Molecular Biology of the Cell Call for Nominations: MBC Editor-in-Chief

Home Help [Feedback] [For Subscribers] [Archive] [Search] --
QUICK SEARCH:   [advanced]


     

MBC in Press, published online ahead of print May 30, 2007
Mol. Biol. Cell 10.1091/mbc.E07-01-0040

A more recent version of this article appeared on August 1, 2007
This Article
Right arrow Full Text (PDF)
Right arrow Supplemental Material
Right arrow All Versions of this Article:
E07-01-0040v1
18/8/3039    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
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 Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Johnson, T. M.
Right arrow Articles by Beckers, C. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Johnson, T. M.
Right arrow Articles by Beckers, C. J.

Submitted on January 18, 2007
Revised on May 14, 2007
Accepted on May 18, 2007

Immobilization of the Type XIV Myosin Complex in Toxoplasma gondii

Terezina M. Johnson, Zenon Rajfur, Ken Jacobson, and Con J. Beckers

Department of Cell and Developmental Biology, The University of North Carolina, Chapel Hill, NC 27599-7090

Monitoring Editor: Yu-li Wang

The substrate-dependent movement of apicomplexan parasites like Toxoplasma gondii and Plasmodium sp. is driven by the interaction of a type XIV myosin with F-actin. A complex containing the myosin-A heavy chain, a myosin light chain and the accessory protein GAP45 is attached to the membranes of the inner membrane complex (IMC) through its tight interaction with the integral membrane glycoprotein GAP50. In order for the interaction of this complex with F-actin to result in net parasite movement, it is necessary that one of them be immobilized with respect to the parasite and the other with respect to the substrate the parasite is moving on. We report here that the myosin motor complex of Toxoplasma is firmly immobilized in the plane of the IMC. This does not appear to be accomplished by direct interactions with cytoskeletal elements. Immobilization of the motor complex does appear to require cholesterol, however. Both the motor complex and the cholesterol are found in detergent-resistant membrane domains that encompass a large fraction of the inner membrane complex surface. The observation that the myosin XIV motor complex of Toxoplasma is immobilized within this cholesterol-rich membrane likely extends to closely related pathogens like Plasmodium and possibly other eukaryotes.

Address correspondence to: Con J. Beckers (cbeckers{at}med.unc.edu)




This article has been cited by other articles:


Home page
 J. Lipid Res.Home page
C. Botte, N. Saidani, R. Mondragon, M. Mondragon, G. Isaac, E. Mui, R. McLeod, J.-F. Dubremetz, H. Vial, R. Welti, et al.
Subcellular localization and dynamics of a digalactolipid-like epitope in Toxoplasma gondii
J. Lipid Res., April 1, 2008; 49(4): 746 - 762.
[Abstract] [Full Text] [PDF]


Home Help [Feedback] [For Subscribers] [Archive] [Search] --
Copyright © 2007 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.