메뉴 건너뛰기




Volumn 20, Issue 10, 2010, Pages 939-943

Neck Linker Length Determines the Degree of Processivity in Kinesin-1 and Kinesin-2 Motors

Author keywords

CELLBIO

Indexed keywords

DROSOPHILA PROTEIN; HYBRID PROTEIN; ISOPROTEIN; KINESIN;

EID: 77953135927     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2010.03.065     Document Type: Article
Times cited : (95)

References (19)
  • 1
    • 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
  • 2
    • 0038381479 scopus 로고    scopus 로고
    • Stepping and stretching. How kinesin uses internal strain to walk processively
    • Rosenfeld S.S., Fordyce P.M., Jefferson G.M., King P.H., and Block S.M. Stepping and stretching. How kinesin uses internal strain to walk processively. J. Biol. Chem. 278 (2003) 18550-18556
    • (2003) J. Biol. Chem. , vol.278 , pp. 18550-18556
    • Rosenfeld, S.S.1    Fordyce, P.M.2    Jefferson, G.M.3    King, P.H.4    Block, S.M.5
  • 3
    • 0142040356 scopus 로고    scopus 로고
    • Modulation of kinesin half-site ADP release and kinetic processivity by a spacer between the head groups
    • Hackney D.D., Stock M.F., Moore J., and Patterson R.A. Modulation of kinesin half-site ADP release and kinetic processivity by a spacer between the head groups. Biochemistry 42 (2003) 12011-12018
    • (2003) Biochemistry , vol.42 , pp. 12011-12018
    • Hackney, D.D.1    Stock, M.F.2    Moore, J.3    Patterson, R.A.4
  • 4
    • 34247571461 scopus 로고    scopus 로고
    • Kinesin motor mechanics: binding, stepping, tracking, gating, and limping
    • Block S.M. Kinesin motor mechanics: binding, stepping, tracking, gating, and limping. Biophys. J. 92 (2007) 2986-2995
    • (2007) Biophys. J. , vol.92 , pp. 2986-2995
    • Block, S.M.1
  • 5
    • 51549097934 scopus 로고    scopus 로고
    • Intramolecular strain coordinates kinesin stepping behavior along microtubules
    • Yildiz A., Tomishige M., Gennerich A., and Vale R.D. Intramolecular strain coordinates kinesin stepping behavior along microtubules. Cell 134 (2008) 1030-1041
    • (2008) Cell , vol.134 , pp. 1030-1041
    • Yildiz, A.1    Tomishige, M.2    Gennerich, A.3    Vale, R.D.4
  • 6
    • 61449240125 scopus 로고    scopus 로고
    • The processivity of kinesin-2 motors suggests diminished front-head gating
    • Muthukrishnan G., Zhang Y., Shastry S., and Hancock W.O. The processivity of kinesin-2 motors suggests diminished front-head gating. Curr. Biol. 19 (2009) 442-447
    • (2009) Curr. Biol. , vol.19 , pp. 442-447
    • Muthukrishnan, G.1    Zhang, Y.2    Shastry, S.3    Hancock, W.O.4
  • 7
    • 75649106490 scopus 로고    scopus 로고
    • Strain through the neck linker ensures processive runs: a DNA-kinesin hybrid nanomachine study
    • DOI: 10.1038/emboj.2009.319
    • Miyazono Y., Hayashi M., Karagiannis P., Harada Y., and Tadakuma H. Strain through the neck linker ensures processive runs: a DNA-kinesin hybrid nanomachine study. EMBO J. 29 (2009) 93-106. The EMBO journal(2010),29(1),93-106, DOI: 10.1038/emboj.2009.319.
    • (2010) The EMBO journal , vol.29 , Issue.1 , pp. 93-106
    • Miyazono, Y.1    Hayashi, M.2    Karagiannis, P.3    Harada, Y.4    Tadakuma, H.5
  • 8
    • 67650659174 scopus 로고    scopus 로고
    • Insights into the mechanical properties of the kinesin neck linker domain from sequence analysis and molecular dynamics simulations
    • Hariharan V., and Hancock W.O. Insights into the mechanical properties of the kinesin neck linker domain from sequence analysis and molecular dynamics simulations. Cell. Mol. Bioeng. 2 (2009) 177-189
    • (2009) Cell. Mol. Bioeng. , vol.2 , pp. 177-189
    • Hariharan, V.1    Hancock, W.O.2
  • 9
    • 0034722373 scopus 로고    scopus 로고
    • Engineering the processive run length of the kinesin motor
    • Thorn K.S., Ubersax J.A., and Vale R.D. Engineering the processive run length of the kinesin motor. J. Cell Biol. 151 (2000) 1093-1100
    • (2000) J. Cell Biol. , vol.151 , pp. 1093-1100
    • Thorn, K.S.1    Ubersax, J.A.2    Vale, R.D.3
  • 10
    • 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., and 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
  • 11
    • 27744552948 scopus 로고    scopus 로고
    • The E-hook of tubulin interacts with kinesin's head to increase processivity and speed
    • Lakämper S., and Meyhöfer E. The E-hook of tubulin interacts with kinesin's head to increase processivity and speed. Biophys. J. 89 (2005) 3223-3234
    • (2005) Biophys. J. , vol.89 , pp. 3223-3234
    • Lakämper, S.1    Meyhöfer, E.2
  • 12
    • 0033539520 scopus 로고    scopus 로고
    • Kinesin's processivity results from mechanical and chemical coordination between the ATP hydrolysis cycles of the two motor domains
    • Hancock W.O., and Howard J. Kinesin's processivity results from mechanical and chemical coordination between the ATP hydrolysis cycles of the two motor domains. Proc. Natl. Acad. Sci. USA 96 (1999) 13147-13152
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13147-13152
    • Hancock, W.O.1    Howard, J.2
  • 13
    • 33847770916 scopus 로고    scopus 로고
    • Internal strain regulates the nucleotide binding site of the kinesin leading head
    • Hyeon C., and Onuchic J.N. Internal strain regulates the nucleotide binding site of the kinesin leading head. Proc. Natl. Acad. Sci. USA 104 (2007) 2175-2180
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 2175-2180
    • Hyeon, C.1    Onuchic, J.N.2
  • 14
    • 0037006974 scopus 로고    scopus 로고
    • Pathway of ADP-stimulated ADP release and dissociation of tethered kinesin from microtubules. Implications for the extent of processivity
    • Hackney D.D. Pathway of ADP-stimulated ADP release and dissociation of tethered kinesin from microtubules. Implications for the extent of processivity. Biochemistry 41 (2002) 4437-4446
    • (2002) Biochemistry , vol.41 , pp. 4437-4446
    • Hackney, D.D.1
  • 15
    • 0032559822 scopus 로고    scopus 로고
    • Processivity of the motor protein kinesin requires two heads
    • Hancock W.O., and Howard J. Processivity of the motor protein kinesin requires two heads. J. Cell Biol. 140 (1998) 1395-1405
    • (1998) J. Cell Biol. , vol.140 , pp. 1395-1405
    • Hancock, W.O.1    Howard, J.2
  • 17
    • 0020009818 scopus 로고
    • Preparation of tubulin from brain
    • Williams Jr. R.C., and Lee J.C. Preparation of tubulin from brain. Methods Enzymol. 85 Pt B (1982) 376-385
    • (1982) Methods Enzymol. , vol.85 PART B , pp. 376-385
    • Williams Jr., R.C.1    Lee, J.C.2
  • 19
    • 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. Kinesin's tail domain is an inhibitory regulator of the motor domain. Nat. Cell Biol. 1 (1999) 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.