monomeric kinesin motor, KIF1A. Cell 100: 241-252
    • (2000) Cell , vol.100 , pp. 241-252
    • Kikkawa, M.1    Okada, Y.2    Hirokawa, N.3
  • 27
    • 0030877444 scopus 로고    scopus 로고
    • Identification of a microtubule-binding domain in a cytoplasmic dynein heavy chain
    • Koonce MP (1997) Identification of a microtubule-binding domain in a cytoplasmic dynein heavy chain. J Biol Chem 272: 19714-19718
    • (1997) J Biol Chem , vol.272 , pp. 19714-19718
    • Koonce, M.P.1
  • 28
    • 0034001336 scopus 로고    scopus 로고
    • Functional elements within the dynein microtubule-binding domain
    • Koonce MP, Tikhonenko I (2000) Functional elements within the dynein microtubule-binding domain. Mol Biol Cell 11: 523-529
    • (2000) Mol Biol Cell , vol.11 , pp. 523-529
    • Koonce, M.P.1    Tikhonenko, I.2
  • 29
    • 0345118121 scopus 로고    scopus 로고
    • Complex formation with kinesin motor domains affects the structure of microtubules
    • Krebs A, Goldie KN, Hoenger A (2004) Complex formation with kinesin motor domains affects the structure of microtubules. J Mol Biol 335: 139-153
    • (2004) J Mol Biol , vol.335 , pp. 139-153
    • Krebs, A.1    Goldie, K.N.2    Hoenger, A.3
  • 30
    • 0029989974 scopus 로고    scopus 로고
    • Crystal structure of the kinesin motor domain reveals a structural similarity to myosin
    • KuIl FJ, Sablin EP, Lau R, Fletterick RJ, Vale RD (1996) Crystal structure of the kinesin motor domain reveals a structural similarity to myosin. Nature 380: 550-555
    • (1996) Nature , vol.380 , pp. 550-555
    • KuIl, F.J.1    Sablin, E.P.2    Lau, R.3    Fletterick, R.J.4    Vale, R.D.5
  • 31
    • 0029012977 scopus 로고
    • Kinesin and ncd bind through a single head to microtubules and compete for a shared MT binding site
    • Lockhart A, Crevel IM, Cross RA (1995) Kinesin and ncd bind through a single head to microtubules and compete for a shared MT binding site. J Mol Biol 249: 763-771
    • (1995) J Mol Biol , vol.249 , pp. 763-771
    • Lockhart, A.1    Crevel, I.M.2    Cross, R.A.3
  • 32
    • 0035834521 scopus 로고    scopus 로고
    • Refined structure of alpha beta-tubulin at 3.5 Å resolution
    • Lowe J, Li H, Downing KH, Nogales E (2001) Refined structure of alpha beta-tubulin at 3.5 Å resolution. J Mol Biol 313: 1045-1057
    • (2001) J Mol Biol , vol.313 , pp. 1045-1057
    • Lowe, J.1    Li, H.2    Downing, K.H.3    Nogales, E.4
  • 33
    • 0032966626 scopus 로고    scopus 로고
    • Structures of kinesin and kinesin-microtubule interactions
    • Mandelkow E, Hoenger A (1999) Structures of kinesin and kinesin-microtubule interactions. Curr Opin Cell Biol 11: 34-44
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 34-44
    • Mandelkow, E.1    Hoenger, A.2
  • 34
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell JA, Grigorieff N (2003) Accurate determination of local defocus and specimen tilt in electron microscopy. J Struct Biol 142: 334-347
    • (2003) J Struct Biol , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 35
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald AF, Aravind L, Spouge JL, Koonin EV (1999) AAA+: a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res 9: 27-43
    • (1999) Genome Res , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 36
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the alpha beta tubulin dimer by electron crystallography
    • Nogales E, Wolf SG, Downing KH (1998) Structure of the alpha beta tubulin dimer by electron crystallography. Nature 391: 199-203
