메뉴 건너뛰기




Volumn 25, Issue 24, 2006, Pages 5932-5941

Identification of a strong binding site for kinesin on the microtubule using mutant analysis of tubulin

Author keywords

Kinesin; Microtubule; Mutant analysis; Stall force; Yeast

Indexed keywords

ADENYLYLIMIDODIPHOSPHATE; ALANINE; BETA TUBULIN; KINESIN; MUTANT PROTEIN;

EID: 33845684194     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/sj.emboj.7601442     Document Type: Article
Times cited : (55)

References (51)
  • 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
    • 0032481381 scopus 로고    scopus 로고
    • Proteolytic mapping of kinesin/ncd-microtubule interface: Nucleotide dependent conformational changes in the loops L8 and L12
    • Alonso MC, Damme J, Vandekerckhove J, Cross RA (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    Damme, J.2    Vandekerckhove, J.3    Cross, R.A.4
  • 3
    • 0019845281 scopus 로고
    • Influence of the composition of commercial sodium dodecyl sulphate preparations on the separation of α- And β-tubulin during polyacrylamide gel electrophoresis
    • Best D, Warr PJ, Gull K (1981) Influence of the composition of commercial sodium dodecyl sulphate preparations on the separation of α- and β-tubulin during polyacrylamide gel electrophoresis. Anal Biochem 114: 281-284
    • (1981) Anal Biochem , vol.114 , pp. 281-284
    • Best, D.1    Warr, P.J.2    Gull, K.3
  • 4
    • 0025222347 scopus 로고
    • Bead movement by single kinesin molecules studied with optical tweezers
    • Block SM, Goldstein LSB, Schnapp BJ (1990) Bead movement by single kinesin molecules studied with optical tweezers. Nature 348: 348-352
    • (1990) Nature , vol.348 , pp. 348-352
    • Block, S.M.1    Goldstein, L.S.B.2    Schnapp, B.J.3
  • 5
    • 0037219233 scopus 로고    scopus 로고
    • The two alpha-tubulin isotypes in budding yeast have opposing effects on microtubule dynamics in vitro
    • Bode CJ, Gupta ML, Suprenant KA, Himes RH (2003) The two alpha-tubulin isotypes in budding yeast have opposing effects on microtubule dynamics in vitro. EMBO Rep 4: 94-99
    • (2003) EMBO Rep , vol.4 , pp. 94-99
    • Bode, C.J.1    Gupta, M.L.2    Suprenant, K.A.3    Himes, R.H.4
  • 6
    • 0024582786 scopus 로고
    • Dominant effects of tubulin overexpression in Saccharomyces cerevisiae
    • Burke D, Gasdaska P, Hartwell L (1989) Dominant effects of tubulin overexpression in Saccharomyces cerevisiae. Mol Cell Biol 9: 1049-1059
    • (1989) Mol Cell Biol , vol.9 , pp. 1049-1059
    • Burke, D.1    Gasdaska, P.2    Hartwell, L.3
  • 7
    • 19644377414 scopus 로고    scopus 로고
    • Mechanics of the kinesin step
    • Carter NJ, Cross RA (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
  • 8
    • 0027248960 scopus 로고
    • Purification and biochemical characterization of tubulin from the budding yeast Saccharomyces cerevisiae
    • Davis A, Sage CR, Wilson L, Farrell KW (1993) Purification and biochemical characterization of tubulin from the budding yeast Saccharomyces cerevisiae. Biochemistry 32: 8823-8835
    • (1993) Biochemistry , vol.32 , pp. 8823-8835
    • Davis, A.1    Sage, C.R.2    Wilson, L.3    Farrell, K.W.4
  • 9
    • 0002662180 scopus 로고
    • Measurement and magnitude of enzymatic rate constants
    • New York, USA: WH Freeman and Company Press
    • Fersht A (1984) Measurement and magnitude of enzymatic rate constants. In Enzyme Structure and Mechanism, pp 121-154. New York, USA: WH Freeman and Company Press
