Molecular Biology of the Cell click for CBE Life Science Education Page

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


     

Originally published as MBC in Press, 10.1091/mbc.E05-02-0086 on June 27, 2005 Originally published as MBC in Press, 10.1091/mbc.E05-02-0086 on June 22, 2005

Vol. 16, Issue 9, 4013-4023, September 2005

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
E05-02-0086v1
E05-02-0086v2
16/9/4013    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 Schüler, H.
Right arrow Articles by Matuschewski, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Schüler, H.
Right arrow Articles by Matuschewski, K.

A Plasmodium Actin-depolymerizing Factor That Binds Exclusively to Actin Monomers

Herwig Schüler * {dagger}, Ann-Kristin Mueller {ddagger}, and Kai Matuschewski {ddagger}

* Department of Biochemistry and Biophysics, Stockholm University, 10691 Stockholm, Sweden; {ddagger} Department of Parasitology, Heidelberg University School of Medicine, 69120 Heidelberg, Germany

Submitted February 1, 2005; Revised June 3, 2005; Accepted June 9, 2005
Monitoring Editor: David Drubin

ADF/cofilins (AC) are essential F- and G-actin binding proteins that modulate microfilament turnover. The genome of Plasmodium falciparum, the parasite causing malaria, contains two members of the AC family. Interestingly, P. falciparum ADF1 lacks the F-actin binding residues of the AC consensus. Reverse genetics in the rodent malaria model system suggest that ADF1 performs vital functions during the pathogenic red blood cell stages, whereas ADF2 is not present in these stages. We show that recombinant PfADF1 interacts with monomeric actin but does not bind to actin polymers. Although other AC proteins inhibit nucleotide exchange on monomeric actin, the Plasmodium ortholog stimulates nucleotide exchange. Thus, PfADF1 differs in its biochemical properties from previously known AC proteins and seems to promote turnover exclusively by interaction with actin monomers. These findings provide important insights into the low cytosolic abundance and unique turnover characteristics of actin polymers in parasites of the phylum Apicomplexa.

This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E05–02–0086) on June 22, 2005.

Abbreviations used: AC, ADF/cofilin; ADF, actin-depolymerizing factor.

{dagger} Present address: Department of Medical Biochemistry and Biophysics, SGC, Karolinska Institutet, 17177 Stockholm, Sweden.

Address correspondence to: Herwig Schüler (herwig.schuler{at}mbb.ki.se).




This article has been cited by other articles:


Home page
 Proc. Natl. Acad. Sci. USAHome page
J. Bosch, C. A. Buscaglia, B. Krumm, B. P. Ingason, R. Lucas, C. Roach, T. Cardozo, V. Nussenzweig, and W. G. J. Hol
Aldolase provides an unusual binding site for thrombospondin-related anonymous protein in the invasion machinery of the malaria parasite
PNAS, April 24, 2007; 104(17): 7015 - 7020.
[Abstract] [Full Text] [PDF]


Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Copyright © 2005 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.