The role of the dynein stalk in cytoplasmic and flagellar motility |
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Authors: | Melissa Gee R Vallee |
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Institution: | (1) Worcester Foundation for Biomedical Research, University of Massachusetts Medical School, 222 Maple Avenue, Shrewsbury, MA 01545, USA e-mail: gee@sci.wfbr.edu, e-mail: vallee@sci.wfbr.edu, US |
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Abstract: | We have recently identified a microtubule binding domain within the motor protein cytoplasmic dynein. This domain is situated
at the end of a slender 10–12 nm projection which corresponds to the stalks previously observed extending from the heads of
both axonemal and cytoplasmic dyneins. The stalks also correspond to the B-links observed to connect outer arm axonemal dyneins
to the B-microtubules in flagella and constitute the microtubule attachment sites during dynein motility. The stalks contrast
strikingly with the polymer attachment domains of the kinesins and myosins which are found on the surface of the motor head.
The difference in dynein's structural design raises intriguing questions as to how the stalk functions in force production
along microtubules. In this article, we attempt to integrate the myriad of biochemical and EM structural data that has been
previously collected regarding dynein with recent molecular findings, in an effort to begin to understand the mechanism of
dynein motility.
Received: 13 March 1998 / Revised version: 17 April 1998 / Accepted: 17 April 1998 |
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Keywords: | Microtube Molecular motor |
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