메뉴 건너뛰기




Volumn 20, Issue 8, 2013, Pages 1001-1007

Structure of a kinesin-tubulin complex and implications for kinesin motility

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ALPHA TUBULIN; BETA TUBULIN; KINESIN; NUCLEOTIDE;

EID: 84881396280     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2624     Document Type: Article
Times cited : (124)

References (47)
  • 1
    • 70349437416 scopus 로고    scopus 로고
    • Kinesin superfamily motor proteins and intracellular transport
    • Hirokawa, N., Noda, Y., Tanaka, Y. & Niwa, S. Kinesin superfamily motor proteins and intracellular transport. Nat. Rev. Mol. Cell Biol. 10, 682-696 (2009).
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 682-696
    • Hirokawa, N.1    Noda, Y.2    Tanaka, Y.3    Niwa, S.4
  • 2
    • 77949540170 scopus 로고    scopus 로고
    • How kinesin motor proteins drive mitotic spindle function: Lessons from molecular assays
    • Wordeman, L. How kinesin motor proteins drive mitotic spindle function: lessons from molecular assays. Semin. Cell Dev. Biol. 21, 260-268 (2010).
    • (2010) Semin. Cell Dev. Biol. , vol.21 , pp. 260-268
    • Wordeman, L.1
  • 5
    • 0033576727 scopus 로고    scopus 로고
    • A structural change in the kinesin motor protein that drives motility
    • Rice, S. et al. A structural change in the kinesin motor protein that drives motility. Nature 402, 778-784 (1999).
    • (1999) Nature , vol.402 , pp. 778-784
    • Rice, S.1
  • 7
    • 33748421625 scopus 로고    scopus 로고
    • Large Conformational Changes in a Kinesin Motor Catalyzed by Interaction with Microtubules
    • DOI 10.1016/j.molcel.2006.07.020, PII S109727650600517X
    • Hirose, K., Akimaru, E., Akiba, T., Endow, S.A. & Amos, L.A. Large conformational changes in a kinesin motor catalyzed by interaction with microtubules. Mol. Cell 23, 913-923 (2006). (Pubitemid 44344516)
    • (2006) Molecular Cell , vol.23 , Issue.6 , pp. 913-923
    • Hirose, K.1    Akimaru, E.2    Akiba, T.3    Endow, S.A.4    Amos, L.A.5
  • 8
    • 33748931452 scopus 로고    scopus 로고
    • High-resolution cryo-EM maps show the nucleotide binding pocket of KIF1A in open and closed conformations
    • DOI 10.1038/sj.emboj.7601299, PII 7601299
    • Kikkawa, M. & Hirokawa, N. High-resolution cryo-EM maps show the nucleotide binding pocket of KIF1A in open and closed conformations. EMBO J. 25, 4187-4194 (2006). (Pubitemid 44435216)
    • (2006) EMBO Journal , vol.25 , Issue.18 , pp. 4187-4194
    • Kikkawa, M.1    Hirokawa, N.2
  • 9
    • 77749239756 scopus 로고    scopus 로고
    • An atomic-level mechanism for activation of the kinesin molecular motors
    • Sindelar, C.V. & Downing, K.H. An atomic-level mechanism for activation of the kinesin molecular motors. Proc. Natl. Acad. Sci. USA 107, 4111-4116 (2010).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 4111-4116
    • Sindelar, C.V.1    Downing, K.H.2
  • 10
    • 0031022509 scopus 로고    scopus 로고
    • Kinetic mechanism of a monomeric kinesin construct
    • DOI 10.1074/jbc.272.2.717
    • Ma, Y.Z. & Taylor, E.W. Kinetic mechanism of a monomeric kinesin construct. J. Biol. Chem. 272, 717-723 (1997). (Pubitemid 27034555)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.2 , pp. 717-723
    • Ma, Y.-Z.1    Taylor, E.W.2
  • 13
    • 0025362646 scopus 로고
    • Evidence that the head of kinesin is suffcient for force generation and motility in vitro
    • Yang, J.T., Saxton, W.M., Stewart, R.J., Raff, E.C. & Goldstein, L.S. Evidence that the head of kinesin is suffcient for force generation and motility in vitro. Science 249, 42-47 (1990).
