A flipped ion pair at the dynein-microtubule interface is critical for dynein motility and ATPase activation.

PubWeight™: 0.82‹?›

🔗 View Article (PMC 4298687)

Published in J Cell Biol on January 12, 2015

Authors

Seiichi Uchimura1, Takashi Fujii2, Hiroko Takazaki1, Rie Ayukawa1, Yosuke Nishikawa3, Itsushi Minoura1, You Hachikubo1, Genji Kurisu4, Kazuo Sutoh5, Takahide Kon6, Keiichi Namba7, Etsuko Muto8

Author Affiliations

1: Laboratory for Molecular Biophysics, RIKEN Brain Science Institute, Wako, Saitama 351-0198, Japan.
2: Graduate School of Frontier Biosciences and Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan Japan Science and Technology Agency, Precursory Research for Embryonic Science and Technology, Kawaguchi, Saitama 332-0012, Japan Quantitative Biology Center, Institute of Physical and Chemical Research, Suita, Osaka 565-0871, Japan.
3: Graduate School of Frontier Biosciences and Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan.
4: Graduate School of Frontier Biosciences and Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan Department of Macromolecular Science, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan.
5: Research Institute for Science and Engineering, Waseda University, Toshima-ku, Tokyo 171-0033, Japan.
6: Japan Science and Technology Agency, Precursory Research for Embryonic Science and Technology, Kawaguchi, Saitama 332-0012, Japan Department of Macromolecular Science, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan Department of Frontier Bioscience, Faculty of Bioscience and Applied Chemistry, Hosei University, Koganei, Tokyo 184-8584, Japan.
7: Graduate School of Frontier Biosciences and Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan Quantitative Biology Center, Institute of Physical and Chemical Research, Suita, Osaka 565-0871, Japan.
8: Laboratory for Molecular Biophysics, RIKEN Brain Science Institute, Wako, Saitama 351-0198, Japan emuto2@brain.riken.jp.

Articles cited by this

Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr (2004) 227.01

Accurate determination of local defocus and specimen tilt in electron microscopy. J Struct Biol (2003) 14.19

Preparation of modified tubulins. Methods Enzymol (1991) 7.90

Refined structure of alpha beta-tubulin at 3.5 A resolution. J Mol Biol (2001) 7.08

Disruption of mitotic spindle orientation in a yeast dynein mutant. Proc Natl Acad Sci U S A (1993) 5.94

Cytoplasmic dynein is required for normal nuclear segregation in yeast. Proc Natl Acad Sci U S A (1993) 5.83

Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay. J Mol Biol (1990) 4.78

Dynein structure and power stroke. Nature (2003) 4.25

Cilia and flagella of eukaryotes. J Cell Biol (1981) 3.37

Saccharomyces cerevisiae kinesin- and dynein-related proteins required for anaphase chromosome segregation. J Cell Biol (1995) 3.22

Protein structure fitting and refinement guided by cryo-EM density. Structure (2008) 3.12

Mutations in alpha-tubulin cause abnormal neuronal migration in mice and lissencephaly in humans. Cell (2007) 3.06

Two microtubule-associated proteins required for anaphase spindle movement in Saccharomyces cerevisiae. J Cell Biol (1995) 3.02

Direct visualization of secondary structures of F-actin by electron cryomicroscopy. Nature (2010) 2.93

Engineering the processive run length of the kinesin motor. J Cell Biol (2000) 2.91

The initial phosphate burst in ATP hydrolysis by myosin and subfragment-1 as studied by a modified malachite green method for determination of inorganic phosphate. J Biochem (1986) 2.83

Structure and functional role of dynein's microtubule-binding domain. Science (2008) 2.80

Genetic control of differentiation of the Caenorhabditis elegans touch receptor neurons. Science (1989) 2.73

The iterative helical real space reconstruction method: surmounting the problems posed by real polymers. J Struct Biol (2006) 2.70

