Kinetochores' gripping feat: conformational wave or biased diffusion?

被引:41
作者
Asbury, Charles L. [1 ]
Tien, Jerry F. [2 ]
Davis, Trisha N. [2 ]
机构
[1] Univ Washington, Dept Physiol & Biophys, Seattle, WA 98195 USA
[2] Univ Washington, Dept Biochem, Seattle, WA 98195 USA
关键词
MICROTUBULE ATTACHMENT SITE; YEAST DASH COMPLEX; DAM1; COMPLEX; MOLECULAR ARCHITECTURE; CHROMOSOME MOTION; NDC80; FISSION YEAST; FORCE PRODUCTION; RING COMPLEX; SKA COMPLEX;
D O I
10.1016/j.tcb.2010.09.003
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Climbing up a cliff while the rope unravels underneath your fingers does not sound like a well-planned adventure. Yet chromosomes face a similar challenge during each cell division. Their alignment and accurate segregation depends on staying attached to the assembling and disassembling tips of microtubule fibers. This coupling is mediated by kinetochores, intricate machines that attach chromosomes to an ever-changing microtubule substrate. Two models for kinetochore-microtubule coupling were proposed a quarter century ago: conformational wave and biased diffusion. These models differ in their predictions for how coupling is performed and regulated. The availability of purified kinetochore proteins has enabled biochemical and biophysical analyses of the kinetochore-microtubule interface. Here, we discuss what these studies reveal about the contributions of each model.
引用
收藏
页码:38 / 46
页数:9
相关论文
共 83 条
[1]  
AKIYOSHI B, 2010, TENSION DIRECE UNPUB
[2]   Force Transduction by the Microtubule-Bound Dam1 Ring [J].
Armond, Jonathan W. ;
Turner, Matthew S. .
BIOPHYSICAL JOURNAL, 2010, 98 (08) :1598-1607
[3]   The Dam1 kinetochore complex harnesses microtubule dynamics to produce force and movement [J].
Asbury, Charles L. ;
Gestaut, Daniel R. ;
Powers, Andrew F. ;
Franck, Andrew D. ;
Davis, Trisha N. .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2006, 103 (26) :9873-9878
[4]  
Beer F.P., 1981, MECH MATER
[5]   Mechanical disruption of individual nucleosomes reveals a reversible multistage release of DNA [J].
Brower-Toland, BD ;
Smith, CL ;
Yeh, RC ;
Lis, JT ;
Peterson, CL ;
Wang, MD .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (04) :1960-1965
[6]   THE FREE-ENERGY FOR HYDROLYSIS OF A MICROTUBULE-BOUND NUCLEOTIDE TRIPHOSPHATE IS NEAR ZERO - ALL OF THE FREE-ENERGY FOR HYDROLYSIS IS STORED IN THE MICROTUBULE LATTICE [J].
CAPLOW, M ;
RUHLEN, RL ;
SHANKS, J .
JOURNAL OF CELL BIOLOGY, 1994, 127 (03) :779-788
[7]   Molecular architecture of the kinetochore-microtubule interface [J].
Cheeseman, Iain M. ;
Desai, Arshad .
NATURE REVIEWS MOLECULAR CELL BIOLOGY, 2008, 9 (01) :33-46
[8]   The conserved KMN network constitutes the core microtubule-binding site of the kinetochore [J].
Cheeseman, Iain M. ;
Chappie, Joshua S. ;
Wilson-Kubalek, Elizabeth M. ;
Desai, Arshad .
CELL, 2006, 127 (05) :983-997
[9]   A conserved protein network controls assembly of the outer kinetochore and its ability to sustain tension [J].
Cheeseman, IM ;
Niessen, S ;
Anderson, S ;
Hyndman, F ;
Yates, JR ;
Oegema, K ;
Desai, A .
GENES & DEVELOPMENT, 2004, 18 (18) :2255-2268
[10]   Phospho-regulation of kinetochore-microtubule attachments by the aurora kinase Ipl1p [J].
Cheeseman, LM ;
Anderson, S ;
Jwa, M ;
Green, EM ;
Kang, JS ;
Yates, JR ;
Chan, CSM ;
Drubin, DG ;
Barnes, G .
CELL, 2002, 111 (02) :163-172