메뉴 건너뛰기




Volumn 120, Issue 22, 2007, Pages 3919-3927

A cool look at the structural changes in kinesin motor domains

Author keywords

Cryo electron microscopy; Image reconstruction; Microtubule motors

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ALPHA TUBULIN; BETA TUBULIN; DIMER; KINESIN; MOLECULAR MOTOR; NUCLEOTIDE;

EID: 37249034254     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.016931     Document Type: Note
Times cited : (10)

References (44)
  • 1
    • 0344198646 scopus 로고    scopus 로고
    • Distinct conformations of the kinesin Unc104 neck regulate a monomer to dimer motor transition
    • Al-Bassam, J., Cui, Y., Klopfenstein, D., Carragher, B. O., Vale, R. D. and Milligan, R. A. (2003). Distinct conformations of the kinesin Unc104 neck regulate a monomer to dimer motor transition. J. Cell Biol. 163, 743-753.
    • (2003) J. Cell Biol , vol.163 , pp. 743-753
    • Al-Bassam, J.1    Cui, Y.2    Klopfenstein, D.3    Carragher, B.O.4    Vale, R.D.5    Milligan, R.A.6
  • 2
    • 0032481381 scopus 로고    scopus 로고
    • Proteolytic mapping of kinesin/ncd-microtubule interface: Nucleotide-dependent conformational changes in the loops L8 and L12
    • Alonso, M. C., Vanderkerckhove, J. and Cross, R. A. (1998). Proteolytic mapping of kinesin/ncd-microtubule interface: Nucleotide-dependent conformational changes in the loops L8 and L12. EMBO J. 17, 945-951.
    • (1998) EMBO J , vol.17 , pp. 945-951
    • Alonso, M.C.1    Vanderkerckhove, J.2    Cross, R.A.3
  • 3
    • 34147188510 scopus 로고    scopus 로고
    • An ATP gate controls tubulin binding by the tethered head of kinesin-1
    • Alonso, M. C., Drummond, D. R., Kain, S., Hoeng, J., Amos, L. A. and Cross, R. A. (2007). An ATP gate controls tubulin binding by the tethered head of kinesin-1. Science 316, 120-123.
    • (2007) Science , vol.316 , pp. 120-123
    • Alonso, M.C.1    Drummond, D.R.2    Kain, S.3    Hoeng, J.4    Amos, L.A.5    Cross, R.A.6
  • 4
    • 0032518489 scopus 로고    scopus 로고
    • Nucleotide-dependent conformations of the kinesin dimer interacting with microtubules
    • Arnal, I. and Wade, R. H. (1998). Nucleotide-dependent conformations of the kinesin dimer interacting with microtubules. Structure 6, 33-38.
    • (1998) Structure , vol.6 , pp. 33-38
    • Arnal, I.1    Wade, R.H.2
  • 5
    • 19644377414 scopus 로고    scopus 로고
    • Mechanics of the kinesin step
    • Carter, N. J. and Cross, R. A. (2005). Mechanics of the kinesin step. Nature 435, 308-312.
    • (2005) Nature , vol.435 , pp. 308-312
    • Carter, N.J.1    Cross, R.A.2
  • 6
    • 0024601079 scopus 로고
    • Quantitative analysis of sea urchin egg kinesin-driven microtubule motility
    • Cohn, S. A., Ingold, A. L. and Scholey, J. M. (1989). Quantitative analysis of sea urchin egg kinesin-driven microtubule motility. J. Biol. Chem. 264, 4290-4297.
    • (1989) J. Biol. Chem , vol.264 , pp. 4290-4297
    • Cohn, S.A.1    Ingold, A.L.2    Scholey, J.M.3
  • 8
    • 32844474892 scopus 로고    scopus 로고
    • A lever-arm rotation drives motility of the minus-end-directed kinesin Ncd
    • Endres, N. F., Yoshioka, C., Milligan, R. A. and Vale, R. D. (2006). A lever-arm rotation drives motility of the minus-end-directed kinesin Ncd. Nature 439, 875-878.
    • (2006) Nature , vol.439 , pp. 875-878
    • Endres, N.F.1    Yoshioka, C.2    Milligan, R.A.3    Vale, R.D.4
  • 9
    • 34147174317 scopus 로고    scopus 로고
    • Processive motor movement
    • Hackney, D. D. (2007). Processive motor movement. Science 316, 58-59.
    • (2007) Science , vol.316 , pp. 58-59
    • Hackney, D.D.1
  • 10
    • 0032559822 scopus 로고    scopus 로고
    • Processivity of the motor protein kinesin requires two heads