    • (1984) Enzyme Structure and Mechanism , pp. 121-154
    • Fersht, A.1
  • 10
    • 0034078008 scopus 로고    scopus 로고
    • Microtubule-based transport systems in neurons: The roles of kinesins and dyneins
    • Goldstein LS, Yang Z (2000) Microtubule-based transport systems in neurons: the roles of kinesins and dyneins. Annu Rev Neurosci 23: 39-71
    • (2000) Annu Rev Neurosci , vol.23 , pp. 39-71
    • Goldstein, L.S.1    Yang, Z.2
  • 11
    • 0037975662 scopus 로고    scopus 로고
    • Understanding tubulin-Taxol interactions: Mutations that impart Taxol binding to yeast tubulin
    • Gupta Jr ML, Bode CJ, Georg GI, Himes RH (2003) Understanding tubulin-Taxol interactions: mutations that impart Taxol binding to yeast tubulin. Proc Natl Acad Sci USA 100: 6394-6397
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6394-6397
    • Gupta Jr., M.L.1    Bode, C.J.2    Georg, G.I.3    Himes, R.H.4
  • 12
    • 0028200793 scopus 로고
    • Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis
    • Hackney DD (1994) Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis. Proc Natl Acad Sci USA 91: 6865-6869
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 6865-6869
    • Hackney, D.D.1
  • 13
    • 0028946849 scopus 로고
    • Implications of diffusion-controlled limit for processivity of dimeric kinesin head domains
    • Hackney DD (1995) Implications of diffusion-controlled limit for processivity of dimeric kinesin head domains. Biophys J 68: 267s-270s
    • (1995) Biophys J , vol.68
    • Hackney, D.D.1
  • 14
    • 0032559822 scopus 로고    scopus 로고
    • Processivity of the motor protein kinesin requires two heads
    • Hancock WO, 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
  • 15
    • 0025104145 scopus 로고
    • Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay
    • Harada Y, Sakurada K, Aoki T, Thomas DD, Yanagida T (1990) Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay. J Mol Biol 216: 49-68
    • (1990) J Mol Biol , vol.216 , pp. 49-68
    • Harada, Y.1    Sakurada, K.2    Aoki, T.3    Thomas, D.D.4    Yanagida, T.5
  • 18
    • 0024463944 scopus 로고
    • Movement of microtubules by single kinesin molecules
    • Howard J, Hudspeth AJ, Vale RD (1989) Movement of microtubules by single kinesin molecules. Nature 342: 154-158
    • (1989) Nature , vol.342 , pp. 154-158
    • Howard, J.1    Hudspeth, A.J.2    Vale, R.D.3
  • 19
    • 0030844286 scopus 로고    scopus 로고
    • Coupling of kinesin steps to ATP hydrolysis
    • Hua W, Young EC, Fleming ML, Gelles J (1997) Coupling of kinesin steps to ATP hydrolysis. Nature 388: 390-393
    • (1997) Nature , vol.388 , pp. 390-393
    • Hua, W.1    Young, E.C.2    Fleming, M.L.3    Gelles, J.4
  • 20
    • 0034765827 scopus 로고    scopus 로고
    • Motility of single one-headed kinesin molecule along microtubules
    • Inoue Y, Hikikoshi-Iwane A, Miyai T, Muto E, Yanagida T (2001) Motility of single one-headed kinesin molecule along microtubules. Biophys J 81: 2838-2850
    • (2001) Biophys J , vol.81 , pp. 2838-2850
    • Inoue, Y.1    Hikikoshi-Iwane, A.2    Miyai, T.3    Muto, E.4    Yanagida, T.5
  • 22
    • 0035951471 scopus 로고    scopus 로고
    • Nucleotide-dependent single to double-headed binding of kinesin
    • Kawaguchi K, Ishiwata S (2001) Nucleotide-dependent single to double-headed binding of kinesin. Science 291: 667-669
    • (2001) Science , vol.291 , pp. 667-669
