Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 12 December 2008:
Vol. 322. no. 5908, pp. 1691 - 1695
DOI: 10.1126/science.1164424
Prev | Table of Contents | Next

Reports

Structure and Functional Role of Dynein's Microtubule-Binding Domain

Andrew P. Carter,1* Joan E. Garbarino,2* Elizabeth M. Wilson-Kubalek,3 Wesley E. Shipley,2 Carol Cho,1 Ronald A. Milligan,3 Ronald D. Vale,1{dagger} I. R. Gibbons2

Dynein motors move various cargos along microtubules within the cytoplasm and power the beating of cilia and flagella. An unusual feature of dynein is that its microtubule-binding domain (MTBD) is separated from its ring-shaped AAA+ adenosine triphosphatase (ATPase) domain by a 15-nanometer coiled-coil stalk. We report the crystal structure of the mouse cytoplasmic dynein MTBD and a portion of the coiled coil, which supports a mechanism by which the ATPase domain and MTBD may communicate through a shift in the heptad registry of the coiled coil. Surprisingly, functional data suggest that the MTBD, and not the ATPase domain, is the main determinant of the direction of dynein motility.

1 Howard Hughes Medical Institute and Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94158, USA.
2 Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.
3 Department of Cell Biology, Scripps Research Institute, La Jolla, CA 92037, USA.

* These authors contributed equally to this work.

{dagger} To whom correspondence should be addressed. E-mail: vale{at}cmp.ucsf.edu

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Multivalency in the Assembly of Intrinsically Disordered Dynein Intermediate Chain.
J. Hall, P. A. Karplus, and E. Barbar (2009)
J. Biol. Chem. 284, 33115-33121
   Abstract »    Full Text »    PDF »
An outer arm dynein light chain acts in a conformational switch for flagellar motility.
R. S. Patel-King and S. M. King (2009)
J. Cell Biol. 186, 283-295
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)