메뉴 건너뛰기




Volumn 383, Issue 2, 2004, Pages 227-235

C-terminus of mitotic centromere-associated kinesin (MCAK) inhibits its lattice-stimulated ATPase activity

Author keywords

ATPase activity; Kin I; Microtubule depolymerization; Mitosis; Mitotic centromere associated kinesin (MCAK); Xenopus kinesin catastrophe modulator 1 (XKCM1)

Indexed keywords

AMINO ACIDS; BIOASSAY; DEPOLYMERIZATION; DIMERS; ENZYME INHIBITION; HYDROLYSIS;

EID: 4644339944     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20040736     Document Type: Article
Times cited : (36)

References (33)
  • 1
    • 0033280668 scopus 로고    scopus 로고
    • The road less traveled: Emerging principles of kinesin motor utilization
    • Goldstein, L. S. and Philp, A. V. (1999) The road less traveled: emerging principles of kinesin motor utilization. Annu. Rev. Cell Dev. Biol. 15, 141-183
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 141-183
    • Goldstein, L.S.1    Philp, A.V.2
  • 3
    • 0022385727 scopus 로고
    • Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility
    • Vale, R. D., Reese, T. S. and Sheetz, M. P. (1985) Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility. Cell 42, 39-50
    • (1985) Cell , vol.42 , pp. 39-50
    • Vale, R.D.1    Reese, T.S.2    Sheetz, M.P.3
  • 4
    • 0021808444 scopus 로고
    • A novel brain ATPase with properties expected for the fast axonal transport motor
    • Brady, S. T. (1985) A novel brain ATPase with properties expected for the fast axonal transport motor. Nature (London) 317, 73-75
    • (1985) Nature (London) , vol.317 , pp. 73-75
    • Brady, S.T.1
  • 5
    • 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
  • 6
    • 1342296567 scopus 로고    scopus 로고
    • A common mechanism for microtubule destabilizes - 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 destabilizes - 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
  • 8
    • 0028887847 scopus 로고
    • Identification and partial characterization of mitotic centromere-associated kinesin, a kinesin-related protein that associates with centromeres during mitosis
    • Wordeman, L. and Mitchison, T. J. (1995) Identification and partial characterization of mitotic centromere-associated kinesin, a kinesin-related protein that associates with centromeres during mitosis. J. Cell Biol. 128, 95-104
    • (1995) J. Cell Biol. , vol.128 , pp. 95-104
    • Wordeman, L.1    Mitchison, T.J.2
  • 9
    • 0033534575 scopus 로고    scopus 로고
    • Kin I kinesins are microtubule-destabilizing enzymes
    • Desai, A., Verma, S., Mitchison, T. J. and Walczak, C. E. (1999) Kin I kinesins are microtubule-destabilizing enzymes. Cell 96, 69-78
    • (1999) Cell , vol.96 , pp. 69-78
    • Desai, A.1    Verma, S.2    Mitchison, T.J.3    Walczak, C.E.4
  • 10
    • 0030031999 scopus 로고    scopus 로고
    • XKCM1: A Xenopus kinesin-related protein that regulates microtubule dynamics during mitotic spindle assembly
    • Walczak, C. E., Mitchison, T. J. and Desai, A. (1996) XKCM1: a Xenopus kinesin-related protein that regulates microtubule dynamics during mitotic spindle assembly. Cell 84, 37-47
    • (1996) Cell , vol.84 , pp. 37-47
    • Walczak, C.E.1    Mitchison, T.J.2    Desai, A.3
  • 11
    • 0035860717 scopus 로고    scopus 로고
    • Molecular dissection of the microtubule depolymerizing activity of mitotic centromere-associated kinesin
    • Maney, T., Wagenbach, M. and Wordeman, L. (2001) Molecular dissection of the microtubule depolymerizing activity of mitotic centromere-associated kinesin. J. Biol. Chem. 276, 34753-34758
    • (2001) J. Biol. Chem. , vol.276 , pp. 34753-34758