    • Hancock, W. O. and Howard, J. (1998). Processivity of the motor protein kinesin requires two heads. J. Cell Biol. 140, 1395-1405.
    • (1998) J. Cell Biol , vol.140 , pp. 1395-1405
    • Hancock, W.O.1    Howard, J.2
  • 11
    • 0029795642 scopus 로고    scopus 로고
    • Three-dimensional cryoelectron microscopy of dimeric kinesin and ncd motor domains on microtubules
    • Hirose, K., Lockhart, A., Cross, R. A. and Amos, L. A. (1996). Three-dimensional cryoelectron microscopy of dimeric kinesin and ncd motor domains on microtubules. Proc. Natl. Acad. Sci. USA 93, 9539-9544.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9539-9544
    • Hirose, K.1    Lockhart, A.2    Cross, R.A.3    Amos, L.A.4
  • 12
    • 0032079618 scopus 로고    scopus 로고
    • Nucleotide-dependent structural changes in dimeric NCD molecules complexed to microtubules
    • Hirose, K., Cross, R. A. and Amos, L. A. (1998). Nucleotide-dependent structural changes in dimeric NCD molecules complexed to microtubules. J. Mol. Biol. 278, 389-400.
    • (1998) J. Mol. Biol , vol.278 , pp. 389-400
    • Hirose, K.1    Cross, R.A.2    Amos, L.A.3
  • 13
    • 0344867017 scopus 로고    scopus 로고
    • Congruent docking of dimeric kinesin and ncd into three-dimensional electron cryomicroscopy maps of microtubule-motor ADP complexes
    • Hirose, K., Löwe, J., Alonso, M., Cross, R. A. and Amos, L. A. (1999). Congruent docking of dimeric kinesin and ncd into three-dimensional electron cryomicroscopy maps of microtubule-motor ADP complexes. Mol. Biol. Cell 10, 2063-2074.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2063-2074
    • Hirose, K.1    Löwe, J.2    Alonso, M.3    Cross, R.A.4    Amos, L.A.5
  • 14
    • 33748421625 scopus 로고    scopus 로고
    • Large conformational changes in a kinesin motor catalysed by interaction with microtubules
    • Hirose, K., Akimaru, E., Akiba, T., Endow, S. A. and Amos, L. A. (2006). Large conformational changes in a kinesin motor catalysed by interaction with microtubules. Mol. Cell 23, 913-923.
    • (2006) Mol. Cell , vol.23 , pp. 913-923
    • Hirose, K.1    Akimaru, E.2    Akiba, T.3    Endow, S.A.4    Amos, L.A.5
  • 15
    • 0032550175 scopus 로고    scopus 로고
    • Image reconstructions of microtubules decorated with monomeric and dimeric kinesins: Comparison with X-ray structure and implications for motility
    • Hoenger, A., Sack, S., Thormahlen, M., Marx, A., Muller, J., Gross, H. and Mandelkow, E. (1998). Image reconstructions of microtubules decorated with monomeric and dimeric kinesins: comparison with X-ray structure and implications for motility. J. Cell Biol. 141, 419-430.
    • (1998) J. Cell Biol , vol.141 , pp. 419-430
    • Hoenger, A.1    Sack, S.2    Thormahlen, M.3    Marx, A.4    Muller, J.5    Gross, H.6    Mandelkow, E.7
  • 17
    • 5144235319 scopus 로고    scopus 로고
    • A new theory and algorithm for reconstructing helical structures with a seam
    • Kikkawa, M. (2004). A new theory and algorithm for reconstructing helical structures with a seam. J. Mol. Biol. 343, 943-955.
    • (2004) J. Mol. Biol , vol.343 , pp. 943-955
    • Kikkawa, M.1
  • 18
    • 33748931452 scopus 로고    scopus 로고
    • High-resolution cryo-EM maps show the nucleotide binding pocket of KIF1A in open and closed conformations
    • Kikkawa, M. and Hirokawa, N. (2006). High-resolution cryo-EM maps show the nucleotide binding pocket of KIF1A in open and closed conformations. EMBO J. 25, 4187-4194.
    • (2006) EMBO J , vol.25 , pp. 4187-4194
    • Kikkawa, M.1    Hirokawa, N.2
  • 22
    • 0033571450 scopus 로고    scopus 로고
    • The crystal structure of the minus-end-directed microtubule motor protein ncd reveals variable dimer conformations
