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Volumn 116, Issue 4, 2004, Pages 591-602

A Common Mechanism for Microtubule Destabilizers - M Type Kinesins Stabilize Curling of the Protofilament Using the Class-Specific Neck and Loops

Author keywords

[No Author keywords available]

Indexed keywords

KINESIN; PROTEIN KIF2C; PROTEIN SUBUNIT; TUBULIN; UNCLASSIFIED DRUG;

EID: 1342296567     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(04)00129-1     Document Type: Article
Times cited : (169)

References (42)
  • 3
    • 0030874883 scopus 로고    scopus 로고
    • The directional preference of kinesin motors is specified by an element outside of the motor catalytic domain
    • Case R.B., Pierce D.W., Hom Booher N., Hart C.L., Vale R.D. The directional preference of kinesin motors is specified by an element outside of the motor catalytic domain. Cell. 90:1997;959-966.
    • (1997) Cell , vol.90 , pp. 959-966
    • Case, R.B.1    Pierce, D.W.2    Hom Booher, N.3    Hart, C.L.4    Vale, R.D.5
  • 5
    • 0033534575 scopus 로고    scopus 로고
    • Kin I kinesins are microtubule-destabilizing enzymes
    • Desai A., Verma S., Mitchison T.J., Walczak C.E. Kin I kinesins are microtubule-destabilizing enzymes. Cell. 96:1999;69-78.
    • (1999) Cell , vol.96 , pp. 69-78
    • Desai, A.1    Verma, S.2    Mitchison, T.J.3    Walczak, C.E.4
  • 6
    • 0028245510 scopus 로고
    • Yeast Kar3 is a minus-end microtubule motor protein that destabilizes microtubules preferentially at the minus ends
    • Endow S.A., Kang S.J., Satterwhite L.L., Rose M.D., Skeen V.P., Salmon E.D. Yeast Kar3 is a minus-end microtubule motor protein that destabilizes microtubules preferentially at the minus ends. EMBO J. 13:1994;2708-2713.
    • (1994) EMBO J. , vol.13 , pp. 2708-2713
    • Endow, S.A.1    Kang, S.J.2    Satterwhite, L.L.3    Rose, M.D.4    Skeen, V.P.5    Salmon, E.D.6
  • 7
    • 0034710696 scopus 로고    scopus 로고
    • A mutant of the motor protein kinesin that moves in both directions on microtubules
    • Endow S.A., Higuchi H. A mutant of the motor protein kinesin that moves in both directions on microtubules. Nature. 406:2000;913-916.
    • (2000) Nature , vol.406 , pp. 913-916
    • Endow, S.A.1    Higuchi, H.2
  • 9
    • 0030924142 scopus 로고    scopus 로고
    • Reversal in the direction of movement of a molecular motor
    • Henningsen U., Schliwa M. Reversal in the direction of movement of a molecular motor. Nature. 389:1997;93-96.
    • (1997) Nature , vol.389 , pp. 93-96
    • Henningsen, U.1    Schliwa, M.2
  • 10
    • 0030028366 scopus 로고    scopus 로고
    • Organelle transport along microtubule - The role of KIFs (kinesin superfamily proteins)
    • Hirokawa N. Organelle transport along microtubule - the role of KIFs (kinesin superfamily proteins). Trends Cell Biol. 132:1996;667-679.
    • (1996) Trends Cell Biol. , vol.132 , pp. 667-679
    • Hirokawa, N.1
  • 11
    • 0032559260 scopus 로고    scopus 로고
    • Kinesin and dynein superfamily proteins and the mechanism of organelle transport
    • Hirokawa N. Kinesin and dynein superfamily proteins and the mechanism of organelle transport. Science. 279:1998;519-526.
    • (1998) Science , vol.279 , pp. 519-526
    • Hirokawa, N.1
  • 12
    • 0032005975 scopus 로고    scopus 로고
    • Kinesin and dynein superfamily proteins in organelle transport and cell division
    • Hirokawa N., Noda Y., Okada Y. Kinesin and dynein superfamily proteins in organelle transport and cell division. Curr. Opin. Cell. Biol. 10:1998;60-73.
    • (1998) Curr. Opin. Cell. Biol. , vol.10 , pp. 60-73
    • Hirokawa, N.1    Noda, Y.2    Okada, Y.3
  • 13