    • Maney, T.1    Wagenbach, M.2    Wordeman, L.3
  • 12
    • 0043199576 scopus 로고    scopus 로고
    • Kinesin superfamily protein 2A (KIF2A) functions in suppression of collateral branch extension
    • Homma, N., Takei, Y., Tanaka, Y., Nakata, T., Terada, S., Kikkawa, M., Noda, Y. and Hirokawa, N. (2003) Kinesin superfamily protein 2A (KIF2A) functions in suppression of collateral branch extension. Cell 114, 229-239
    • (2003) Cell , vol.114 , pp. 229-239
    • Homma, N.1    Takei, Y.2    Tanaka, Y.3    Nakata, T.4    Terada, S.5    Kikkawa, M.6    Noda, Y.7    Hirokawa, N.8
  • 15
    • 0031873388 scopus 로고    scopus 로고
    • Mitotic centromere-associated kinesin is important for anaphase chromosome segregation
    • Maney, T., Hunter, A. W., Wagenbach, M. and Wordeman, L. (1998) Mitotic centromere-associated kinesin is important for anaphase chromosome segregation. J. Cell Biol. 142, 787-801
    • (1998) J. Cell Biol. , vol.142 , pp. 787-801
    • Maney, T.1    Hunter, A.W.2    Wagenbach, M.3    Wordeman, L.4
  • 16
    • 0037175396 scopus 로고    scopus 로고
    • K-loop insertion restores microtubule depolymerizing activity of a 'neckless' MCAK mutant
    • Ovechkina, Y., Wagenbach, M. and Wordeman, L. (2002) K-loop insertion restores microtubule depolymerizing activity of a 'neckless' MCAK mutant. J. Cell Biol. 159, 557-562
    • (2002) J. Cell Biol. , vol.159 , pp. 557-562
    • Ovechkina, Y.1    Wagenbach, M.2    Wordeman, L.3
  • 17
    • 0037292454 scopus 로고    scopus 로고
    • The kinesin-related protein MCAK is a microtubule depolymerase that forms an ATP-hydrolyzing complex at microtubule ends
    • Hunter, A. W., Caplow, M., Coy, D. L., Hancock, W. O., Diez, S., Wordeman, L. and Howard, J. (2003) The kinesin-related protein MCAK is a microtubule depolymerase that forms an ATP-hydrolyzing complex at microtubule ends. Mol. Cell 11, 445-457
    • (2003) Mol. Cell , vol.11 , pp. 445-457
    • Hunter, A.W.1    Caplow, M.2    Coy, D.L.3    Hancock, W.O.4    Diez, S.5    Wordeman, L.6    Howard, J.7
  • 19
  • 20
    • 0033525190 scopus 로고    scopus 로고
    • Kinesin takes one 8-nm step for each ATP that it hydrolyzes
    • Coy, D. L., Wagenbach, M. and Howard, J. (1999) Kinesin takes one 8-nm step for each ATP that it hydrolyzes. J. Biol. Chem. 274, 3667-3671
    • (1999) J. Biol. Chem. , vol.274 , pp. 3667-3671
    • Coy, D.L.1    Wagenbach, M.2    Howard, J.3
  • 21
    • 0026705754 scopus 로고
    • Kinesin undergoes a 9 S to 6 S conformational transition
    • Hackney, D. D., Levitt, J. D. and Suhan, J. (1992) Kinesin undergoes a 9 S to 6 S conformational transition. J. Biol. Chem. 267, 8696-8701
    • (1992) J. Biol. Chem. , vol.267 , pp. 8696-8701
    • Hackney, D.D.1    Levitt, J.D.2    Suhan, J.3
  • 22
    • 0033771901 scopus 로고    scopus 로고
    • Kinesin's IAK tail domain inhibits initial microtubule-stimulated ADP release
    • Hackney, D. D. and Stock, M. F. (2000) Kinesin's IAK tail domain inhibits initial microtubule-stimulated ADP release. Nat. Cell Biol. 2, 257-260
    • (2000) Nat. Cell Biol. , vol.2 , pp. 257-260
    • Hackney, D.D.1    Stock, M.F.2
  • 23
    • 0033193864 scopus 로고    scopus 로고
    • Kinesin's tail domain is an inhibitory regulator of the motor domain
    • Coy, D. L., Hancock, W. O., Wagenbach, M. and Howard, J. (1999) Kinesin's tail domain is an inhibitory regulator of the motor domain. Nat. Cell Biol. 1, 288-292
    • (1999) Nat. Cell Biol. , vol.1 , pp. 288-292
    • Coy, D.L.1    Hancock, W.O.2    Wagenbach, M.3    Howard, J.4
  • 25
    • 0347480274 scopus 로고    scopus 로고
