메뉴 건너뛰기




Volumn 136, Issue 1, 2009, Pages 110-122

ATPase Cycle of the Nonmotile Kinesin NOD Allows Microtubule End Tracking and Drives Chromosome Movement

Author keywords

CELLBIO

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; KINESIN; KINESIN 10; NOD PROTEIN; NUCLEOTIDE; UNCLASSIFIED DRUG;

EID: 58149098730     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2008.11.048     Document Type: Article
Times cited : (53)

References (49)
  • 1
    • 0028969659 scopus 로고
    • DNA binding and meiotic chromosomal localization of the Drosophila nod kinesin-like protein
    • Afshar K., Barton N.R., Hawley R.S., and Goldstein L.S. DNA binding and meiotic chromosomal localization of the Drosophila nod kinesin-like protein. Cell 81 (1995) 129-138
    • (1995) Cell , vol.81 , pp. 129-138
    • Afshar, K.1    Barton, N.R.2    Hawley, R.S.3    Goldstein, L.S.4
  • 2
    • 0028098798 scopus 로고
    • Direct, real-time measurement of rapid inorganic phosphate release using a novel fluorescent probe and its application to actomyosin subfragment 1 ATPase
    • Brune M., Hunter J.L., Corrie J.E., and Webb M.R. Direct, real-time measurement of rapid inorganic phosphate release using a novel fluorescent probe and its application to actomyosin subfragment 1 ATPase. Biochemistry 33 (1994) 8262-8271
    • (1994) Biochemistry , vol.33 , pp. 8262-8271
    • Brune, M.1    Hunter, J.L.2    Corrie, J.E.3    Webb, M.R.4
  • 4
    • 0015833833 scopus 로고
    • A meiotic mutant defective in distributive disjunction in Drosophila melanogaster
    • Carpenter A.T. A meiotic mutant defective in distributive disjunction in Drosophila melanogaster. Genetics 73 (1973) 393-428
    • (1973) Genetics , vol.73 , pp. 393-428
    • Carpenter, A.T.1
  • 5
    • 22844437213 scopus 로고    scopus 로고
    • The roles of MAD1, MAD2 and MAD3 in meiotic progression and the segregation of nonexchange chromosomes
    • Cheslock P.S., Kemp B.J., Boumil R.M., and Dawson D.S. The roles of MAD1, MAD2 and MAD3 in meiotic progression and the segregation of nonexchange chromosomes. Nat. Genet. 37 (2005) 756-760
    • (2005) Nat. Genet. , vol.37 , pp. 756-760
    • Cheslock, P.S.1    Kemp, B.J.2    Boumil, R.M.3    Dawson, D.S.4
  • 6
    • 29244476067 scopus 로고    scopus 로고
    • ATPase mechanism of Eg5 in the absence of microtubules: insight into microtubule activation and allosteric inhibition by monastrol
    • Cochran J.C., and Gilbert S.P. ATPase mechanism of Eg5 in the absence of microtubules: insight into microtubule activation and allosteric inhibition by monastrol. Biochemistry 44 (2005) 16633-16648
    • (2005) Biochemistry , vol.44 , pp. 16633-16648
    • Cochran, J.C.1    Gilbert, S.P.2
  • 9
    • 33749507219 scopus 로고    scopus 로고
    • Pathway of ATP hydrolysis by monomeric Kinesin eg5
    • Cochran J.C., Krzysiak T.C., and Gilbert S.P. Pathway of ATP hydrolysis by monomeric Kinesin eg5. Biochemistry 45 (2006) 12334-12344
    • (2006) Biochemistry , vol.45 , pp. 12334-12344
    • Cochran, J.C.1    Krzysiak, T.C.2    Gilbert, S.P.3
  • 10
    • 27644522292 scopus 로고    scopus 로고
    • The HhH2/NDD domain of the Drosophila Nod chromokinesin-like protein is required for binding to chromosomes in the oocyte nucleus
    • Cui W., and Hawley R.S. The HhH2/NDD domain of the Drosophila Nod chromokinesin-like protein is required for binding to chromosomes in the oocyte nucleus. Genetics 171 (2005) 1823-1835
    • (2005) Genetics , vol.171 , pp. 1823-1835
    • Cui, W.1    Hawley, R.S.2
  • 11
    • 27644509696 scopus 로고    scopus 로고
    • Drosophila Nod protein binds preferentially to the plus ends of microtubules and promotes microtubule polymerization in vitro
    • Cui W., Sproul L.R., Gustafson S.M., Matthies H.J., Gilbert S.P., and Hawley R.S. Drosophila Nod protein binds preferentially to the plus ends of microtubules and promotes microtubule polymerization in vitro. Mol. Biol. Cell 16 (2005) 5400-5409
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5400-5409
    • Cui, W.1    Sproul, L.R.2    Gustafson, S.M.3    Matthies, H.J.4    Gilbert, S.P.5    Hawley, R.S.6
  • 12