    • 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., Hirokawa N. Kinesin superfamily protein 2A (KIF2A) functions in suppression of collateral branch extension. Cell. 114:2003;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
  • 14
    • 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., Howard J. The kinesin-related protein MCAK is a microtubule depolymerase that forms an ATP-hydrolyzing complex at microtubule ends. Mol. Cell. 11:2003;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
  • 16
    • 0031004867 scopus 로고    scopus 로고
    • Influence of the kinesin neck domain on dimerization and ATPase kinetics
    • Jiang W., Stock M.F., Li X., Hackney D.D. Influence of the kinesin neck domain on dimerization and ATPase kinetics. J. Biol. Chem. 272:1997;7626-7632.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7626-7632
    • Jiang, W.1    Stock, M.F.2    Li, X.3    Hackney, D.D.4
  • 18
    • 0033693656 scopus 로고    scopus 로고
    • A kinesin family tree
    • Kim A.J., Endow S.A. A kinesin family tree. J. Cell Sci. 113:2000;3681-3682.
    • (2000) J. Cell Sci. , vol.113 , pp. 3681-3682
    • Kim, A.J.1    Endow, S.A.2
  • 19
    • 0035860717 scopus 로고    scopus 로고
    • Molecular dissection of the microtubule depolymerizing activity of mitotic centromere-associated kinesin
    • Maney T., Wagenbach M., Wordeman L. Molecular dissection of the microtubule depolymerizing activity of mitotic centromere-associated kinesin. J. Biol. Chem. 276:2001;34753-34758.
    • (2001) J. Biol. Chem. , vol.276 , pp. 34753-34758
    • Maney, T.1    Wagenbach, M.2    Wordeman, L.3
  • 21
    • 0037673498 scopus 로고    scopus 로고
    • Kinesin superfamily proteins (KIFs) in the mouse transcriptome
    • Miki H., Setou M., Hirokawa N., Group R.I.K.E.N.G.E.R., Members G.S.L. Kinesin superfamily proteins (KIFs) in the mouse transcriptome. Genome Res. 13:2003;1455-1465.
    • (2003) Genome Res. , vol.13 , pp. 1455-1465
    • Miki, H.1    Setou, M.2    Hirokawa, N.3
  • 23
    • 0347480274 scopus 로고    scopus 로고
    • Regulation of KinI kinesin ATPase activity by binding to the microtubule lattice
    • Moores C.A., Hekmat-Nejad M., Sakowicz R., Milligan R.A. Regulation of KinI kinesin ATPase activity by binding to the microtubule lattice. J. Cell Biol. 163:2003;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
  • 24
    • 0032584067 scopus 로고    scopus 로고
    • Structural changes at microtubule ends accompanying GTP hydrolysis: Information from a slowly hydrolyzable analogue of GTP, guanylyl (alpha,beta)methylenediphosphonate
    • Muller Reichert T., Chretien D., Severin F., Hyman A.A. Structural changes at microtubule ends accompanying GTP hydrolysis. information from a slowly hydrolyzable analogue of GTP, guanylyl (alpha,beta) methylenediphosphonate Proc. Natl. Acad. Sci. USA. 95:1998;3661-3666.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3661-3666
    • Muller Reichert, T.1    Chretien, D.2    Severin, F.3    Hyman, A.A.4
  • 26
    • 0028948491 scopus 로고
    • KIF2 is a new microtubule-based anterograde motor that transports membranous organelles distinct from those carried by kinesin heavy chain or KIF3A/B
    • Noda Y., Sato Yoshitake R., Kondo S., Nangaku M., Hirokawa N. KIF2 is a new microtubule-based anterograde motor that transports membranous organelles distinct from those carried by kinesin heavy chain or KIF3A/B. J. Cell Biol. 129:1995;157-167.
    • (1995) J. Cell Biol. , vol.129 , pp. 157-167
    • Noda, Y.1    Sato Yoshitake, R.2    Kondo, S.3    Nangaku, M.4    Hirokawa, N.5
  • 27
    • 0034681137 scopus 로고    scopus 로고