    • (1990) Science , vol.249 , pp. 42-47
    • Yang, J.T.1    Saxton, W.M.2    Stewart, R.J.3    Raff, E.C.4    Goldstein, L.S.5
  • 14
    • 34147188510 scopus 로고    scopus 로고
    • An ATP gate controls tubulin binding by the tethered head of kinesin-1
    • DOI 10.1126/science.1136985
    • Alonso, M.C. et al. An ATP gate controls tubulin binding by the tethered head of kinesin-1. Science 316, 120-123 (2007). (Pubitemid 46559532)
    • (2007) Science , vol.316 , Issue.5821 , pp. 120-123
    • Alonso, M.C.1    Drummond, D.R.2    Kain, S.3    Hoeng, J.4    Amos, L.5    Cross, R.A.6
  • 15
    • 0031042321 scopus 로고    scopus 로고
    • The structure of microtubule-motor complexes
    • DOI 10.1016/S0955-0674(97)80145-7
    • Amos, L.A. & Hirose, K. The structure of microtubule-motor complexes. Curr. Opin. Cell Biol. 9, 4-11 (1997). (Pubitemid 27065102)
    • (1997) Current Opinion in Cell Biology , vol.9 , Issue.1 , pp. 4-11
    • Amos, L.A.1    Hirose, K.2
  • 16
    • 84866119981 scopus 로고    scopus 로고
    • Design and characterization of modular scaffolds for tubulin assembly
    • Mignot, I. et al. Design and characterization of modular scaffolds for tubulin assembly. J. Biol. Chem. 287, 31085-31094 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 31085-31094
    • Mignot, I.1
  • 17
    • 84864343828 scopus 로고    scopus 로고
    • A designed ankyrin repeat protein selected to bind to tubulin caps the microtubule plus end
    • Pecqueur, L. et al. A designed ankyrin repeat protein selected to bind to tubulin caps the microtubule plus end. Proc. Natl. Acad. Sci. USA 109, 12011-12016 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 12011-12016
    • Pecqueur, L.1
  • 18
    • 0033534629 scopus 로고    scopus 로고
    • High-resolution model of the microtubule
    • DOI 10.1016/S0092-8674(00)80961-7
    • Nogales, E., Whittaker, M., Milligan, R.A. & Downing, K.H. High-resolution model of the microtubule. Cell 96, 79-88 (1999). (Pubitemid 29044155)
    • (1999) Cell , vol.96 , Issue.1 , pp. 79-88
    • Nogales, E.1    Whittaker, M.2    Milligan, R.A.3    Downing, K.H.4
  • 19
  • 20
    • 0033563154 scopus 로고    scopus 로고
    • Motor proteins of the kinesin family. Structures, variations, and nucleotide binding sites
    • DOI 10.1046/j.1432-1327.1999.00341.x
    • Sack, S., Kull, F.J. & Mandelkow, E. Motor proteins of the kinesin family: structures, variations, and nucleotide binding sites. Eur. J. Biochem. 262, 1-11 (1999). (Pubitemid 29242602)
    • (1999) European Journal of Biochemistry , vol.262 , Issue.1 , pp. 1-11
    • Sack, S.1    Kull, F.J.2    Mandelkow, E.3
  • 21
    • 34247237308 scopus 로고    scopus 로고
    • Multivariate Analysis of Conserved Sequence-Structure Relationships in Kinesins: Coupling of the Active Site and a Tubulin-binding Sub-domain
    • DOI 10.1016/j.jmb.2007.02.049, PII S0022283607002306
    • Grant, B.J., McCammon, J.A., Caves, L.S. & Cross, R.A. Multivariate analysis of conserved sequence-structure relationships in kinesins: coupling of the active site and a tubulin-binding sub-domain. J. Mol. Biol. 368, 1231-1248 (2007). (Pubitemid 46617587)
    • (2007) Journal of Molecular Biology , vol.368 , Issue.5 , pp. 1231-1248
    • Grant, B.J.1    McCammon, J.A.2    Caves, L.S.D.3    Cross, R.A.4
  • 22
    • 84877698868 scopus 로고    scopus 로고
    • Structural basis for the ATP-induced isomerization of kinesin
    • Chang, Q., Nitta, R., Inoue, S. & Hirokawa, N. Structural basis for the ATP-induced isomerization of kinesin. J. Mol. Biol. 425, 1869-1880 (2013).