    • Regulation of Kinl kinesin ATPase activity by binding to the microtubule lattice
    • Moores, C. A., Hekmat-Nejad, M., Sakowicz, R. and Milligan, R. A. (2003) Regulation of Kinl kinesin ATPase activity by binding to the microtubule lattice. J. Cell Biol. 163, 963-971
    • (2003) J. Cell Biol. , vol.163 , pp. 963-971
    • Moores, C.A.1    Hekmat-Nejad, M.2    Sakowicz, R.3    Milligan, R.A.4
  • 27
    • 0028887848 scopus 로고
    • Structural changes accompanying GTP hydrolysis in microtubules: Information from a slowly hydrolyzable analogue guanylyl-(α,β)- methylene-diphosphonate
    • Hyman, A. A., Chretien, D., Arnal, I. and Wade, R. H. (1995) Structural changes accompanying GTP hydrolysis in microtubules: information from a slowly hydrolyzable analogue guanylyl-(α,β)-methylene-diphosphonate. J. Cell Biol. 128, 117-125
    • (1995) J. Cell Biol. , vol.128 , pp. 117-125
    • Hyman, A.A.1    Chretien, D.2    Arnal, I.3    Wade, R.H.4
  • 28
    • 0030921846 scopus 로고    scopus 로고
    • Kinetochores distinguish GTP from GDP forms of the microtubule lattice
    • Severin, F. F., Sorger, P. K. and Hyman, A. A. (1997) Kinetochores distinguish GTP from GDP forms of the microtubule lattice. Nature (London) 388, 888-891
    • (1997) Nature (London) , vol.388 , pp. 888-891
    • Severin, F.F.1    Sorger, P.K.2    Hyman, A.A.3
  • 29
    • 0141750616 scopus 로고    scopus 로고
    • A structural analysis of the interaction between ncd tail and tubulin protofilaments
    • Wendt, T., Karabay, A., Krebs, A., Gross, H., Walker, R. and Hoenger, A. (2003) A structural analysis of the interaction between ncd tail and tubulin protofilaments. J. Mol. Biol. 333, 541-552
    • (2003) J. Mol. Biol. , vol.333 , pp. 541-552
    • Wendt, T.1    Karabay, A.2    Krebs, A.3    Gross, H.4    Walker, R.5    Hoenger, A.6
  • 30
    • 0041522803 scopus 로고    scopus 로고
    • Processivity of the single-headed kinesin KIF1A through biased binding to tubulin
    • Okada, Y., Higuchi, H. and Hirokawa, N. (2003) Processivity of the single-headed kinesin KIF1A through biased binding to tubulin. Nature (London) 424, 574-577
    • (2003) Nature (London) , vol.424 , pp. 574-577
    • Okada, Y.1    Higuchi, H.2    Hirokawa, N.3
  • 31
    • 0038709397 scopus 로고    scopus 로고
    • The microtubule plus-end proteins EB1 and dynactin have differential effects on microtubule polymerization
    • Ligon, L. A., Shelly, S. S., Tokito, M. and Holzbaur, E. L. (2003) The microtubule plus-end proteins EB1 and dynactin have differential effects on microtubule polymerization. Mol. Biol. Cell 14, 1405-1417
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1405-1417
    • Ligon, L.A.1    Shelly, S.S.2    Tokito, M.3    Holzbaur, E.L.4
  • 32
    • 0033582659 scopus 로고    scopus 로고
    • CLIP-170 highlights growing microtubule ends in vivo
    • Perez, F., Diamantopoulos, G. S., Stalder, R. and Kreis, T. E. (1999) CLIP-170 highlights growing microtubule ends in vivo. Cell 96, 517-527
    • (1999) Cell , vol.96 , pp. 517-527
    • Perez, F.1    Diamantopoulos, G.S.2    Stalder, R.3    Kreis, T.E.4
  • 33
    • 0041941573 scopus 로고    scopus 로고
    • An inner centromere protein that stimulates the microtubule depolymerizing activity of a Kinl kinesin
    • Ohi, R., Coughlin, M. L., Lane, W. S. and Mitchison, T. J. (2003) An inner centromere protein that stimulates the microtubule depolymerizing activity of a Kinl kinesin. Dev. Cell 5, 309-321
    • (2003) Dev. Cell , vol.5 , pp. 309-321
    • Ohi, R.1    Coughlin, M.L.2    Lane, W.S.3    Mitchison, T.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.