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 37
    • 0026425498 scopus 로고
    • Four ATP-binding sites in the midregion of the beta heavy chain of dynein
    • Ogawa K (1991) Four ATP-binding sites in the midregion of the beta heavy chain of dynein. Nature 352: 643-645
    • (1991) Nature , vol.352 , pp. 643-645
    • Ogawa, K.1
  • 38
    • 0024306241 scopus 로고
    • Interaction of brain cytoplasmic dynein and MAP2 with a common sequence at the C terminus of tubulin
    • Paschal BM, Obar RA, Vallee RB (1989) Interaction of brain cytoplasmic dynein and MAP2 with a common sequence at the C terminus of tubulin. Nature 342: 569-572
    • (1989) Nature , vol.342 , pp. 569-572
    • Paschal, B.M.1    Obar, R.A.2    Vallee, R.B.3
  • 39
    • 0027211908 scopus 로고
    • Kinesin follows the microtubule's protofilament axis
    • Ray S, Meyhofer E, Milligan R, Howard J (1993) Kinesin follows the microtubule's protofilament axis. J Cell Biol 121: 1083-1093
    • (1993) J Cell Biol , vol.121 , pp. 1083-1093
    • Ray, S.1    Meyhofer, E.2    Milligan, R.3    Howard, J.4
  • 41
    • 0033527027 scopus 로고    scopus 로고
    • Inner-arm dynein c of Chlamydomonas flagella is a single-headed processive motor
    • Sakakibara H, Kojima H, Sakai Y, Katayama E, Oiwa K (1999) Inner-arm dynein c of Chlamydomonas flagella is a single-headed processive motor. Nature 400: 586-590
    • (1999) Nature , vol.400 , pp. 586-590
    • Sakakibara, H.1    Kojima, H.2    Sakai, Y.3    Katayama, E.4    Oiwa, K.5
  • 42
    • 0032513004 scopus 로고    scopus 로고
    • Structural characterization of a dynein motor domain
    • Samso M, Radermacher M, Frank J, Koonce MP (1998) Structural characterization of a dynein motor domain. J Mol Biol 276: 927-937
    • (1998) J Mol Biol , vol.276 , pp. 927-937
    • Samso, M.1    Radermacher, M.2    Frank, J.3    Koonce, M.P.4
  • 43
    • 0037119947 scopus 로고    scopus 로고
    • Single-molecule investigation of the interference between kinesin, tau and MAP2c
    • Seitz A, Kojima H, Oiwa K, Mandelkow EM, Song YH, Mandelkow E (2002) Single-molecule investigation of the interference between kinesin, tau and MAP2c. EMBO J 21: 4896-4905
    • (2002) EMBO J , vol.21 , pp. 4896-4905
    • Seitz, A.1    Kojima, H.2    Oiwa, K.3    Mandelkow, E.M.4    Song, Y.H.5    Mandelkow, E.6
  • 44
    • 0015595694 scopus 로고
    • Microtubule assembly in the absence of added nucleotides
    • Shelanski M, Gaskin F, Cantor C (1973) Microtubule assembly in the absence of added nucleotides. Proc Natl Acad Sci USA 70: 765-768
    • (1973) Proc Natl Acad Sci USA , vol.70 , pp. 765-768
    • Shelanski, M.1    Gaskin, F.2    Cantor, C.3
  • 45
    • 0034871465 scopus 로고    scopus 로고
    • Regulation of monomeric dynein activity by ATP and ADP concentrations
    • Shiroguchi K, Toyoshima YY (2001) Regulation of monomeric dynein activity by ATP and ADP concentrations. Cell Motil Cytoskeleton 49: 189-199
    • (2001) Cell Motil Cytoskeleton , vol.49 , pp. 189-199
    • Shiroguchi, K.1    Toyoshima, Y.Y.2
  • 48
    • 2342509760 scopus 로고    scopus 로고
    • Properties of the full-length heavy chains of Tetrahymena ciliary outer arm dynein separated by urea treatment
    • Toba S, Gibson TM, Shiroguchi K, Toyoshima YY, Asai DJ (2004) Properties of the full-length heavy chains of Tetrahymena ciliary outer arm dynein separated by urea treatment. Cell Motil Cytoskeleton 58: 30-38
    • (2004) Cell Motil Cytoskeleton , vol.58 , pp. 30-38
    • Toba, S.1    Gibson, T.M.2    Shiroguchi, K.3    Toyoshima, Y.Y.4    Asai, D.J.5
  • 49