    • (2013) J. Mol. Biol. , vol.425 , pp. 1869-1880
    • Chang, Q.1    Nitta, R.2    Inoue, S.3    Hirokawa, N.4
  • 24
    • 77949318844 scopus 로고    scopus 로고
    • ATP hydrolysis in Eg5 kinesin involves a catalytic two-water mechanism
    • Parke, CL., Wojcik, E.J., Kim, S. & Worthylake, D.K. ATP hydrolysis in Eg5 kinesin involves a catalytic two-water mechanism. J. Biol. Chem. 285, 5859-5867 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 5859-5867
    • Parke, C.L.1    Wojcik, E.J.2    Kim, S.3    Worthylake, D.K.4
  • 26
    • 0029989974 scopus 로고    scopus 로고
    • Crystal structure of the kinesin motor domain reveals a structural similarity to myosin
    • DOI 10.1038/380550a0
    • Kull, F.J., Sablin, E.P., Lau, R., Fletterick, R.J. & Vale, R.D. Crystal structure of the kinesin motor domain reveals a structural similarity to myosin. Nature 380, 550-555 (1996). (Pubitemid 26110647)
    • (1996) Nature , vol.380 , Issue.6574 , pp. 550-555
    • Kull, F.J.1    Sablin, E.P.2    Lau, R.3    Fletterick, R.J.4    Vale, R.D.5
  • 27
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • DOI 10.1006/jmbi.2001.5378
    • Leipe, D.D., Wolf, Y.I., Koonin, E.V. & Aravind, L. Classifcation and evolution of P-loop GTPases and related ATPases. J. Mol. Biol. 317, 41-72 (2002). (Pubitemid 34722199)
    • (2002) Journal of Molecular Biology , vol.317 , Issue.1 , pp. 41-72
    • Leipe, D.D.1    Wolf, Y.I.2    Koonin, E.V.3    Aravind, L.4
  • 29
    • 84870768560 scopus 로고    scopus 로고
    • An inherited TUBB2B mutation alters a kinesin-binding site and causes polymicrogyria, CFEOM and axon dysinnervation
    • Cederquist, G.Y. et al. An inherited TUBB2B mutation alters a kinesin-binding site and causes polymicrogyria, CFEOM and axon dysinnervation. Hum. Mol. Genet. 21, 5484-5499 (2012).
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 5484-5499
    • Cederquist, G.Y.1
  • 30
    • 73349096922 scopus 로고    scopus 로고
    • Human TUBB3 mutations perturb microtubule dynamics, kinesin interactions, and axon guidance
    • Tischfeld, M.A. et al. Human TUBB3 mutations perturb microtubule dynamics, kinesin interactions, and axon guidance. Cell 140, 74-87 (2010).
    • (2010) Cell , vol.140 , pp. 74-87
    • Tischfeld, M.A.1
  • 31
    • 3242776257 scopus 로고    scopus 로고
    • The kinetic mechanism of kinesin
    • DOI 10.1016/j.tibs.2004.04.010, PII S0968000404001033
    • Cross, R.A. The kinetic mechanism of kinesin. Trends Biochem. Sci. 29, 301-309 (2004). (Pubitemid 38968762)
    • (2004) Trends in Biochemical Sciences , vol.29 , Issue.6 , pp. 301-309
    • Cross, R.A.1
  • 32
    • 1542353988 scopus 로고
    • Kinesin ATPase: Rate-limiting ADP release
    • Hackney, D.D. Kinesin ATPase: rate-limiting ADP release. Proc. Natl. Acad. Sci. USA 85, 6314-6318 (1988).