    • Kawaguchi, K.1    Ishiwata, S.2
  • 23
    • 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
  • 25
    • 0030824684 scopus 로고    scopus 로고
    • Mechanics of single kinesin molecules measured by optical trapping nanometry
    • Kojima H, Muto E, Higuchi H, Yanagida T (1997) Mechanics of single kinesin molecules measured by optical trapping nanometry. Biophys J 73: 2012-2022
    • (1997) Biophys J , vol.73 , pp. 2012-2022
    • Kojima, H.1    Muto, E.2    Higuchi, H.3    Yanagida, T.4
  • 26
    • 27744552948 scopus 로고    scopus 로고
    • The E-hook of tubulin interacts with kinesin's head to increase processivity and speed
    • Lakämper S, Meyhöfer E (2005) The E-hook of tubulin interacts with kinesin's head to increase processivity and speed. Biophys J 89: 3223-3234
    • (2005) Biophys J , vol.89 , pp. 3223-3234
    • Lakämper, S.1    Meyhöfer, E.2
  • 27
    • 0024195951 scopus 로고
    • Comparative analysis of tubulin sequences
    • Little M, Seehaus T (1988) Comparative analysis of tubulin sequences. Comp Biochem Physiol 90B: 655-670
    • (1988) Comp Biochem Physiol , vol.90 B , pp. 655-670
    • Little, M.1    Seehaus, T.2
  • 28
    • 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
  • 29
    • 0030709242 scopus 로고    scopus 로고
    • Multiple forms of tubulin: Different gene products and covalent modifications
    • Luduena RF (1998) Multiple forms of tubulin: different gene products and covalent modifications. Int Rev Cytol 178: 207-275
    • (1998) Int Rev Cytol , vol.178 , pp. 207-275
    • Luduena, R.F.1
  • 30
    • 0031021473 scopus 로고    scopus 로고
    • Interacting head mechanism of microtubule-kinesin ATPase
    • Ma YZ, Taylor EW (1997) Interacting head mechanism of microtubule-kinesin ATPase. J Biol Chem 272: 724-730
    • (1997) J Biol Chem , vol.272 , pp. 724-730
    • Ma, Y.Z.1    Taylor, E.W.2
  • 32
    • 0036798857 scopus 로고    scopus 로고
    • Chemomechanical coupling of the forward and backward steps of single kinesin molecules
    • Nishiyama M, Higuchi H, Yanagida T (2002) Chemomechanical coupling of the forward and backward steps of single kinesin molecules. Nat Cell Biol 4: 790-797
    • (2002) Nat Cell Biol , vol.4 , pp. 790-797
    • Nishiyama, M.1    Higuchi, H.2    Yanagida, T.3
  • 33
    • 0029075829 scopus 로고
    • Unbinding force of a single motor molecule of muscle measured using optical tweezers
    • Nishizaka T, Miyata H, Yoshikawa H, Ishiwata S, Kinosita Jr K (1995) Unbinding force of a single motor molecule of muscle measured using optical tweezers. Nature 377: 251-254
    • (1995) Nature , vol.377 , pp. 251-254
    • Nishizaka, T.1    Miyata, H.2    Yoshikawa, H.3    Ishiwata, S.4    Kinosita Jr., K.5
  • 34
    • 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
  • 35
    • 1342296567 scopus 로고    scopus 로고
    • A common mechanism for microtubule destabilizers - M type kinesins stabilize curling of the protofilament using the class-specific neck loops
    • Ogawa T, Nitta R, Okada Y, Hirokawa N (2004) A common mechanism for microtubule destabilizers - M type kinesins stabilize curling of the protofilament using the class-specific neck loops. Cell 116: 591-602
    • (2004) Cell , vol.116 , pp. 591-602
    • Ogawa, T.1    Nitta, R.2    Okada, Y.3    Hirokawa, N.4
  • 36
    • 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 (2000) 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: 640-645