Crystal structure of the dynein motor domain. Science (2011) 2.57

Molecular motors: strategies to get along. Curr Biol (2004) 2.41

Tools for integrated sequence-structure analysis with UCSF Chimera. BMC Bioinformatics (2006) 2.38

One-dimensional diffusion of microtubules bound to flagellar dynein. Cell (1989) 2.31

New data on the microtubule surface lattice. Biol Cell (1991) 2.26

ATP hydrolysis cycle-dependent tail motions in cytoplasmic dynein. Nat Struct Mol Biol (2005) 2.15

Stu2p: A microtubule-binding protein that is an essential component of the yeast spindle pole body. J Cell Biol (1997) 2.14

Dynein achieves processive motion using both stochastic and coordinated stepping. Nat Struct Mol Biol (2012) 1.98

The beginning of kinesin's force-generating cycle visualized at 9-A resolution. J Cell Biol (2007) 1.97

The affinity of the dynein microtubule-binding domain is modulated by the conformation of its coiled-coil stalk. J Biol Chem (2005) 1.79

The C-terminus of tubulin increases cytoplasmic dynein and kinesin processivity. Biophys J (2000) 1.66

The 2.8 Å crystal structure of the dynein motor domain. Nature (2012) 1.65

Cytoplasmic dynein moves through uncoordinated stepping of the AAA+ ring domains. Science (2011) 1.63

The dynein family at a glance. J Cell Sci (2006) 1.62

Helix sliding in the stalk coiled coil of dynein couples ATPase and microtubule binding. Nat Struct Mol Biol (2009) 1.61

Dynein and kinesin share an overlapping microtubule-binding site. EMBO J (2004) 1.57

Functions and mechanics of dynein motor proteins. Nat Rev Mol Cell Biol (2013) 1.56

Purification and biochemical characterization of tubulin from the budding yeast Saccharomyces cerevisiae. Biochemistry (1993) 1.56

Mechanism of microtubule kinesin ATPase. Biochemistry (1995) 1.55

Structural basis for microtubule binding and release by dynein. Science (2012) 1.45

Web servers and services for electrostatics calculations with APBS and PDB2PQR. J Comput Chem (2011) 1.45

End-to-end annealing of microtubules in vitro. J Cell Biol (1986) 1.43

LIS1: cellular function of a disease-causing gene. Trends Cell Biol (2001) 1.30

Understanding tubulin-Taxol interactions: mutations that impart Taxol binding to yeast tubulin. Proc Natl Acad Sci U S A (2003) 1.30

Functional elements within the dynein microtubule-binding domain. Mol Biol Cell (2000) 1.29

Head-head coordination is required for the processive motion of cytoplasmic dynein, an AAA+ molecular motor. J Struct Biol (2006) 1.24

Identification of a strong binding site for kinesin on the microtubule using mutant analysis of tubulin. EMBO J (2006) 1.18

Electron energy filtering significantly improves amplitude contrast of frozen-hydrated protein at 300kV. J Struct Biol (2006) 1.05

Key residues on microtubule responsible for activation of kinesin ATPase. EMBO J (2010) 1.04

C-sequence of the Dictyostelium cytoplasmic dynein participates in processivity modulation. FEBS Lett (2011) 1.02

Overexpression, purification, and functional analysis of recombinant human tubulin dimer. FEBS Lett (2013) 0.89

Real-space refinement with DireX: from global fitting to side-chain improvements. Biopolymers (2012) 0.89

Structure of the entire stalk region of the Dynein motor domain. J Mol Biol (2014) 0.87

One-dimensional Brownian motion of charged nanoparticles along microtubules: a model system for weak binding interactions. Biophys J (2010) 0.86

Protein engineering approaches to study the dynein mechanism using a Dictyostelium expression system. Methods Cell Biol (2009) 0.81

Microtubule structure in Caenorhabditis elegans neurons. Cold Spring Harb Symp Quant Biol (1982) 0.79