Skip Navigation



Journal of Biochemistry Advance Access published online on September 10, 2007
Journal of Biochemistry, doi:10.1093/jb/mvm161
This Article
Right arrow Advance Access manuscript (PDF)
Right arrow All Versions of this Article:
142/4/481    most recent
mvm161v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Sakata, S.
Right arrow Articles by Mabuchi, I.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sakata, S.
Right arrow Articles by Mabuchi, I.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2007 The Japanese Biochemical Society

Characterizaion of native myosin VI isolated from sea urchin eggs

Souhei Sakata1, Yuuko Watanabe1, Jiro Usukura2 and Issei Mabuchi1,*

1Division of Biology, Department of Life Sciences, Graduate School of Arts and Science, University of Tokyo, Komaba, Meguro-ku, Tokyo 153-8902, Japan
2Center for Cooperative Research in Advanced Science and Technology, Nagoya University, Nagoya, 464-0814, Japan

*To whom correspondence should be addressed at: Issei Mabuchi: Department of Chemistry and Insititute for Biomolecular Science, School of Science, Gakushuin University, 1-5-1 Mejiro, Toshima-ku, Tokyo 171-8588, Japan Tel. +81-3-3986-0221 ext. 6421; Fax. +81-3-5992-1029, E-mail: issei.mabuchi{at}gakushuin.ac.jp

Received May 30, 2007; Accepted July 16, 2007


  Abstract

Myosin VI is a molecular motor that is ubiquitously expressed among eukaryotic cells, and thought to be involved in membrane trafficking and anchoring the organelle to actin cytoskeleton. Studies on myosin VI have been carried out using recombinant proteins, but native myosin VI has not been purified yet. Here we purified native myosin VI from sea urchin eggs and characterized its properties. We found that the native myosin VI was a monomeric and non-processive motor protein, and also showed that it moved toward the pointed end of F-actin. Ca2+ stimulated actin-activated MgATPase activity of the native myosin VI, while it lowered its motility on F-actin. Immunofluorescence microscopy showed that the myosin VI was translocated from the inner cytoplasm to the cortex after fertilization. Myosin VI may be involved in endocytic activities in fertilized eggs.

Key Words: F-actin, motor protein, native myosin VI, sea urchin, unconventional myosin


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Mol. Biol. CellHome page
T. Noguchi, D. J. Frank, M. Isaji, and K. G. Miller
Coiled-Coil-Mediated Dimerization Is Not Required for Myosin VI to Stabilize Actin during Spermatid Individualization in Drosophila melanogaster
Mol. Biol. Cell, January 1, 2009; 20(1): 358 - 367.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.