    • 1642333310 scopus 로고    scopus 로고
    • Relating biochemistry and function in the myosin superfamily
    • De La Cruz E.M., and Ostap E.M. Relating biochemistry and function in the myosin superfamily. Curr. Opin. Cell Biol. 16 (2004) 61-67
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 61-67
    • De La Cruz, E.M.1    Ostap, E.M.2
  • 14
    • 0030581163 scopus 로고    scopus 로고
    • Direct evidence of a role for heterochromatin in meiotic chromosome segregation
    • Dernburg A.F., Sedat J.W., and Hawley R.S. Direct evidence of a role for heterochromatin in meiotic chromosome segregation. Cell 86 (1996) 135-146
    • (1996) Cell , vol.86 , pp. 135-146
    • Dernburg, A.F.1    Sedat, J.W.2    Hawley, R.S.3
  • 16
    • 0034430847 scopus 로고    scopus 로고
    • Kinetics: a tool to study molecular motors
    • Gilbert S.P., and Mackey A.T. Kinetics: a tool to study molecular motors. Methods 22 (2000) 337-354
    • (2000) Methods , vol.22 , pp. 337-354
    • Gilbert, S.P.1    Mackey, A.T.2
  • 17
    • 0141768258 scopus 로고    scopus 로고
    • The roles of microtubule-based motor proteins in mitosis: comprehensive RNAi analysis in the Drosophila S2 cell line
    • Goshima G., and Vale R.D. The roles of microtubule-based motor proteins in mitosis: comprehensive RNAi analysis in the Drosophila S2 cell line. J. Cell Biol. 162 (2003) 1003-1016
    • (2003) J. Cell Biol. , vol.162 , pp. 1003-1016
    • Goshima, G.1    Vale, R.D.2
  • 18
    • 1542353988 scopus 로고
    • Kinesin ATPase: rate-limiting ADP release
    • Hackney D.D. Kinesin ATPase: rate-limiting ADP release. Proc. Natl. Acad. Sci. USA 85 (1988) 6314-6318
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 6314-6318
    • Hackney, D.D.1
  • 19
    • 33748421625 scopus 로고    scopus 로고
    • Large conformational changes in a kinesin motor catalyzed by interaction with microtubules
    • Hirose K., Akimaru E., Akiba T., Endow S.A., and Amos L.A. Large conformational changes in a kinesin motor catalyzed by interaction with microtubules. Mol. Cell 23 (2006) 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
  • 20
    • 0021070504 scopus 로고
    • The pathway of ATP hydrolysis by dynein. Kinetics of a presteady state phosphate burst
    • Johnson K.A. The pathway of ATP hydrolysis by dynein. Kinetics of a presteady state phosphate burst. J. Biol. Chem. 258 (1983) 13825-13832
    • (1983) J. Biol. Chem. , vol.258 , pp. 13825-13832
    • Johnson, K.A.1
  • 21
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26 (1993) 795-800
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 25
    • 0036150882 scopus 로고    scopus 로고
    • Kinesin: switch I & II and the motor mechanism
    • Kull F.J., and Endow S.A. Kinesin: switch I & II and the motor mechanism. J. Cell Sci. 115 (2002) 15-23
    • (2002) J. Cell Sci. , vol.115 , pp. 15-23
    • Kull, F.J.1    Endow, S.A.2
  • 26
    • 1542286175 scopus 로고    scopus 로고
    • A new structural state of myosin
    • Kull F.J., and Endow S.A. A new structural state of myosin. Trends Biochem. Sci. 29 (2004) 103-106
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 103-106
    • Kull, F.J.1    Endow, S.A.2
  • 27
    • 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. Crystal structure of the kinesin motor domain reveals a structural similarity to myosin. Nature 380 (1996) 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
  • 28
    • 0033552614 scopus 로고    scopus 로고
    • Mutations in the alpha-tubulin 67C gene specifically impair achiasmate segregation in Drosophila melanogaster
    • Matthies H.J., Messina L.G., Namba R., Greer K.J., Walker M.Y., and Hawley R.S. Mutations in the alpha-tubulin 67C gene specifically impair achiasmate segregation in Drosophila melanogaster. J. Cell Biol. 147 (1999) 1137-1144
    • (1999) J. Cell Biol. , vol.147 , pp. 1137-1144
    • Matthies, H.J.1    Messina, L.G.2    Namba, R.3    Greer, K.J.4    Walker, M.Y.5    Hawley, R.S.6
  • 29
    • 0035658281 scopus 로고    scopus 로고
    • Orphan kinesin NOD lacks motile properties but does possess a microtubule-stimulated ATPase activity