    • Mechanism of the single-headed processivity: Diffusional anchoring between the K-loop of kinesin and the C terminus of tubulin
    • Okada Y., Hirokawa N. Mechanism of the single-headed processivity. diffusional anchoring between the K-loop of kinesin and the C terminus of tubulin Proc. Natl. Acad. Sci. USA. 97:2000;640-645.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 640-645
    • Okada, Y.1    Hirokawa, N.2
  • 28
    • 0041522803 scopus 로고    scopus 로고
    • Processivity of the single-headed kinesin KIF1A through biased binding to tubulin
    • Okada Y., Higuchi H., Hirokawa N. Processivity of the single-headed kinesin KIF1A through biased binding to tubulin. Nature. 424:2003;574-577.
    • (2003) Nature , vol.424 , pp. 574-577
    • Okada, Y.1    Higuchi, H.2    Hirokawa, N.3
  • 29
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 30
    • 0037175396 scopus 로고    scopus 로고
    • K-loop insertion restores microtubule depolymerizing activity of a "neckless" MCAK mutant
    • Ovechkina Y., Wagenbach M., Wordeman L. K-loop insertion restores microtubule depolymerizing activity of a "neckless" MCAK mutant. J. Cell Biol. 159:2002;557-562.
    • (2002) J. Cell Biol. , vol.159 , pp. 557-562
    • Ovechkina, Y.1    Wagenbach, M.2    Wordeman, L.3
  • 33
    • 0030939131 scopus 로고    scopus 로고
    • KIFC2 is a novel neuron-specific C-terminal type kinesin superfamily motor for dendritic transport of multivesicular body-like organelles
    • Saito N., Okada Y., Noda Y., Kinoshita Y., Kondo S., Hirokawa N. KIFC2 is a novel neuron-specific C-terminal type kinesin superfamily motor for dendritic transport of multivesicular body-like organelles. Neuron. 18:1997;425-438.
    • (1997) Neuron , vol.18 , pp. 425-438
    • Saito, N.1    Okada, Y.2    Noda, Y.3    Kinoshita, Y.4    Kondo, S.5    Hirokawa, N.6
  • 35
    • 0027102583 scopus 로고
    • Increased microtubule stability and alpha tubulin acetylation in cells transfected with microtubule-associated proteins MAP1B, MAP2 or tau
    • Takemura R., Okabe S., Umeyama T., Kanai Y., Cowan N.J., Hirokawa N. Increased microtubule stability and alpha tubulin acetylation in cells transfected with microtubule-associated proteins MAP1B, MAP2 or tau. J. Cell Sci. 103:1992;953-964.
    • (1992) J. Cell Sci. , vol.103 , pp. 953-964
    • Takemura, R.1    Okabe, S.2    Umeyama, T.3    Kanai, Y.4    Cowan, N.J.5    Hirokawa, N.6
  • 37
    • 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., Desai A. XKCM1. a xenopus kinesin-related protein that regulates microtubule dynamics during mitotic spindle assembly Cell. 84:1996;37-47.
    • (1996) Cell , vol.84 , pp. 37-47
    • Walczak, C.E.1    Mitchison, T.J.2    Desai, A.3
  • 40
    • 0028887847 scopus 로고
    • Identification and partial characterization of mitotic centromere-associated kinesin, a kinesin-related protein that associates with centromeres during mitosis
    • Wordeman L., Mitchison T.J. Identification and partial characterization of mitotic centromere-associated kinesin, a kinesin-related protein that associates with centromeres during mitosis. J. Cell Biol. 128:1995;95-104.
    • (1995) J. Cell Biol. , vol.128 , pp. 95-104
    • Wordeman, L.1    Mitchison, T.J.2
  • 41
    • 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., Endow S.A. A structural pathway for activation of the kinesin motor ATPase. EMBO J. 20:2001;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
  • 42
    • 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., Endow S.A. Rotation of the stalk/neck and one head in a new crystal structure of the kinesin motor protein, Ncd. EMBO J. 22:2003;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.