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 6314-6318
    • Hackney, D.D.1
  • 33
    • 0141732282 scopus 로고    scopus 로고
    • A structural state of the myosin v motor without bound nucleotide
    • Coureux, P.D. et al. A structural state of the myosin V motor without bound nucleotide. Nature 425, 419-423 (2003).
    • (2003) Nature , vol.425 , pp. 419-423
    • Coureux, P.D.1
  • 35
    • 0035834521 scopus 로고    scopus 로고
    • Refined structure of αβ-tubulin at 3.5 Å resolution
    • DOI 10.1006/jmbi.2001.5077
    • Löwe, J., Li, H., Downing, K.H. & Nogales, E. Refned structure of aß-tubulin at 3.5 Å resolution. J. Mol. Biol. 313, 1045-1057 (2001). (Pubitemid 33081900)
    • (2001) Journal of Molecular Biology , vol.313 , Issue.5 , pp. 1045-1057
    • Lowe, J.1    Li, H.2    Downing, K.H.3    Nogales, E.4
  • 36
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera: A visualization system for exploratory research and analysis
    • Pettersen, E.F. et al. UCSF Chimera: a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 37
    • 0345393105 scopus 로고    scopus 로고
    • Purification of brain tubulin through two cycles of polymerization- depolymerization in a high-molarity buffer
    • DOI 10.1016/S1046-5928(03)00218-3
    • Castoldi, M. & Popov, A.V. Purifcation of brain tubulin through two cycles of polymerization-depolymerization in a high-molarity buffer. Protein Expr. Purif. 32, 83-88 (2003). (Pubitemid 37436140)
    • (2003) Protein Expression and Purification , vol.32 , Issue.1 , pp. 83-88
    • Castoldi, M.1    Popov, A.V.2
  • 39
    • 77955379085 scopus 로고    scopus 로고
    • Kinesin's light chains inhibit the head-and microtubule-binding activity of its tail
    • Wong, Y.L. & Rice, S.E. Kinesin's light chains inhibit the head-and microtubule-binding activity of its tail. Proc. Natl. Acad. Sci. USA 107, 11781-11786 (2010).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 11781-11786
    • Wong, Y.L.1    Rice, S.E.2
  • 40
    • 84860357530 scopus 로고    scopus 로고
    • Kif2C minimal functional domain has unusual nucleotide binding properties that are adapted to microtubule depolymerization
    • Wang, W. et al. Kif2C minimal functional domain has unusual nucleotide binding properties that are adapted to microtubule depolymerization. J. Biol. Chem. 287, 15143-15153 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 15143-15153
    • Wang, W.1
  • 43
    • 76449106188 scopus 로고    scopus 로고
    • Integration scaling, space-group assignment and post-refnement
    • Kabsch, W. Integration, scaling, space-group assignment and post-refnement. Acta Crystallogr. D Biol. Crystallogr. 66, 133-144 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 133-144
    • Kabsch, W.1
  • 44
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A 50, 157-163 (1994).
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 45
    • 84860390007 scopus 로고    scopus 로고
    • The determinants that govern microtubule assembly from the atomic structure of GTP-tubulin
    • Nawrotek, A., Knossow, M. & Gigant, B. The determinants that govern microtubule assembly from the atomic structure of GTP-tubulin. J. Mol. Biol. 412, 35-42 (2011).
    • (2011) J. Mol. Biol. , vol.412 , pp. 35-42
    • Nawrotek, A.1    Knossow, M.2    Gigant, B.3
  • 47
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • Chen, V.B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D Biol. Crystallogr. 66, 12-21 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 12-21
    • Chen, V.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.