    • Kozielski, F., De Bonis, S., Burmeister, W. P., Cohen-Addad, C. and Wade, R. H. (1999). The crystal structure of the minus-end-directed microtubule motor protein ncd reveals variable dimer conformations. Structure 7, 1407-1416.
    • (1999) Structure , vol.7 , pp. 1407-1416
    • Kozielski, F.1    De Bonis, S.2    Burmeister, W.P.3    Cohen-Addad, C.4    Wade, R.H.5
  • 23
    • 0029989974 scopus 로고    scopus 로고
    • Crystal structure of the kinesin motor domain reveals a structural similarity to myosin
    • Kull, F. J., Sablin, E. P., Lau, R., Fletterick, R. J. and Vale, R. D. (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
    • Kull, F.J.1    Sablin, E.P.2    Lau, R.3    Fletterick, R.J.4    Vale, R.D.5
  • 25
    • 0035834521 scopus 로고    scopus 로고
    • Refined structure of alpha beta-tubulin at 3.5 A resolution
    • Löwe, J., Li, H., Downing, K. H. and Nogales, E. (2001). Refined structure of alpha beta-tubulin at 3.5 A resolution. J. Mol. Biol. 313, 1045-1057.
    • (2001) J. Mol. Biol , vol.313 , pp. 1045-1057
    • Löwe, J.1    Li, H.2    Downing, K.H.3    Nogales, E.4
  • 26
    • 33750456123 scopus 로고    scopus 로고
    • Lucky 13 - microtubule depolymerisation by kinesin-13 motors
    • Moores, C. A. and Milligan, R. A. (2006). Lucky 13 - microtubule depolymerisation by kinesin-13 motors. J. Cell Sci. 119, 3905-3913.
    • (2006) J. Cell Sci , vol.119 , pp. 3905-3913
    • Moores, C.A.1    Milligan, R.A.2
  • 27
    • 33747805355 scopus 로고    scopus 로고
    • Human kinetochore-associated kinesin CENP-E visualized at 17 A resolution bound to microtubules
    • Neumann, E., Garcia-Saez, I., DeBonis, S., Wade, R. H., Kozielski, F. and Conway, J. F. (2006). Human kinetochore-associated kinesin CENP-E visualized at 17 A resolution bound to microtubules. J. Mol. Biol. 362, 203-211.
    • (2006) J. Mol. Biol , vol.362 , pp. 203-211
    • Neumann, E.1    Garcia-Saez, I.2    DeBonis, S.3    Wade, R.H.4    Kozielski, F.5    Conway, J.F.6
  • 28
    • 3442876110 scopus 로고    scopus 로고
    • KIF1A alternately uses two loops to bind microtubules
    • Nitta, R., Kikkawa, M., Okada, Y. and Hirokawa, N. (2004). KIF1A alternately uses two loops to bind microtubules. Science 305, 678-683.
    • (2004) Science , vol.305 , pp. 678-683
    • Nitta, R.1    Kikkawa, M.2    Okada, Y.3    Hirokawa, N.4
  • 29
    • 1342296567 scopus 로고    scopus 로고
    • A common mechanism for microtubule destabilizers - M type kinesins stabilize curling of the protofilament using the class-specific neck and loops
    • Ogawa, T., Nitta, R., Okada, Y. and Hirokawa, N. (2004). A common mechanism for microtubule destabilizers - M type kinesins stabilize curling of the protofilament using the class-specific neck and loops. Cell 116, 591-602.
    • (2004) Cell , vol.116 , pp. 591-602
    • Ogawa, T.1    Nitta, R.2    Okada, Y.3    Hirokawa, N.4
  • 33
    • 0030744142 scopus 로고    scopus 로고
    • Kinesin hydrolyses one ATP per 9-nm step
    • Schnitzer, M. J. and Block, S. M. (1997). Kinesin hydrolyses one ATP per 9-nm step. Nature 388, 386-390.
    • (1997) Nature , vol.388 , pp. 386-390
    • Schnitzer, M.J.1    Block, S.M.2
  • 34
    • 34248200882 scopus 로고    scopus 로고
    • ne beginning of kinesin's force-generating cycle visualized at 9-A resolution
    • Sindelar, C. V. and Downing, K. H. (2007). ne beginning of kinesin's force-generating cycle visualized at 9-A resolution. J. Cell Biol. 177, 377-385.
    • (2007) J. Cell Biol , vol.177 , pp. 377-385
    • Sindelar, C.V.1    Downing, K.H.2
  • 35
    • 0036830220 scopus 로고    scopus 로고
    • Two conformations in the human kinesin power stroke defined by X-ray crystallography and EPR spectroscopy
