List of Publication
From 2001 to present
1. Allosteric regulation of microtubules
Ayukawa R, Iwata S, Imai S, Kamimura S, Hayashi M, Ngo Kien Xuan, Minoura S, Uchimura S, Makino T, Shirouzu M, Shigematsu H, Sekimoto K, Gigant B, and Muto E. GTP-dependent formation of straight tubulin oligomers leads to microtubule nucleation.
J. Cell Biol. 220: doi. 10.1083/jcb.202007033 (2021).
Muto E, Sakai H, Kaseda K. Long-range cooperative binding of kinesin to a microtubule in the presence of ATP.
J Cell Biol. 168:691-6 (2005).
Some evidence for a long-range state transition of microtubules during motility of kinesin is presented. Despite the conventional view of microtubules as being static tracks for motors, the study indicates conformational flexibility of microtubules could be an essential component in kinesin motility mechanism. The paper was recommended in Faculty Opinion (https://facultyopinions.com/prime/home/).
2. Interface of microtubule for motor proteins
Uchimura S, Fujii T, Takazaki H, Ayukawa R, Nishikawa Y, Minoura I, Hachikubo Y, Kurisu G, Sutoh K, Kon T, Namba K, Muto E. A flipped ion pair at the dynein-microtubule interface is critical for dynein motility and ATPase activation.
J Cell Biol. 208:211-22 (2015).
In this and the following two papers, the residues on the microtubule critical for motility of motor proteins, kinesin and dynein, have been characterized using mutational analysis of tubulin. The short loop/helix of alpha-tubulin composed of four peptides appeared critical for ATPase activation in both kinesin and dynein.
Uchimura S, Oguchi Y, Hachikubo Y, Ishiwata S, Muto E. Key residues on microtubule responsible for activation of kinesin ATPase.
Uchimura S, Oguchi Y, Katsuki M, Usui T, Osada H, Nikawa J, Ishiwata S, Muto E. Identification of a strong binding site for kinesin on the microtubule using mutant analysis of tubulin.
3. Physics of microtubules
Minoura I, Katayama E, Sekimoto K, Muto E. One-dimensional Brownian motion of charged nanoparticles along microtubules: a model system for weak binding interactions.
Extending the previous paper (Minoura and Muto, 2006), this study established a theoretical framework for the mechanism of weak electrostatic interactions of microtubules with various proteins.
Minoura I, Muto E. Dielectric measurement of individual microtubules using the electroorientation method.
We developed an experiment system to quantitatively evaluate the polyelectrolyte nature of microtubules. The study paves a way for future exploration of the physicochemical mechanism underlying the weak electrostatic interactions of microtubules with various proteins.
3. Recombinant tubulin and other technique
Minoura I, Takazaki H, Ayukawa R, Saruta C, Hachikubo Y, Uchimura S, Hida T, Kamiguchi H, Shimogori T, Muto E. Reversal of axonal growth defects in an extraocular fibrosis model by engineering the kinesin-microtubule interface.
Using the recombinant human tubulin TUBB3 , the study dissects the molecular mechanism underlying the neuronal disease named CFEOM. The paper was recommended in Faculty Opinion.
Hotta T, Fujita S, Uchimura S, Noguchi M, Demura T, Muto E, Hashimoto T. Affinity purification and characterization of functional tubulin from cell suspension cultures of Arabidopsis and tobacco. Plant Physiol. 170(3): 1189-1205 (2016).
The technology of recombinant tubulin was arranged for the expression and purification of plant tubulin. The paper was recommended in Faculty Opinion.
Minoura I, Hachikubo Y, Yamakita Y, Takazaki H, Ayukawa R, Uchimura S, Muto E. Overexpression, purification, and functional analysis of recombinant human tubulin dimer.
We established a baculovirus-insect cell expression system for the purification of recombinant human tubulin, which has been a major challenge for decades. The paper was recommended in Faculty Opinion.
Katsuki M, Muto E, Cross RA. Preparation of dual-color polarity-marked fluorescent microtubule seeds.
Methods Mol Biol. 777:117-26 (2011).
Until 2001
Nishiyama M, Muto E, Inoue Y, Yanagida T, Higuchi H. Substeps within the 8-nm step of the ATPase cycle of single kinesin molecules.
Nat Cell Biol. 3:425-8 (2001).
Inoue Y, Iwane AH, Miyai T, Muto E, Yanagida T. Motility of single one-headed kinesin molecules along microtubules.
Biophys J. 81:2838-50 (2001).
Miyamoto Y, Muto E, Mashimo T, Iwane AH, Yoshiya I, Yanagida T. Direct inhibition of microtubule-based kinesin motility by local anesthetics.
Biophys J. 78:940-9 (2000).
Higuchi H, Muto E, Inoue Y, Yanagida T. Kinetics of force generation by single kinesin molecules activated by laser photolysis of caged ATP.
Proc Natl Acad Sci USA. 94:4395-400 (1997).
Kojima H, Muto E, Higuchi H, Yanagida T. Mechanics of single kinesin molecules measured by optical nanometry.
Biophys J. 73:2012-22 (1997).
Muto E, Edamatsu M, Hirono M, Kamiya R. Immunological detection of actin in the 14S ciliary dynein of Tetrahymena.
FEBS Lett. 343:173-6 (1994).
Kamiya R, Kurimoto E, Muto E. Two types of Chlamydomonas flagellar mutants missing different components of inner-arm dynein.
J Cell Biol. 112:441-7 (1991).
Muto E, Kamiya R, Tsukita S. Double-rowed organization of inner dynein arms in Chlamydomonas flagella revealed by tilt- series thin-section electron microscopy.
J Cell Sci. 99:57-66 (1991).
Kamiya R, Hasegawa E. Intrinsic difference in beat frequency between the two flagella of Chlamydomonas reinhardtii.
Exp Cell Res. 173:299-304 (1987).
Hasegawa E, Hayashi H, Asakura S, Kamiya R. Stimulation of in vitro motility of Chlamydomonas axonemes by inhibition of cAMP-dependent phosphorylation.
Cell Motil Cytoskel. 8:302-11 (1987).
Newman SA, Frenz DA, Hasegawa E, Akiyama SK. Matrix-driven translocation: Dependence on interaction of amino-terminal domain of fibronectin with heparin-like surface components of cells or particles.
Proc Natl Acad Sci USA. 84:4791-5 (1987).
McDonald JA, Quade BJ, Broekelmann TJ, LaChance R, Forsmant K, Hasegawa E, Akiyama S. Fibronectin’s cell-adhesive domain and an amino-terminal matrix assembly domain participate in its assembly into fibroblast pericellular matrix.
J Biol Chem. 262:2957-67 (1987).
Akiyama SK, Hasegawa E, Hasegawa T, Yamada KM. The interaction of fibronectin fragments with fibroblastic cells.
J Biol Chem. 260:13256-60 (1985).
Hasegawa T, Hasegawa E, Chen WT, Yamada KM. Characterization of a membrane-associated glycoprotein complex implicated in cell adhesion to firbonectin.
J Cell Biochem. 28:307-18 (1985).
Chen WT, Hasegawa E, Hasegawa T, Weinstock C, Yamada KM. Development of cell surface linkage complexes in cultured fibroblasts.
J Cell Biol. 100:1103-14 (1985).
Hasegawa E, Kamiya R, Asakura S. Thermal transition in helical forms of Salmonella flagella.
J Mol Biol. 160:609-21 (1982).