JCB logo
Quantitative Colocalization Analysis Software
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 602K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lantz, V. A.
Right arrow Articles by Miller, K. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lantz, V. A.
Right arrow Articles by Miller, K. G.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Facebook   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

© The Rockefeller University Press, 0021-9525/1998//897 $5.00
The Journal of Cell Biology, Volume 140, Number 4, , 1998 897-910

Article

A Class VI Unconventional Myosin Is Associated with a Homologue of a Microtubule-binding Protein, Cytoplasmic Linker Protein–170, in Neurons and at the Posterior Pole of Drosophila Embryos



Valerie A. Lantz and Kathryn G. Miller

Department of Biology, Washington University, St. Louis, Missouri 63130

Abstract. Coordination of cellular organization requires the interaction of the cytoskeletal filament systems. Recently, several lines of investigation have suggested that transport of cellular components along both microtubules and actin filaments is important for cellular organization and function. We report here on molecules that may mediate coordination between the actin and microtubule cytoskeletons. We have identified a 195-kD protein that coimmunoprecipitates with a class VI myosin, Drosophila 95F unconventional myosin. Cloning and sequencing of the gene encoding the 195-kD protein reveals that it is the first homologue identified of cytoplasmic linker protein (CLIP)–170, a protein that links endocytic vesicles to microtubules. We have named this protein D-CLIP-190 (the predicted molecular mass is 189 kD) based on its similarity to CLIP-170 and its ability to cosediment with microtubules. The similarity between D-CLIP-190 and CLIP-170 extends throughout the length of the proteins, and they have a number of predicted sequence and structural features in common. 95F myosin and D-CLIP-190 are coexpressed in a number of tissues during embryogenesis in Drosophila. In the axonal processes of neurons, they are colocalized in the same particulate structures, which resemble vesicles. They are also colocalized at the posterior pole of the early embryo, and this localization is dependent on the actin cytoskeleton. The association of a myosin and a homologue of a microtubule-binding protein in the nervous system and at the posterior pole, where both microtubule and actin-dependent processes are known to be important, leads us to speculate that these two proteins may functionally link the actin and microtubule cytoskeletons.

We are especially grateful for the help of J. Verbsky and C. Cheney (both from Washington University, St. Louis, MO) with automated fluorescent DNA sequencing. In addition, we thank the Department of Genetics at Washington University School of Medicine for use of the ABI Prism sequencing system. We thank J. Diani and the animal facility in the Biology Department at Washington University for injecting and bleeding the mice. We thank R. Steward for the dorsal antibody. We thank J. Cooper, J. McNally, C. Cheney, C. Wagner, R. Hopmann, J. Hicks, B. Clifford (all from Washington University), and T. Schroer (Johns Hopkins University, Baltimore, MD) for helpful suggestions on the manuscript.

This work was supported by an American Cancer Society postdoctoral fellowship to V. Lantz and a National Institutes of Health grant to K.G. Miller.

Address all correspondence to Valerie A. Lantz, Department of Biology, Washington University, St. Louis, MO 63130. Tel.: (314) 935-7339. Fax: (314) 935-5125. E-mail: Lantz{at}biodec.WUSTL.edu

1. Abbreviations used in this paper: CLIP, cytoplasmic linker protein; CNS, central nervous system; GST, glutathione-S-transferase; IP, immunoprecipitation; MBP, maltose-binding protein fusion; ORF, open reading frame.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Facebook Facebook   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?


This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents