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Eur Biophys J. 1998;27(5):466-73.

The role of the dynein stalk in cytoplasmic and flagellar motility.

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  • 1Worcester Foundation for Biomedical Research, University of Massachusetts Medical School, Shrewsbury 01545, USA. gee@sci.wfbr.edu

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.

PMID:
9760728
[PubMed - indexed for MEDLINE]
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