    • Matthies H.J., Baskin R.J., and Hawley R.S. Orphan kinesin NOD lacks motile properties but does possess a microtubule-stimulated ATPase activity. Mol. Biol. Cell 12 (2001) 4000-4012
    • (2001) Mol. Biol. Cell , vol.12 , pp. 4000-4012
    • Matthies, H.J.1    Baskin, R.J.2    Hawley, R.S.3
  • 30
    • 0036859964 scopus 로고    scopus 로고
    • Crossover distribution and high interference for both the X chromosome and an autosome during oogenesis and spermatogenesis in Caenorhabditis elegans
    • Meneely P.M., Farago A.F., and Kauffman T.M. Crossover distribution and high interference for both the X chromosome and an autosome during oogenesis and spermatogenesis in Caenorhabditis elegans. Genetics 162 (2002) 1169-1177
    • (2002) Genetics , vol.162 , pp. 1169-1177
    • Meneely, P.M.1    Farago, A.F.2    Kauffman, T.M.3
  • 31
    • 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. A common mechanism for microtubule destabilizers-M type kinesins stabilize curling of the protofilament using the class-specific neck and loops. Cell 116 (2004) 591-602
    • (2004) Cell , vol.116 , pp. 591-602
    • Ogawa, T.1    Nitta, R.2    Okada, Y.3    Hirokawa, N.4
  • 32
    • 0028084845 scopus 로고
    • A structure-function analysis of NOD, a kinesin-like protein from Drosophila melanogaster
    • Rasooly R.S., Zhang P., Tibolla A.K., and Hawley R.S. A structure-function analysis of NOD, a kinesin-like protein from Drosophila melanogaster. Mol. Gen. Genet. 242 (1994) 145-151
    • (1994) Mol. Gen. Genet. , vol.242 , pp. 145-151
    • Rasooly, R.S.1    Zhang, P.2    Tibolla, A.K.3    Hawley, R.S.4
  • 34
    • 34248200882 scopus 로고    scopus 로고
    • The beginning of kinesin's force-generating cycle visualized at 9-A resolution
    • Sindelar C.V., and Downing K.H. The beginning of kinesin's force-generating cycle visualized at 9-A resolution. J. Cell Biol. 177 (2007) 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. Two conformations in the human kinesin power stroke defined by X-ray crystallography and EPR spectroscopy. Nat. Struct. Biol. 9 (2002) 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
  • 38
    • 33845291163 scopus 로고    scopus 로고
    • Ab initio resolution measurement for single particle structures
    • Sousa D., and Grigorieff N. Ab initio resolution measurement for single particle structures. J. Struct. Biol. 157 (2007) 201-210
    • (2007) J. Struct. Biol. , vol.157 , pp. 201-210
    • Sousa, D.1    Grigorieff, N.2
  • 39
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier F.W. Protein production by auto-induction in high density shaking cultures. Protein Expr. Purif. 41 (2005) 207-234
    • (2005) Protein Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 43
    • 0037459061 scopus 로고    scopus 로고
    • The molecular motor toolbox for intracellular transport
    • Vale R.D. The molecular motor toolbox for intracellular transport. Cell 112 (2003) 467-480
    • (2003) Cell , vol.112 , pp. 467-480
    • Vale, R.D.1
  • 44
    • 0343415156 scopus 로고    scopus 로고
    • The way things move: looking under the hood of molecular motor proteins
    • Vale R.D., and Milligan R.A. The way things move: looking under the hood of molecular motor proteins. Science 288 (2000) 88-95
    • (2000) Science , vol.288 , pp. 88-95
    • Vale, R.D.1    Milligan, R.A.2
  • 45
    • 0023090371 scopus 로고
    • Similarity measures between images
    • Van Heel M. Similarity measures between images. Ultramicroscopy 21 (1987) 95-100
    • (1987) Ultramicroscopy , vol.21 , pp. 95-100
    • Van Heel, M.1
  • 48
    • 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. 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
  • 49
    • 0025147718 scopus 로고
    • A kinesin-like protein required for distributive chromosome segregation in Drosophila
    • Zhang P., Knowles B.A., Goldstein L.S., and Hawley R.S. A kinesin-like protein required for distributive chromosome segregation in Drosophila. Cell 62 (1990) 1053-1062
    • (1990) Cell , vol.62 , pp. 1053-1062
    • Zhang, P.1    Knowles, B.A.2    Goldstein, L.S.3    Hawley, R.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.