    • Sindelar, C. V., Budny, M. J., Rice, S., Naber, N., Fletterick, R. and Cooke, R. (2002). Two conformations in the human kinesin power stroke defined by X-ray crystallography and EPR spectroscopy. Nat. Struct. Biol. 9, 844-848.
    • (2002) Nat. Struct. Biol , vol.9 , pp. 844-848
    • Sindelar, C.V.1    Budny, M.J.2    Rice, S.3    Naber, N.4    Fletterick, R.5    Cooke, R.6
  • 36
    • 0030927934 scopus 로고    scopus 로고
    • Three different approaches for calculating the three-dimensional structure of microtubules decorated with kinesin motor domains
    • Sosa, H., Hoenger, A. and Milligan, R. A. (1997). Three different approaches for calculating the three-dimensional structure of microtubules decorated with kinesin motor domains. J. Struct. Biol. 118, 149-158.
    • (1997) J. Struct. Biol , vol.118 , pp. 149-158
    • Sosa, H.1    Hoenger, A.2    Milligan, R.A.3
  • 37
    • 0035816597 scopus 로고    scopus 로고
    • Crystal structure of the mitotic spindle kinesin Eg5 reveals a novel conformation of the neck-linker
    • Turner, J., Anderson, R., Guo, J., Beraud, C., Fletterick, R. and Sakowicz, R. (2001). Crystal structure of the mitotic spindle kinesin Eg5 reveals a novel conformation of the neck-linker. J. Biol. Chem. 276, 25496-25502.
    • (2001) J. Biol. Chem , vol.276 , pp. 25496-25502
    • Turner, J.1    Anderson, R.2    Guo, J.3    Beraud, C.4    Fletterick, R.5    Sakowicz, R.6
  • 38
    • 0343415156 scopus 로고    scopus 로고
    • The way things move: Looking under the hood of molecular motor proteins
    • Vale, R. D. and Milligan, R. A. (2000). The way things move: looking under the hood of molecular motor proteins. Science 288, 88-95.
    • (2000) Science , vol.288 , pp. 88-95
    • Vale, R.D.1    Milligan, R.A.2
  • 39
    • 0029879228 scopus 로고    scopus 로고
    • Direct observation of single kinesin molecules moving along microtubules
    • Vale, R. D., Funatsu, T., Pierce, D. W., Romberg, L., Harada, Y. and Yanagida, T. (1996). Direct observation of single kinesin molecules moving along microtubules. Nature 380, 451-453.
    • (1996) Nature , vol.380 , pp. 451-453
    • Vale, R.D.1    Funatsu, T.2    Pierce, D.W.3    Romberg, L.4    Harada, Y.5    Yanagida, T.6
  • 40
  • 42
    • 0032502328 scopus 로고    scopus 로고
    • One-headed kinesin derivatives move by a nonprocessive, low-duty ratio mechanism unlike that of two-headed kinesin
    • Young, E. C., Mahtani, H. K. and Gelles, J. (1998). One-headed kinesin derivatives move by a nonprocessive, low-duty ratio mechanism unlike that of two-headed kinesin. Biochemistry 37, 3467-3479.
    • (1998) Biochemistry , vol.37 , pp. 3467-3479
    • Young, E.C.1    Mahtani, H.K.2    Gelles, J.3
  • 43
    • 0035355208 scopus 로고    scopus 로고
    • A structural pathway for activation of the kinesin motor ATPase
    • Yun, M., Zhang, X., Park, C. G., Park, H. W. and Endow, S. A. (2001). A structural pathway for activation of the kinesin motor ATPase. EMBO J. 20, 2611-2618.
    • (2001) EMBO J , vol.20 , pp. 2611-2618
    • Yun, M.1    Zhang, X.2    Park, C.G.3    Park, H.W.4    Endow, S.A.5
  • 44
    • 0142073737 scopus 로고    scopus 로고
    • Rotation of the stalk/neck and one head in a new crystal structure of the kinesin motor protein, Ncd
    • Yun, M., Bronner, C. E., Park, C. G., Cha, S. S., Park, H. W. and Endow, S. A. (2003). Rotation of the stalk/neck and one head in a new crystal structure of the kinesin motor protein, Ncd. EMBO J. 22, 5382-5389.
    • (2003) EMBO J , vol.22 , pp. 5382-5389
    • Yun, M.1    Bronner, C.E.2    Park, C.G.3    Cha, S.S.4    Park, H.W.5    Endow, S.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.