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 640-645
    • Okada, Y.1    Hirokawa, N.2
  • 38
    • 0842277818 scopus 로고    scopus 로고
    • Inhibition of kinesin motility by ADP and phosphate supports a hand-over-hand mechanism
    • Schief WR, Clark RH, Crevenna AH, Howard J (2004) Inhibition of kinesin motility by ADP and phosphate supports a hand-over-hand mechanism. Proc Natl Acad Sci USA 101: 1183-1188
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 1183-1188
    • Schief, W.R.1    Clark, R.H.2    Crevenna, A.H.3    Howard, J.4
  • 39
    • 0030744142 scopus 로고    scopus 로고
    • Kinesin hydrolyses one ATP per 8-nm step
    • Schnitzer MJ, Block SM (1997) Kinesin hydrolyses one ATP per 8-nm step. Nature 388: 386-390
    • (1997) Nature , vol.388 , pp. 386-390
    • Schnitzer, M.J.1    Block, S.M.2
  • 40
    • 33744467383 scopus 로고    scopus 로고
    • On the hand-over-hand mechanism of kinesin
    • Shao Q, Gao YQ (2006) On the hand-over-hand mechanism of kinesin. Proc Natl Acad Sci USA 103: 8072-8077
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 8072-8077
    • Shao, Q.1    Gao, Y.Q.2
  • 43
    • 0034995132 scopus 로고    scopus 로고
    • ADP-induced rocking of the kinesin motor domain revealed by single-molecule fluorescence polarization microscopy
    • Sosa H, Peterman EJG, Moerner WE, Goldstein LSB (2001) ADP-induced rocking of the kinesin motor domain revealed by single-molecule fluorescence polarization microscopy. Nat Struct Biol 8: 540-544
    • (2001) Nat Struct Biol , vol.8 , pp. 540-544
    • Sosa, H.1    Peterman, E.J.G.2    Moerner, W.E.3    Goldstein, L.S.B.4
  • 44
    • 0032541102 scopus 로고    scopus 로고
    • Visualization of the GDP-dependent switching in the growth polarity of microtubules
    • Tanaka-Takiguchi Y, Itoh TJ, Hotani H (1998) Visualization of the GDP-dependent switching in the growth polarity of microtubules. J Mol Biol 280: 365-373
    • (1998) J Mol Biol , vol.280 , pp. 365-373
    • Tanaka-Takiguchi, Y.1    Itoh, T.J.2    Hotani, H.3
  • 45
    • 0034722373 scopus 로고    scopus 로고
    • Engineering the processive run length of the kinesin motor
    • Thorn KS, Ubersax JA, Vale RD (2000) Engineering the processive run length of the kinesin motor. J Cell Biol 151: 1093-1100
    • (2000) J Cell Biol , vol.151 , pp. 1093-1100
    • Thorn, K.S.1    Ubersax, J.A.2    Vale, R.D.3
  • 46
    • 0037390461 scopus 로고    scopus 로고
    • Loading direction regulates the affinity of ADP for kinesin
    • Uemura S, Ishiwata S (2003) Loading direction regulates the affinity of ADP for kinesin. Nat Struct Biol 10: 308-311
    • (2003) Nat Struct Biol , vol.10 , pp. 308-311
    • Uemura, S.1    Ishiwata, S.2
  • 48
    • 0030029076 scopus 로고    scopus 로고
    • Motors involved in spindle assembly and chromosome segregation
    • Vernos I, Karsenti E (1996) Motors involved in spindle assembly and chromosome segregation. Curr Opin Cell Biol 8: 4-9
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 4-9
    • Vernos, I.1    Karsenti, E.2
  • 49
    • 0033536183 scopus 로고    scopus 로고
    • Single kinesin molecules studied with a molecular force clamp
    • Visscher K, Schnitzer MJ, Block SM (1999) Single kinesin molecules studied with a molecular force clamp. Nature 400: 184-189
    • (1999) Nature , vol.400 , pp. 184-189
    • Visscher, K.1    Schnitzer, M.J.2    Block, S.M.3
  • 50
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.