    • 0031004776 scopus 로고    scopus 로고
    • Probing the kinesin-microtubule interaction
    • Tucker C, Goldstein LS (1997) Probing the kinesin-microtubule interaction. J Biol Chem 272: 9481-9488
    • (1997) J Biol Chem , vol.272 , pp. 9481-9488
    • Tucker, C.1    Goldstein, L.S.2
  • 50
    • 0034693043 scopus 로고    scopus 로고
    • Distinct but overlapping sites within the cytoplasmic dynein heavy chain for dimerization and for intermediate chain and light intermediate chain binding
    • Tynan SH, Gee MA, Vallee RB (2000) Distinct but overlapping sites within the cytoplasmic dynein heavy chain for dimerization and for intermediate chain and light intermediate chain binding. J Biol Chem 275: 32769-32774
    • (2000) J Biol Chem , vol.275 , pp. 32769-32774
    • Tynan, S.H.1    Gee, M.A.2    Vallee, R.B.3
  • 51
    • 0037459061 scopus 로고    scopus 로고
    • The molecular motor toolbox for intracellular transport
    • Vale RD (2003) The molecular motor toolbox for intracellular transport. Cell 112: 467-480
    • (2003) Cell , vol.112 , pp. 467-480
    • Vale, R.D.1
  • 52
    • 0024284804 scopus 로고
    • Rotation and translocation of microtubules in vitro induced by dyneins from Tetrahymena cilia
    • Vale RD, Toyoshima YY (1988) Rotation and translocation of microtubules in vitro induced by dyneins from Tetrahymena cilia. Cell 52: 459-469
    • (1988) Cell , vol.52 , pp. 459-469
    • Vale, R.D.1    Toyoshima, Y.Y.2
  • 53
    • 0029932027 scopus 로고    scopus 로고
    • Targeting of motor proteins
    • Vallee RB, Sheetz MP (1996) Targeting of motor proteins. Science 271: 1539-1544
    • (1996) Science , vol.271 , pp. 1539-1544
    • Vallee, R.B.1    Sheetz, M.P.2
  • 54
    • 0029055373 scopus 로고
    • ncd and kinesin motor domains interact with both alpha- and beta-tubulin
    • Walker RA (1995) ncd and kinesin motor domains interact with both alpha- and beta-tubulin. Proc Natl Acad Sci USA 92: 5960-5964
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5960-5964
    • Walker, R.A.1
  • 55
    • 0028859428 scopus 로고
    • Single cytoplasmic dynein molecule movements: Characterization and comparison with kinesin
    • Wang Z, Khan S, Sheetz MP (1995) Single cytoplasmic dynein molecule movements: characterization and comparison with kinesin. Biophys J 69: 2011-2023
    • (1995) Biophys J , vol.69 , pp. 2011-2023
    • Wang, Z.1    Khan, S.2    Sheetz, M.P.3
  • 56
    • 0034079578 scopus 로고    scopus 로고
    • The C-terminus of tubulin increases cytoplasmic dynein and kinesin processivity
    • Wang Z, Sheetz MP (2000) The C-terminus of tubulin increases cytoplasmic dynein and kinesin processivity. Biophys J 78: 1955-1964
    • (2000) Biophys J , vol.78 , pp. 1955-1964
    • Wang, Z.1    Sheetz, M.P.2
  • 57
    • 0024550571 scopus 로고
    • A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses
    • Yang J, Laymon R, Goldstein L (1989) A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses. Cell 56: 879-889
    • (1989) Cell , vol.56 , pp. 879-889
    • Yang, J.1    Laymon, R.2    Goldstein, L.3
  • 58
    • 0034085151 scopus 로고    scopus 로고
    • Structure determination of tubular crystals of membrane proteins. II. Averaging of tubular crystals of different helical classes
    • Yonekura K, Toyoshima C (2000) Structure determination of tubular crystals of membrane proteins. II. Averaging of tubular crystals of different helical classes. Ultramicroscopy 84: 15-28
    • (2000) Ultramicroscopy , vol.84 , pp. 15-28
    • Yonekura, K.1    Toyoshima, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.